Research into the development of sustainable biomaterials is increasing in both interest and global importance due to the increasing demand for materials with decreased environmental impact. This research field utilises natural, renewable resources to develop innovative biomaterials. The development of sustainable biomaterials encompasses the entire material life cycle, from desirable traits, and environmental impact from production through to recycling or disposal. The main objective of this review is to provide a comprehensive definition of sustainable biomaterials and to give an overview of the use of natural proteins in biomaterial development. Proteins such as collagen, gelatin, keratin, and silk, are biocompatible, biodegradable, and may form materials with varying properties. Proteins, therefore, provide an intriguing source of biomaterials for numerous applications, including additive manufacturing, nanotechnology, and tissue engineering. We give an insight into current research and future directions in each of these areas, to expand knowledge on the capabilities of sustainably sourced proteins as advanced biomaterials.

Introduction

Sustainable biomaterials refer to the development of innovative biomaterials using building blocks obtained from natural, renewable resources. Due to their unique properties and abundance, proteins hold great promise as a green source of sustainable biomaterials for various applications. Additionally, alternative protein sources, such as recombinant proteins and peptides produced in different prokaryotic, eukaryotic, plant, and mammalian expression systems have also been explored to develop biomaterials with properties comparable to natural materials. This review provides an overview of sustainable biomaterials and the potential of protein biomaterials within this context. It covers aspects of protein sourcing and processing, along with recent trends and challenges, including alternative sustainable protein sources for biomaterial development, followed by examples of different protein-based biomaterials and their properties and applications.

Sustainable biomaterials

To understand what a sustainable biomaterial is, the entire life cycle of the material needs to be considered. This includes desirable and durable material characteristics, and the environmental impact of the entire production process, from the production through processing, degradation, recycling, or ultimate disposal at the end of its useful lifespan [1–3]. Based on these factors, a sustainable biomaterial can be classified as a material that is

  • Sourced from sustainably grown renewable resources.

  • Produced using environmentally friendly manufacturing processes.

  • Safe and non-hazardous for the environment.

  • Reused and recycled at the end of their intended use, such as feedstock for another process or via recycling or composting.

Other important aspects to consider for sustainability criteria are economic feasibility and societal benefits. For instance, in considering environmental impact, a sustainable biomaterial should fulfil a real need of society so that the ecological footprint of its production can be justified by its benefits to the society [1]. For this review, these social-economic issues will not be discussed in detail, but it is important to highlight that their integration is vital as shown in Figure 1. This will improve the sustainability outcomes of the new generation of biomaterials and to contribute to achieving the United Nation's sustainable development goals for 2030 [4]

Sustainability criteria for materials, from environment related factors, to economy-related factors and social contexts; these concepts are interconnected. Adapted with permission from [1]. Copyright 2016 by Taylor and Francis.

Figure 1.
Sustainability criteria for materials, from environment related factors, to economy-related factors and social contexts; these concepts are interconnected. Adapted with permission from [1]. Copyright 2016 by Taylor and Francis.
Figure 1.
Sustainability criteria for materials, from environment related factors, to economy-related factors and social contexts; these concepts are interconnected. Adapted with permission from [1]. Copyright 2016 by Taylor and Francis.

Based on the sustainability criteria above, protein-based biomaterials can be classified as sustainable materials due to their abundance and renewability [5,6], and ease of modification and chemical heterogeneity, offered by the variable amino acid composition of proteins obtained from different sources [7,8]. Furthermore, as most proteins are water-soluble, the entire production process can be conducted with limited use of organic solvents [9]. Protein biomaterials also offer exceptional physical properties, with the enormous benefit that they are intrinsically biodegradable making them a part of a circular economy of source materials [10]. There is, therefore, currently much interest in both developing new protein-based materials and sourcing proteins for these materials in different ways [6,11–13].

Protein sourcing and processing for sustainable protein biomaterials

A great diversity in protein-based biomaterials with various applications in different fields exists, however, to meet sustainability criteria it is important that the protein source is renewable and the entire production process including biomaterial development is low energy and eco-friendly [14]. In this context, the use of proteins from agro-wastes or food side streams provides a sustainable, economical, and reliable feedstock [15]. Similarly, the direct utilisation of several fibrous proteins, such as keratin, silk, resilin, and elastin into biodegradable hierarchical biomaterials also offers sustainable methods towards developing green biomaterials [10,16].

In the last few years, several proteins have emerged as novel sustainable protein biomaterials due to their easy availability, simple production methods and biocompatibility, for example, soy [17,18], milk proteins — casein [19,20], whey [21,22], keratin [23], collagen [24,25], haemoglobin [26], silk [27,28]. However, there are some drawbacks to harvesting these proteins from natural sources, these include batch-to-batch variation, impurities, the quantity available, the risk for disease transmission, and potentially fast biodegradation [29,30]. To mitigate these issues, biotechnological solutions have been developed to produce larger amounts of protein with more consistent quality and greater biological safety [8,11,31,32].

Alternative protein sourcing technologies

Recombinant technology provides an alternative method to produce proteins that are not naturally available in abundant quantities, as well as to modify the properties of these recombinant proteins, for example, by adding other bioactive molecules, growth factors, cell-binding domains, or other direct chemical modifications [33,34]. There are many successful reports of using of recombinant proteins to develop protein-based biomaterials; however, issues relating to low yield and scalability hinder their widespread commercial adoption [35–37]. However, with increasing interest in cellular agriculture, these limitations may soon be overcome. Table 1 provides a non-exhaustive list of different proteins used to develop biomaterials, along with their commonly used source and alternative sources available. For a more in-depth discussion on the recombinant production of proteins towards sustainable biomaterials, the authors refer readers to detailed reviews on this subject [54–57]. In the following sections: additive manufacturing, nanotechnology and tissue engineering, a range of applications of protein-based biomaterials will be discussed.

Table 1.
Proteins used to develop biomaterials, along with their commonly used source and alternative sources available
ProteinTraditional sourceAlternative source
Keratin Wool fibres, horns, nails and feathers from butchery [23,38–40]. Biomimetic recombinant hagfish thread keratin [41], recombinant human hair keratins K31 and K81 [42,43]. 
Collagen Collagen type I: Mammalian skin, and tendon tissues (porcine, bovine and ovine in origin); collagen type II: bovine, porcine and chicken cartilaginous tissues [24,44]; marine collagen [45–47]. Recombinant human collagen in different prokaryotic, eukaryotic, plant and mammalian expression systems [35,48]. 
Silk Domestic silkworms: Bombyx mori (B. mori); wild silkworms: Antheraea pernyi and Samia cynthia ricini; Spiders: Nephila clavipes and Araneus diadematus [12]. Recombinant silk proteins in different host systems [11,29,49]. 
Elastin and resilin Animal-derived tropoelastin, recombinant production [16]. Recombinant elastin-like recombinamers (ELRs) [11,36,39]; Recombinant resilin-like peptides (RLPs)/protein [50–52] or protein [53]. 
ProteinTraditional sourceAlternative source
Keratin Wool fibres, horns, nails and feathers from butchery [23,38–40]. Biomimetic recombinant hagfish thread keratin [41], recombinant human hair keratins K31 and K81 [42,43]. 
Collagen Collagen type I: Mammalian skin, and tendon tissues (porcine, bovine and ovine in origin); collagen type II: bovine, porcine and chicken cartilaginous tissues [24,44]; marine collagen [45–47]. Recombinant human collagen in different prokaryotic, eukaryotic, plant and mammalian expression systems [35,48]. 
Silk Domestic silkworms: Bombyx mori (B. mori); wild silkworms: Antheraea pernyi and Samia cynthia ricini; Spiders: Nephila clavipes and Araneus diadematus [12]. Recombinant silk proteins in different host systems [11,29,49]. 
Elastin and resilin Animal-derived tropoelastin, recombinant production [16]. Recombinant elastin-like recombinamers (ELRs) [11,36,39]; Recombinant resilin-like peptides (RLPs)/protein [50–52] or protein [53]. 

Additive manufacturing

Additive manufacturing, also called three-dimensional (3D) printing, has been recognised as a more sustainable manufacturing method compared with traditional manufacturing, allowing for flexible designs and prints of complex structures [58]. The advantageous energy and environmental impacts of additive manufacturing is thoroughly reviewed in [59]. Current 3D printing research explores the integration of natural biopolymer resources such as proteins, polysaccharides and other green materials as the main components of novel bio- and biomaterial inks [60].

Groll et al. [61] propose a general definition of bio-inks that clarifies its distinction from biomaterial inks. They define a bio-ink as ‘a formulation of cells suitable for processing by an automated biofabrication technology that may also contain biologically active components and biomaterials’ which defers from biomaterial inks which do not contain cells during processing — cells can be post-seeded onto the end-biomaterial product depending on the applications. The development of such inks is well reviewed in many recent publications [61–67].

Collagen, gelatin, silk fibroin, and keratin are examples of proteins that are employed in the formulation of inks for a variety of applications such as films, hydrogels and scaffolds for tissue, bone and cartilage engineering [57,62,68]. Features such as biocompatibility and biodegradability along with the ease of availability, low processing cost, and varying mechanical properties make proteins ideal components of biomaterial inks [67]. Protein-based inks along with the additive manufacturing process offer an opportunity to address the niche issue of tissue engineering — e.g. fabrication of suitable scaffolds with biocompatibility and functional mechanical properties. The layer-by-layer assembly provides a complex 3D construct with robust and highly ordered structures for cell proliferation and differentiation [69]. Major classes of printing processes where proteins are used in are lithography and material extrusion [70,71]. Choi et al. [57] review the advances in protein-based materials and the following is a snapshot of how proteins are integrated within bio- and biomaterial inks.

Protein-based inks

Collagen materials are abundant throughout biomaterials research, and Marques et al. [72] present a comprehensive review on the state-of-the-art of the development of collagen-based inks for tissue engineering applications. Various methods to improve the printability of collagen by either combining collagen with synthetic polymers or by directly printing collagen into a sacrificial support gel have been established [73,74]. For example, a homogeneous hybrid collagen/nano-hydroxyapetite formulation has been developed to mimic the composition of bone tissue with suitable properties for 3D printing via material extrusion processes [73]. Gelatin, formed from the partial hydrolysis of collagen, is also frequently used in the biomaterial industry. Modifying gelatin with methacrylic anhydride (MA) to obtain gelatin-methacryloyl (GelMA) is the most common modification of the protein to render it photosensitive, and protocols are well established throughout the literature [75–77]. Compared with the more solid collagen/nano-hydroxyapetite ink that is extruded, GelMA is a moderately viscous liquid ink that solidifies upon exposure to ultraviolet light. GelMA is used in various applications such as micropatterning, fluidic systems, 3D scaffolds and bioprinting [75,78–81]. GelMA is also added to synthetic polymer mixtures for improved mechanical properties. One example is the addition of GelMA to methacrylated poly(vinyl alcohol) (PVA-MA) with tris-bipyridyl ruthenium hexahydrate and sodium persulfate (Ru/SPS) as the photoinitiator [82]. This study describes the development and characterisation of a bio-resin containing PVA-MA/Gel-MA/Ru/SPS which demonstrated compatibility with commercial 3D printing fabrication using a vat photopolymerisation process [82].

Silk fibroin-based scaffolds have also been fabricated using 3D printing processes. Mixtures of silk with several other biopolymers such as gelatin and alginate were developed to achieve the rheological requirements suitable for 3D extrusion printing [83]. The methacrylation of silk fibroin favours the 3D printing of silk via lithography techniques. One recent study from Kim et al. [65] follows a similar approach to GelMA production, where silk fibroin is methacrylated using glycidyl methacrylate to print scaffolds via digital light processing 3D printing. They also demonstrated the cytocompatibility of the Sil-MA hydrogels by successfully encapsulating NIH/3T3 fibroblast within the hydrogels [65]. And, more recently, Grigsby et al. [38] published a paper on the fabrication of keratin-lignin inks for 3D printing using green chemistry principles. Keratin is one such protein, which can be extracted from wool, feathers, and other biological waste products from the meat industry, a sustainable, economical, and reliable feedstock [84–86]. In this case, keratin is extracted as an intermediate filament protein powder by treating wool with copper sulfate and sodium sulphite following a standard oxidative sufitolysis procedure. Keratin-lignin copolymer materials show promising capability for processing as filaments in material extrusion printing (more specifically, fused deposition melting, FDM, printing) and for deposition as hydrogels using 3D paste printing [38].

The literature demonstrates a wide range of successful research outcomes for the use of natural proteins within the additive manufacturing sector. The flexibility in transforming proteins into different sorts of inks, from viscous photosensitive liquids to hard melting filaments, allows for the fabrication of a large variety of biomaterials. The layer-by-layer construction of these biomaterials offer a particular advantage for the fine detail of the constructs and specific seeding of cells which may be difficult to obtain from traditional manufacturing such as moulding. Overall, the combined use of protein-based inks and 3D printing technologies offer an opportunity for an improved and more sustainable production of biomaterials.

Building blocks for nanotechnology

Nanotechnology and the creation of new nanostructures offer many exciting opportunities for new products and materials. However, there are concerns regarding the environmental impact of both the processes to produce nanostructures and the nanostructures themselves which have led to the adoption of green chemistry techniques for nanostructure synthesis. Proteins are one of nature's nanostructures, self-assembling from amino acids into a range of intriguing nanoscale structures, such as nanofibrils and nanocages. Protein nanostructures are of great interest as biomaterials, due to their increased biocompatibility when compared with more traditional nanomaterials, e.g. metallic nanoparticles [87]. They have shown the potential to be used in extensive applications, such as biosensors, catalysts, and drug delivery systems [88–91]. Here, we will provide some key examples of protein nanostructures, specifically protein nanofibrils, nanoparticles, and nanogels. For further reading on the use of protein nanotechnology, including the use of recombinant technology to produce designed protein nanostructures, we refer the readers to [92].

Protein nanofibrils

Beta-sheet rich protein nanofibrils, or amyloid-like fibrils, have many desirable properties for use in biomaterial fabrication. When compared with other natural fibrous structures, like collagen fibrils, amyloid-like fibrils have been found to have distinct advantages in regards to tensile strength, stability, and deformation resistance, with many different proteins able to adopt this structure [93]. For instance, whey proteins (a by-product of cheese-making) can form amyloid-like protein nanofibrils, at low pH (≤2), low ionic strength, and high temperature (≥80°C), and the resulting structures are observed to be highly stable under various environmental [94]. These fibrils alone can make different forms of materials, such as hydrogels (via the addition of divalent cation salts), microcapsules (via a layer-by-layer self-assembly technique), and coatings (via adsorption) [95–97].

With the further addition of other biomolecules, such as nanoparticles, enzymes, and bioactive substances, whey protein nanofibrils (WPNFs) can display other functions and forms. For example, WPNFs can induce the formation of ZrO2 nanoparticles from Zr ions, and a fluoride ion-removal filter membrane can be produced using these nanoparticle-carrying fibrils and a carbon matrix via vacuum-filtration, which exhibited excellent selectivity for F-against various competitive ions [98]. Moreover, WPNFs may contribute interesting features to a new composite material. Zhang et al. [99] demonstrated an emulsion microstructure formed with WPNFs, oil and D-limonene that showed excellent antioxidant and antibacterial activity and functions as a carrier system for lipophilic bioactive molecules. When composited with graphene, the presence of ß-lactoglobulin (from whey protein isolate) fibrils endowed unique periodic troughs and crests to the topography of the composite film without the need of lithographic techniques or etching, enabling this film to provide an efficient support for cellular polarisation and differentiation [100]. Later, the same fibrils were mixed with silica precursor tetraethyl orthosilicate, and fibril–silica core–shell nanostructures with stiffness up to beyond ∼20 GPa (similar Young's moduli as many metal alloys and inorganic materials) were made [101]. In fact, many proteins can be reconstructed into this particular structure under certain conditions, including many sustainably sourced proteins, such as casein, haemoglobin (from meat industry waste), crystallins (from fish industry waste), and soy proteins [94,102–105]. However, compared with whey protein fibrils, less research has focused on these alternative nanofibril sources as biomaterials. Future biomaterials design should take advantage of the flexible choice of protein fibrils according to their specific intended application.

Nanoparticles (NPs)

NPs generally refer to materials with sizes ranging from 1 to 100 nm [106]. Collagen-based ZnO NPs have been successfully fabricated into hexagonal wurtzite structure with particle sizes ranging between 20 and 50 nm by a bioinspired synthesis method [107]. These NPs not only exhibited antibacterial, antibiofilm, and anti-cancer (against human liver (HepG2) cells) effects, but also showed no ecotoxicity [107]. Another method to produce nanoparticles using sustainably sourced proteins was demonstrated by Perotto and co-workers. They extracted keratin from wool and formed keratin particles by water-solving the auxiliary structure [40]. The tunable mucoadhesive properties of these particles can dramatically improve drug delivery efficiency [40].

Bioactive glass (bioglass) has been developed to supplement damaged bone tissue in the physiological environment. Reiter and colleagues coated bioactive glass (SiO2–CaO–P2O5 system) nanoparticles with gelatin by using a foam replication technique [108]. With the addition of gelatin, the scaffold's strength and toughness were significantly increased. Additionally, the cross-linked gelatin network endowed the bioglass with the ability to sustained release the bioactive molecule icariin for bone defect repair [108].

Other nanostructures

Different from typical hydrogels, nanohydrogels/nanogels (NGs) are nano-scaled cross-linked networks showing both features of a hydrogel and nanoparticle [109]. Kang and colleagues used fish gelatin to form NGs, which can contain and release doxorubicin by pH regulation, through water-in-oil emulsion and photopolymerization [110]. This nano-sized drug delivery system shows many advantages, including enhanced permeability, retention (EPR) effect, and improved drug stability. Nanonets commonly compromise interlinked ultrathin fibres which are stacked layer-by-layer in the final porous membranes [111]. Wang et al. [111,112] demonstrated spider-web-like nanonets (∼35 nm) structures formed by gelatin through electrospinning and a recent paper based on their work designed more complicated systems to improve the magnetic properties of CoFe2O4 nanoparticles.

In addition to the known advantages of nanoscale structures, in the examples detailed, protein nanostructures are favourable due to their ease of synthesis, and often improved functional properties, particularly biocompatibility.

Tissue engineering

The application of biomaterials to tissue engineering represents a logical progression of protein-based technology. The tunable physical, biological, and chemical functionalities of proteins provide a toolbox from which materials for almost any tissue engineering application can be designed. Here, we have very crudely delineated our examples into drug delivery vehicles or structural scaffolds. However, these are generalised terms under which a variety of subclasses such as medical devices, biosensors, and tissue mimics can be defined.

Drug delivery vehicles

Much like the nanostructures discussed earlier, protein biomaterials can be utilised for drug delivery. Bioengineered silk offers a divergence from traditional Bombyx mori reliant production and allows for functionalisation for targeted applications. A prime example is the production of silk spidroin proteins with the integration of the H2.1 or DOX peptide [113]. H2.1 selectively binds to Human Epidermal growth factor Receptor 2 (HER2), a receptor expressed by some aggressive forms of breast cancer, while DOX confers an affinity for the cancer drug doxorubicin. Composite silk spidroin spheres, therefore, offer a cancer drug delivery system which is targeted, controlled and biodegradable [113], potentially enhancing patient outcomes and reducing overall medical costs. Bioengineered silk is more sustainable than traditional silk harvesting, with recombinant systems being designed in prokaryotic and eukaryotic models including Escherichia coli, rice, tobacco, and kidney cells [114]. If green production and processing of silk fibroin and spidroin become commonplace, the use of silk biomaterials for drug delivery could be utilised for consumer products. For example, improving insulin delivery patient compliance is of particular interest in translational medicine. Subcutaneous injections of silk fibroin hydrogels with encapsulated insulin enables sustained release of insulin for blood glucose control in diabetic rats [115]. Similarly, silk fibroin microneedle patches offer a sustained release of insulin via transdermal delivery, removing the need for traditional injections which require high patient compliance and careful management of injection sites to protect tissue integrity [116].

Collagen biomaterials also exhibit potential in drug delivery, having natural biocompatibility as an extracellular matrix protein [44]. Collagen extracted from turkey tendon, a waste product from the poultry industry, can be formed into sponge scaffolds following gelation, cross-linking and freeze-drying, with prilocaine hydrochloride loaded as a model drug [44]. Gelatin, formed from the partial hydrolysis of collagen, can similarly form hydrogels for drug delivery applications. Hydrogels formulated from gelatin and hyaluronic acid produce an injectable substrate which directly delivers anti-inflammatory drugs to knee joints for the treatment of osteoarthrosis [117]. Gelatin/salecan (a bacterial polysaccharide) composites loaded with vancomycin, an antibiotic traditionally given intravenously, showed sustained release over several days and positive preliminary results for eliminating E. coli and Staphylococcus aureus populations in co-culture [118]. Delivery vehicles enhance the longevity, targeting, and therapeutic efficacy of pharmaceuticals, making biodegradable protein-based scaffolds a viable strategy for improving patient outcomes.

Structural scaffolds

Protein scaffolds are of particular interest in the tissue engineering field for their biocompatibility, mechanical properties, and biodegradability. Keratin is one such protein, and its ability to be formed into a rigid, yet porous, scaffold makes it well suited for bone matrix engineering. Wool keratin scaffolds demonstrate chemical and physical stability and can be manufactured by both liquid casting [119] and electrospinning with polymers [120]. Both methods produce porous scaffolds supporting cell migration, adhesion and expression of osteogenic markers. The biocompatibility of keratin scaffolds is such that bone grafts have been shown not to elicit innate or antibody-mediated immune responses in ovine models, a critical feature for any scaffold intended for implantation [121].

Elastin is an extracellular matrix protein commonly sourced from bovine neck ligaments. As the name suggests, elastin is a protein which confers elasticity and resilience to tissue. The inclusion of elastin cross-linking into tendon-derived collagen scaffolds designed for vascular grafts both improves the mechanical properties and increases endothelial and smooth muscle cell viability [122]. Hydrogels and films produced from genetically engineered elastin expressed in E. coli have been formulated to specifically promote endothelial cell adhesion [39], a property which if combined with the aforementioned vascular grafts could improve vascular tissue engineering technology. Elastin has also been shown to improve the mechanical properties of other protein-based materials, such as gelatin and cellulose acetate scaffolds for skin tissue engineering where the ability of the graft to flex with surrounding healthy tissue is paramount [123]. Resilin, much like elastin, is a protein with high elasticity and resilience to repetitive mechanical loading [50]. Although natively found in insects, resilin and modified resilin-like proteins are commonly produced by expression in bacterial culture [50–52]. Resilin-like proteins can be designed to include function-specific peptides to mimic tissue and promote differentiation of cells [50]. Structurally, engineered resilin can form conductive, elastic and adhesive hydrogels suitable as biosensors [52], or be combined with silk spidroin carboxyl-terminal domains to increase the gelation temperature range of reversible hydrogels [51]. Whether a product uses elastin or resilin, derived from industry waste material or modified and recombinantly produced, will depend on specific material requirements. However, both offer improved properties for tissue mimics in which resilience is necessary for successful integration.

Recombinant peptides based on human type I collagen can be produced by yeast fermentation [124]. Following methacrylation and formation into hydrogels (as detailed in Protein-based inks section), it displays comparable properties to hydrogels formed from animal-derived methacrylated gelatins to mimic extracellular matrix and support encapsulated stem cells [124]. Bacterial fermentation is also being utilised, with human-like collagen expressed in E. coli BL21 being used in conjunction with the polysaccharide chitosan to produce hydrogels which accelerate the closure of full-thickness skin defects [125]. However, when vast natural sources of collagen are available, recombinant protein production is perhaps less renewable. Chicken skin collagen electrospun with elastin displays similar promise for the development of engineered skin substitutes [126]. Products derived from marine environments, so-called ‘blue biomaterials’, are also on the rise. Collagen extracted from eel [45], codfish [46], and tilapia [47] skin all exhibit biocompatibility and structural properties comparable with traditional, mammalian collagen sources.

In this paper, we have covered a non-exhaustive list exemplifying just some of the potential applications that materials formed from sustainably sourced proteins have in the biomaterials field, as illustrated in Figure 2. Despite great opportunity, there remain multifaced challenges in designing fully sustainable and efficient protein-based biomaterials. For example, batch-to-batch variation, and sometimes complicated paths of translation to clinical settings. We expect future work to address these challenges, as well as uncover new novel protein sources and material fabrication techniques.

Illustrative representation of renewable protein sources and their potential application in the biomaterials field.

Figure 2.
Illustrative representation of renewable protein sources and their potential application in the biomaterials field.
Figure 2.
Illustrative representation of renewable protein sources and their potential application in the biomaterials field.

Perspectives

  • Fabricating biomaterials from natural polymers such as proteins, offer various advantages such as increased biocompatibility, biodegradability, cytocompatibility, and flexible construct designs. This field is leading in the development of innovative materials and more sustainable production of biomaterials by the efficient harnessing of natural resources.

  • Currently, the development of protein-based biomaterials is expanding our knowledge on the importance of using available natural resources to improve the negative environmental impacts of some traditional materials and to increase the valorisation of these natural resources.

  • As large scale fermentor technology improves, cellular agriculture is likely to become a more common source of producing protein biomaterials.

Competing Interests

The authors declare that there are no competing interests associated with the manuscript.

Funding

This work was supported by the Science for Technological Innovation National Science Challenge and The MacDiarmid Institute for Advanced Materials and Nanotechnology.

Open Access

Open access for this article was enabled by the participation of University of Auckland in an all-inclusive Read & Publish pilot with Portland Press and the Biochemical Society under a transformative agreement with CAUL.

Author Contribution

All authors reviewed the literature, selected and organised content, and wrote major text sections. J.G. prepared the figures. L.J.D. and H.A. critically revised the manuscript.

Abbreviations

     
  • GelMA

    gelatin-methacryloyl

  •  
  • NGs

    nanogels

  •  
  • NPs

    nanoparticles

  •  
  • WPNFs

    whey protein nanofibrils

References

References
1
Lefèvre
,
T.
and
Auger
,
M.
(
2016
)
Spider silk inspired materials and sustainability: perspective
.
Mater. Technol.
31
,
384
399
2
Biswal
,
T.
,
BadJena
,
S.K.
and
Pradhan
,
D.
(
2020
)
Sustainable biomaterials and their applications: a short review
.
Mater. Today Proc.
30
,
274
282
3
Zhu
,
Y.
,
Romain
,
C.
and
Williams
,
C.K.
(
2016
)
Sustainable polymers from renewable resources
.
Nature
540
,
354
362
4
United Nations Development Programme (2015) Evaluation of the Role of {UNDP} in Supporting National Achievement of the Millennium Development Goals. United Nations, Thematic Development Reports
5
Bonduelle
,
C.
(
2018
)
Secondary structures of synthetic polypeptide polymers
.
Polym. Chem.
9
,
1517
1529
6
DeFrates
,
K.
,
Moore
,
R.
,
Borgesi
,
J.
,
Lin
,
G.
,
Mulderig
,
T.
,
Beachley
,
V.
et al (
2018
)
Protein-based fiber materials in medicine: a review
.
Nanomaterials
8
,
457
7
Shadish
,
J.A.
and
DeForest
,
C.A.
(
2020
)
Site-selective protein modification: from functionalized proteins to functional biomaterials
.
Matter
2
,
50
77
8
Wang
,
Y.
,
Katyal
,
P.
and
Montclare
,
J.K.
(
2019
)
Protein-engineered functional materials
.
Adv. Healthc. Mater.
8
,
1801374
9
Capezza
,
A.J.
,
Newson
,
W.R.
,
Olsson
,
R.T.
,
Hedenqvist
,
M.S.
and
Johansson
,
E.
(
2019
)
Advances in the use of protein-based materials: toward sustainable naturally sourced absorbent materials
.
ACS Sustain. Chem. Eng.
7
,
4532
4547
10
Abascal
,
N.C.
and
Regan
,
L.
(
2018
)
The past, present and future of protein-based materials
.
Open Biol.
8
,
180113
11
Chambre
,
L.
,
Martín-Moldes
,
Z.
,
Parker
,
R.N.
and
Kaplan
,
D.L.
(
2020
)
Bioengineered elastin- and silk-biomaterials for drug and gene delivery
.
Adv. Drug Deliv. Rev.
160
,
186
198
12
Nguyen
,
T.P.
,
Nguyen
,
Q.V.
,
Nguyen
,
V.-H.
,
Le
,
T.-H.
,
Huynh
,
V.Q.N.
,
Vo
,
D.-V.N.
et al (
2019
)
Silk fibroin-based biomaterials for biomedical applications: a review
.
Polymers (Basel)
11
,
1933
13
Numata
,
K.
(
2020
)
How to define and study structural proteins as biopolymer materials
.
Polym. J.
52
,
1043
1056
14
Zuin
,
V.G.
and
Ramin
,
L.Z.
(
2018
)
Green and sustainable separation of natural products from agro-industrial waste: challenges, potentialities, and perspectives on emerging approaches
.
Top. Curr. Chem. Collect.
376
,
229
282
15
Sozer
,
N.
,
Nordlund
,
E.
,
Ercili-Cura
,
D.
and
Poutanen
,
K.
(
2017
)
Cereal side-streams as alternative protein sources
.
Cereal Foods World
62
,
132
137
16
Costa
,
F.
,
Silva
,
R.
and
Boccaccini
,
A.R.
(
2017
)
Fibrous protein-based biomaterials (silk, keratin, elastin, and resilin proteins) for tissue regeneration and repair
.
Pept. Proteins Biomater. Tissue Regen. Repair
175
204
17
Tian
,
H.
,
Guo
,
G.
,
Fu
,
X.
,
Yao
,
Y.
,
Yuan
,
L.
and
Xiang
,
A.
(
2018
)
Fabrication, properties and applications of soy-protein-based materials: a review
.
Int. J. Biol. Macromol.
120
,
475
490
18
Tansaz
,
S.
and
Boccaccini
,
A.R.
(
2015
)
Biomedical applications of soy protein: a brief overview
.
J. Biomed. Mater. Res. A
104
,
553
569
19
Nascimento
,
L.G.L.
,
Casanova
,
F.
,
Silva
,
N.F.N.
,
de Carvalho Teixeira
,
A.V.N.
and
de Carvalho
,
A.F.
(
2020
)
Casein-based hydrogels: a mini-review
.
Food Chem.
314
,
126063
20
Selvaraj
,
S.
,
Thangam
,
R.
and
Fathima
,
N.N.
(
2018
)
Electrospinning of casein nanofibers with silver nanoparticles for potential biomedical applications
.
Int. J. Biol. Macromol.
120
,
1674
1681
21
Farooq
,
M.A.
,
Aquib
,
M.
,
Ghayas
,
S.
,
Bushra
,
R.
,
Khan
,
D.H.
,
Parveen
,
A.
et al (
2019
)
Whey protein: a functional and promising material for drug delivery systems recent developments and future prospects
.
Polym. Adv. Technol.
30
,
2183
2191
22
Dziadek
,
M.
,
Douglas
,
T.E.L.
,
Dziadek
,
K.
,
Zagrajczuk
,
B.
,
Serafim
,
A.
,
Stancu
,
I.-C.
et al (
2020
)
Novel whey protein isolate-based highly porous scaffolds modified with therapeutic ion-releasing bioactive glasses
.
Mater. Lett.
261
,
127115
23
Shavandi
,
A.
,
Silva
,
T.H.
,
Bekhit
,
A.A.
and
Bekhit
,
A.E.-D.A.
(
2017
)
Keratin: dissolution, extraction and biomedical application
.
Biomater. Sci.
5
,
1699
1735
24
Sorushanova
,
A.
,
Delgado
,
L.M.
,
Wu
,
Z.
,
Shologu
,
N.
,
Kshirsagar
,
A.
,
Raghunath
,
R.
et al (
2018
)
The collagen suprafamily: from biosynthesis to advanced biomaterial development
.
Adv. Mater.
31
,
1801651
25
Akturk
,
O.
,
Kismet
,
K.
,
Yasti
,
A.C.
,
Kuru
,
S.
,
Duymus
,
M.E.
,
Kaya
,
F.
et al (
2016
)
Collagen/gold nanoparticle nanocomposites: a potential skin wound healing biomaterial
.
J. Biomater. Appl.
31
,
283
301
26
Paciello
,
A.
,
Amalfitano
,
G.
,
Garziano
,
A.
,
Urciuolo
,
F.
and
Netti
,
P.A.
(
2016
)
Hemoglobin-conjugated gelatin microsphere as a smart oxygen releasing biomaterial
.
Adv. Healthc. Mater.
5
,
2655
2666
27
Kadakia
,
P.U.
,
Kalaf
,
E.A.G.
,
Dunn
,
A.J.
,
Shornick
,
L.P.
and
Sell
,
S.A.
(
2017
)
Comparison of silk fibroin electrospun scaffolds with poloxamer and honey additives for burn wound applications
.
J. Bioact. Compat. Polym.
33
,
79
94
28
Janani
,
G.
,
Kumar
,
M.
,
Chouhan
,
D.
,
Moses
,
J.C.
,
Gangrade
,
A.
,
Bhattacharjee
,
S.
et al (
2019
)
Insight into silk-based biomaterials: from physicochemical attributes to recent biomedical applications
.
ACS Appl. Bio Mater.
2
,
5460
5491
29
Aigner
,
T.B.
,
DeSimone
,
E.
and
Scheibel
,
T.
(
2018
)
Biomedical applications of recombinant silk-based materials
.
Adv. Mater.
30
,
1704636
30
Gauza-Włodarczyk
,
M.
,
Kubisz
,
L.
,
Mielcarek
,
S.
and
Włodarczyk
,
D.
(
2017
)
Comparison of thermal properties of fish collagen and bovine collagen in the temperature range 298-670K
.
Mater. Sci. Eng. C
80
,
468
471
31
Huang
,
W.
,
Ling
,
S.
,
Li
,
C.
,
Omenetto
,
F.G.
and
Kaplan
,
D.L.
(
2018
)
Silkworm silk-based materials and devices generated using bio-nanotechnology
.
Chem. Soc. Rev.
47
,
6486
6504
32
Werten
,
M.W.T.
,
Eggink
,
G.
,
Stuart
,
M.A.C.
and
de Wolf
,
F.A.
(
2019
)
Production of protein-based polymers in Pichia pastoris
.
Biotechnol. Adv.
37
,
642
666
33
Que
,
R.A.
,
Arulmoli
,
J.
,
Da
,
S.N.
,
Flanagan
,
L.A.
and
Wang
,
S.-W.
(
2018
)
Recombinant collagen scaffolds as substrates for human neural stem/progenitor cells
.
J. Biomed. Mater. Res. A
106
,
1363
1372
34
Ibáñez-Fonseca
,
A.
,
Flora
,
T.
,
Acosta
,
S.
and
Rodríguez-Cabello
,
J.C.
(
2019
)
Trends in the design and use of elastin-like recombinamers as biomaterials
.
Matrix Biol.
84
,
111
126
35
Davison-Kotler
,
E.
,
Marshall
,
W.S.
and
García-Gareta
,
E.
(
2019
)
Sources of collagen for biomaterials in skin wound healing
.
Bioengineering
6
,
56
36
Acosta
,
S.
,
Quintanilla-Sierra
,
L.
,
Mbundi
,
L.
,
Reboto
,
V.
and
Rodríguez-Cabello
,
J.C.
(
2020
)
Elastin-like recombinamers: deconstructing and recapitulating the functionality of extracellular matrix proteins using recombinant protein polymers
.
Adv. Funct. Mater.
30
,
1909050
37
Borkner
,
C.B.
,
Wohlrab
,
S.
,
Möller
,
E.
,
Lang
,
G.
and
Scheibel
,
T.
(
2016
)
Surface modification of polymeric biomaterials using recombinant spider silk proteins
.
ACS Biomater. Sci. Eng.
3
,
767
775
38
Grigsby
,
W.J.
,
Scott
,
S.M.
,
Plowman-Holmes
,
M.I.
,
Middlewood
,
P.G.
and
Recabar
,
K.
(
2020
)
Combination and processing keratin with lignin as biocomposite materials for additive manufacturing technology
.
Acta Biomater.
104
,
95
103
39
Girotti
,
A.
,
Gonzalez-Valdivieso
,
J.
,
Santos
,
M.
,
Martin
,
L.
and
Arias
,
F.J.
(
2020
)
Functional characterization of an enzymatically degradable multi-bioactive elastin-like recombinamer
.
Int. J. Biol. Macromol.
164
,
1640
1648
40
Perotto
,
G.
,
Sandri
,
G.
,
Pignatelli
,
C.
,
Milanesi
,
G.
and
Athanassiou
,
A.
(
2019
)
Water-based synthesis of keratin micro- and nanoparticles with tunable mucoadhesive properties for drug delivery
.
J. Mater. Chem. B
7
,
4385
4392
41
Fu
,
J.
,
Guerette
,
P.A.
and
Miserez
,
A.
(
2015
)
Self-assembly of recombinant hagfish thread keratins amenable to a strain-induced α-helix to β-sheet transition
.
Biomacromolecules
16
,
2327
2339
42
Parker
,
R.N.
,
Roth
,
K.L.
,
Kim
,
C.
,
McCord
,
J.P.
,
Van Dyke
,
M.E.
and
Grove
,
T.Z.
(
2017
)
Homo- and heteropolymer self-assembly of recombinant trichocytic keratins
.
Biopolymers
107
,
e23037
43
Parker
,
R.N.
,
Trent
,
A.
,
Stefaniak
,
K.L.R.
,
Van Dyke
,
M.E.
and
Grove
,
T.Z.
(
2020
)
A comparative study of materials assembled from recombinant K31 and K81 and extracted human hair keratins
.
Biomed. Mater.
15
,
065006
44
Grønlien
,
K.G.
,
Pedersen
,
M.E.
,
Sanden
,
K.W.
,
Høst
,
V.
,
Karlsen
,
J.
and
Tønnesen
,
H.H.
(
2019
)
Collagen from Turkey (Meleagris gallopavo) tendon: a promising sustainable biomaterial for pharmaceutical use
.
Sustain. Chem. Pharm.
13
,
100166
45
Govindharaj
,
M.
,
Roopavath
,
U.K.
and
Rath
,
S.N.
(
2019
)
Valorization of discarded Marine Eel fish skin for collagen extraction as a 3D printable blue biomaterial for tissue engineering
.
J. Clean Prod.
230
,
412
419
46
Carvalho
,
A.
,
Marques
,
A.
,
Silva
,
T.
and
Reis
,
R.
(
2018
)
Evaluation of the potential of collagen from codfish skin as a biomaterial for biomedical applications
.
Mar. Drugs
16
,
495
47
Li
,
D.
,
Gao
,
Y.
,
Wang
,
Y.
,
Yang
,
X.
,
He
,
C.
,
Zhu
,
M.
et al (
2019
)
Evaluation of biocompatibility and immunogenicity of micro/nanofiber materials based on tilapia skin collagen
.
J. Biomater. Appl.
33
,
1118
1127
48
Campuzano
,
S.
and
Pelling
,
A.E.
(
2019
)
Scaffolds for 3D cell culture and cellular agriculture applications derived from non-animal sources
.
Front. Sustain. Food Syst.
3
,
38
49
Peng
,
Q.
,
Zhang
,
Y.
,
Lu
,
L.
,
Shao
,
H.
,
Qin
,
K.
,
Hu
,
X.
et al (
2016
)
Recombinant spider silk from aqueous solutions via a bio-inspired microfluidic chip
.
Sci. Rep.
6
,
1
12
50
Li
,
L.
,
Stiadle
,
J.M.
,
Levendoski
,
E.E.
,
Lau
,
H.K.
,
Thibeault
,
S.L.
and
Kiick
,
K.L.
(
2018
)
Biocompatibility of injectable resilin-based hydrogels
.
J. Biomed. Mater. Res. A
106
,
2229
2242
51
Luo
,
F.
,
Qian
,
Z.-G.
and
Xia
,
X.-X.
(
2018
)
Responsive protein hydrogels assembled from spider silk carboxyl-terminal domain and resilin copolymers
.
Polymers (Basel)
10
,
915
52
Hu
,
X.
,
Xia
,
X.-X.
,
Huang
,
S.-C.
and
Qian
,
Z.-G.
(
2019
)
Development of adhesive and conductive resilin-based hydrogels for wearable sensors
.
Biomacromolecules
20
,
3283
3293
53
Su
,
R.S.C.
,
Gill
,
E.E.
,
Kim
,
Y.
and
Liu
,
J.C.
(
2019
)
Characterization of resilin-like proteins with tunable mechanical properties
.
J. Mech. Behav. Biomed. Mater.
91
,
68
75
54
Dinjaski
,
N.
and
Kaplan
,
D.L.
(
2016
)
Recombinant protein blends: silk beyond natural design
.
Curr. Opin. Biotechnol.
39
,
1
7
55
Debabov
,
V.G.
and
Bogush
,
V.G.
(
2020
)
Recombinant spidroins as the basis for new materials
.
ACS Biomater. Sci. Eng.
6
,
3745
3761
56
Saric
,
M.
and
Scheibel
,
T.
(
2019
)
Engineering of silk proteins for materials applications
.
Curr. Opin. Biotechnol.
60
,
213
220
57
Choi
,
S.M.
,
Chaudhry
,
P.
,
Zo
,
S.M.
and
Han
,
S.S.
(
2018
)
Advances in protein-based materials: from origin to novel biomaterials
.
Adv. Exp. Med. Biol.
1078
,
161
210
58
Liu
,
Z.
,
Jiang
,
Q.
,
Zhang
,
Y.
,
Li
,
T.
and
Zhang
,
H.C.
(
2016
)
Sustainability of 3D printing: A critical review and recommendations
. In
ASME 2016 11th International Manufacturing Science and Engineering Conference, MSEC 2016
.
American Society of Mechanical Engineers
59
Donderwinkel
,
I.
,
Van Hest
,
J.C.M.
and
Cameron
,
N.R.
(
2017
)
Bio-inks for 3D bioprinting: recent advances and future prospects
.
Polym. Chem.
8
,
4451
4471
60
Liu
,
J.
,
Sun
,
L.
,
Xu
,
W.
,
Wang
,
Q.
,
Yu
,
S.
and
Sun
,
J.
(
2019
)
Current advances and future perspectives of 3D printing natural-derived biopolymers
.
Carbohydr. Polym.
207
,
297
316
61
Groll
,
J.
,
Burdick
,
J.A.
,
Cho
,
D.W.
,
Derby
,
B.
,
Gelinsky
,
M.
,
Heilshorn
,
S.C.
et al (
2019
)
A definition of bioinks and their distinction from biomaterial inks
.
Biofabrication
11
,
013001
62
Schloss
,
A.C.
,
Williams
,
D.M.
and
Regan
,
L.J.
(
2016
)
Protein-based hydrogels for tissue engineering
.
Adv. Exp. Med. Biol.
940
,
167
177
63
Jammalamadaka
,
U.
and
Tappa
,
K.
(
2018
)
Recent advances in biomaterials for 3d printing and tissue engineering
.
J. Funct. Biomater.
9
,
22
64
Ngo
,
T.D.
,
Kashani
,
A.
,
Imbalzano
,
G.
,
Nguyen
,
K.T.Q.
and
Hui
,
D.
(
2018
)
Additive manufacturing (3D printing): a review of materials, methods, applications and challenges
.
Compos. B: Eng.
143
,
172
196
65
Kim
,
S.H.
,
Yeon
,
Y.K.
,
Lee
,
J.M.
,
Chao
,
J.R.
,
Lee
,
Y.J.
,
Seo
,
Y.B.
et al (
2018
)
Precisely printable and biocompatible silk fibroin bioink for digital light processing 3D printing
.
Nat. Commun.
9
,
1620
66
Li
,
J.
,
Wu
,
C.
,
Chu
,
P.K.
and
Gelinsky
,
M.
(
2020
)
3D printing of hydrogels: rational design strategies and emerging biomedical applications
.
Mater. Sci. Eng. R: Rep.
140
,
100543
67
Guvendiren
,
M.
,
Molde
,
J.
,
Soares
,
R.M.D.
and
Kohn
,
J.
(
2016
)
Designing biomaterials for 3D printing
.
ACS Biomater. Sci. Eng.
2
,
1679
1693
68
Calva-Estrada
,
S.J.
,
Jiménez-Fernández
,
M.
and
Lugo-Cervantes
,
E.
(
2019
)
Protein-based films: advances in the development of biomaterials applicable to food packaging
.
Food Eng. Rev.
11
,
78
92
69
Yang
,
J.M.
,
Olanrele
,
O.S.
,
Zhang
,
X.
and
Hsu
,
C.C.
(
2018
)
Fabrication of hydrogel materials for biomedical applications
.
Adv. Exp. Med. Biol.
1077
,
197
224
70
Ozbolat
,
I.T.
and
Hospodiuk
,
M.
(
2016
)
Current advances and future perspectives in extrusion-based bioprinting
.
Biomaterials
76
,
321
343
71
Choi
,
G.
and
Cha
,
H.J.
(
2019
)
Recent advances in the development of nature-derived photocrosslinkable biomaterials for 3D printing in tissue engineering [Internet]
.
Biomater. Res.
23
,
1
7
72
Marques
,
C.F.
,
Diogo
,
G.S.
,
Pina
,
S.
,
Oliveira
,
J.M.
,
Silva
,
T.H.
and
Reis
,
R.L.
(
2019
)
Collagen-based bioinks for hard tissue engineering applications: a comprehensive review
.
J. Mater. Sci.: Mater. Med.
30
,
1
12
73
Montalbano
,
G.
,
Molino
,
G.
,
Fiorilli
,
S.
and
Vitale-Brovarone
,
C.
(
2020
)
Synthesis and incorporation of rod-like nano-hydroxyapatite into type I collagen matrix: a hybrid formulation for 3D printing of bone scaffolds
.
J. Eur. Ceram. Soc.
40
,
3689
3697
74
Lee
,
A.
,
Hudson
,
A.R.
,
Shiwarski
,
D.J.
,
Tashman
,
J.W.
,
Hinton
,
T.J.
,
Yerneni
,
S.
et al (
2019
)
3D bioprinting of collagen to rebuild components of the human heart
.
Science
365
,
482
487
75
Yue
,
K.
,
Trujillo-de Santiago
,
G.
,
Alvarez
,
M.M.
,
Tamayol
,
A.
,
Annabi
,
N.
and
Khademhosseini
,
A.
(
2015
)
Synthesis, properties, and biomedical applications of gelatin methacryloyl (GelMA) hydrogels
.
Biomaterials
73
,
254
271
76
Shirahama
,
H.
,
Lee
,
B.H.
,
Tan
,
L.P.
and
Cho
,
N.J.
(
2016
)
Precise tuning of facile one-pot gelatin methacryloyl (GelMA) synthesis
.
Sci. Rep.
6
,
31036
77
Yue
,
K.
,
Li
,
X.
,
Schrobback
,
K.
,
Sheikhi
,
A.
,
Annabi
,
N.
,
Leijten
,
J.
et al (
2017
)
Structural analysis of photocrosslinkable methacryloyl-modified protein derivatives
.
Biomaterials
139
,
163
171
78
Eng
,
G.
,
Lee
,
B.W.
,
Parsa
,
H.
,
Chin
,
C.D.
,
Schneider
,
J.
,
Linkov
,
G.
et al (
2013
)
Assembly of complex cell microenvironments using geometrically docked hydrogel shapes
.
Proc. Natl Acad. Sci. U.S.A.
110
,
4551
4556
79
Hasan
,
A.
,
Paul
,
A.
,
Memic
,
A.
and
Khademhosseini
,
A.
(
2015
)
A multilayered microfluidic blood vessel-like structure
.
Biomed. Microdevices
17
,
88
80
Boere
,
K.W.M.
,
Visser
,
J.
,
Seyednejad
,
H.
,
Rahimian
,
S.
,
Gawlitta
,
D.
,
Van Steenbergen
,
M.J.
et al (
2014
)
Covalent attachment of a three-dimensionally printed thermoplast to a gelatin hydrogel for mechanically enhanced cartilage constructs
.
Acta Biomater.
10
,
2602
2611
81
Wang
,
Z.
,
Abdulla
,
R.
,
Parker
,
B.
,
Samanipour
,
R.
,
Ghosh
,
S.
and
Kim
,
K.
(
2015
)
A simple and high-resolution stereolithography-based 3D bioprinting system using visible light crosslinkable bioinks
.
Biofabrication
7
,
045009
82
Lim
,
K.S.
,
Levato
,
R.
,
Costa
,
P.F.
,
Castilho
,
M.D.
,
Alcala-Orozco
,
C.R.
,
Van Dorenmalen
,
K.M.A.
et al (
2018
)
Bio-resin for high resolution lithography-based biofabrication of complex cell-laden constructs
.
Biofabrication
10
,
034101
83
Wang
,
Q.
,
Han
,
G.
,
Yan
,
S.
and
Zhang
,
Q.
(
2019
)
3D printing of silk fibroin for biomedical applications
.
Materials
12
,
504
84
Zarei
,
M.
,
Tanideh
,
N.
,
Zare
,
S.
,
Aslani
,
F.S.
,
Koohi-Hosseinabadi
,
O.
,
Rowshanghias
,
A.
et al (
2019
)
Electrospun poly(3-hydroxybutyrate)/chicken feather-derived keratin scaffolds: fabrication, in vitro and in vivo biocompatibility evaluation
.
J. Biomater. Appl.
34
,
741
752
85
Ruzgar
,
D.G.
,
Kurtoglu
,
S.A.
and
Bhullar
,
S.K.
(
2020
)
A study on extraction and characterization of keratin films and nanofibers from waste wool fiber
.
J. Nat. Fibers
17
,
427
436
86
Suarato
,
G.
,
Contardi
,
M.
,
Perotto
,
G.
,
Heredia-Guerrero
,
J.A.
,
Fiorentini
,
F.
,
Ceseracciu
,
L.
et al (
2020
)
From fabric to tissue: recovered wool keratin/polyvinylpyrrolidone biocomposite fibers as artificial scaffold platform
.
Mater. Sci. Eng. C
116
,
111151
87
Zarrintaj
,
P.
,
Yazdi
,
M.K.
,
Jouyandeh
,
M.
and
Saeb
,
M.R.
(
2019
)
PANI-based nanostructures
.
Fundam. Emerg. Appl. Polyaniline
121
130
88
Jayarajan
,
R.
,
Kumar
,
R.
,
Gupta
,
J.
,
Dev
,
G.
,
Kadu
,
P.
,
Chatterjee
,
D.
et al (
2019
)
Fabrication of an amyloid fibril-palladium nanocomposite: a sustainable catalyst for C-H activation and the electrooxidation of ethanol
.
J. Mater. Chem. A
7
,
4486
4493
89
Li
,
X.
,
Cao
,
Y.
,
Luo
,
K.
,
Sun
,
Y.
,
Xiong
,
J.
,
Wang
,
L.
et al (
2019
)
Highly active enzyme–metal nanohybrids synthesized in protein–polymer conjugates
.
Nat. Catal.
2
,
718
725
90
Ljubetič
,
A.
,
Lapenta
,
F.
,
Gradišar
,
H.
,
Drobnak
,
I.
,
Aupič
,
J.
,
Strmšek
,
Ž
et al (
2017
)
Design of coiled-coil protein-origami cages that self-assemble in vitro and in vivo
.
Nat. Biotechnol.
35
,
1094
1101
91
Azmi
,
M.A.
and
Shad
,
K.F.
(
2017
)
Role of nanostructure molecules in enhancing the bioavailability of oral drugs
.
Nanostructures Nov. Ther.
375
407
92
Domigan
,
L.J.
and
Gerrard
,
J.A.
(
2020
)
Introduction to protein nanotechnology
.
Methods Mol. Biol.
2073
,
1
13
93
Bleem
,
A.
and
Daggett
,
V.
(
2016
)
Structural and functional diversity among amyloid proteins: agents of disease, building blocks of biology, and implications for molecular engineering
.
Biotechnol. Bioeng.
114
,
7
20
94
Cao
,
Y.
and
Mezzenga
,
R.
(
2019
)
Food protein amyloid fibrils: origin, structure, formation, characterization, applications and health implications
.
Adv. Colloid Interface Sci.
269
,
334
356
95
Mohammadian
,
M.
and
Madadlou
,
A.
(
2016
)
Cold-set hydrogels made of whey protein nanofibrils with different divalent cations
.
Int. J. Biol. Macromol.
89
,
499
506
96
Rabe
,
R.
,
Hempel
,
U.
,
Martocq
,
L.
,
Keppler
,
J.K.
,
Aveyard
,
J.
and
Douglas
,
T.E.L.
(
2020
)
Dairy-inspired coatings for bone implants from whey protein isolate-derived self-assembled fibrils
.
Int. J. Mol. Sci.
21
,
5544
97
Lee
,
J.
,
Lee
,
J.-H.
,
Yeom
,
B.
and
Char
,
K.
(
2018
)
Layer-by-layer assembly of κ-Casein amyloid fibrils for the preparation of hollow microcapsules
.
Macromol. Chem. Phys.
219
,
1700382
98
Zhang
,
Q.
,
Bolisetty
,
S.
,
Cao
,
Y.
,
Handschin
,
S.
,
Adamcik
,
J.
,
Peng
,
Q.
et al (
2019
)
Selective and efficient removal of fluoride from water: in situ engineered amyloid fibril/ZrO 2 hybrid membranes
.
Angew. Chem. Int. Ed.
58
,
6012
6016
99
Zhang
,
Y.
,
Liang
,
S.
,
Zhang
,
J.
,
Chi
,
Y.
,
Tian
,
B.
,
Li
,
L.
et al (
2020
)
Preparation of whey protein isolate nanofibrils by microwave heating and its application as carriers of lipophilic bioactive substances
.
LWT
125
,
109213
100
Das
,
S.
,
Kumawat
,
M.K.
,
Ranganathan
,
S.
,
Kumar
,
R.
,
Adamcik
,
J.
,
Kadu
,
P.
et al (
2018
)
Cell alignment on graphene-amyloid composites
.
Adv. Mater. Interfaces
5
,
1800621
101
Cao
,
Y.
,
Bolisetty
,
S.
,
Wolfisberg
,
G.
,
Adamcik
,
J.
and
Mezzenga
,
R.
(
2019
)
Amyloid fibril-directed synthesis of silica core–shell nanofilaments, gels, and aerogels
.
Proc. Natl Acad. Sci. U.S.A.
116
,
4012
4017
102
Pan
,
K.
and
Zhong
,
Q.
(
2015
)
Amyloid-like fibrils formed from intrinsically disordered caseins: physicochemical and nanomechanical properties
.
Soft Matter
11
,
5898
5904
103
Jayawardena
,
N.
,
Kaur
,
M.
,
Nair
,
S.
,
Malmstrom
,
J.
,
Goldstone
,
D.
,
Negron
,
L.
et al (
2017
)
Amyloid fibrils from hemoglobin
.
Biomolecules
7
,
37
104
Sarkar
,
N.
(
2020
)
Functional amyloids
.
Biopolym.-Based Formul.: Biomed. Food Appl.
263
282
105
Wan
,
Z.
,
Yang
,
X.
and
Sagis
,
L.M.C.
(
2016
)
Contribution of long fibrils and peptides to surface and foaming behavior of Soy protein fibril system
.
Langmuir
32
,
8092
8101
106
Khan
,
I.
,
Saeed
,
K.
and
Khan
,
I.
(
2019
)
Nanoparticles: properties, applications and toxicities
.
Arab. J. Chem.
12
,
908
931
107
Vijayakumar
,
S.
and
Vaseeharan
,
B.
(
2018
)
Antibiofilm, anti cancer and ecotoxicity properties of collagen based ZnO nanoparticles
.
Adv. Powder Technol.
29
,
2331
2345
108
Reiter
,
T.
,
Panick
,
T.
,
Schuhladen
,
K.
,
Roether
,
J.A.
,
Hum
,
J.
and
Boccaccini
,
A.R.
(
2019
)
Bioactive glass based scaffolds coated with gelatin for the sustained release of icariin
.
Bioact. Mater.
4
,
1
7
109
Neamtu
,
I.
,
Rusu
,
A.G.
,
Diaconu
,
A.
,
Nita
,
L.E.
and
Chiriac
,
A.P.
(
2017
)
Basic concepts and recent advances in nanogels as carriers for medical applications
.
Drug Deliv.
24
,
539
557
110
Kang
,
M.G.
,
Lee
,
M.Y.
,
Cha
,
J.M.
,
Lee
,
J.K.
,
Lee
,
S.C.
,
Kim
,
J.
et al (
2019
)
Nanogels derived from fish gelatin: application to drug delivery system
.
Mar. Drugs
17
,
246
111
Wang
,
X.
,
Ding
,
B.
,
Yu
,
J.
and
Yang
,
J.
(
2011
)
Large-scale fabrication of two-dimensional spider-web-like gelatin nano-nets via electro-netting
.
Colloids Surf. B Biointerfaces
86
,
345
352
112
Saber
,
O.
,
Aljaafari
,
A.
,
Asiri
,
S.
and
Batoo
,
K.M.
(
2018
)
Designing magnetic layered double hydroxides and two-dimensional magnetic nano-nets of cobalt ferrite through a novel approach
.
Appl. Sci.
8
,
2099
113
Kucharczyk
,
K.
,
Florczak
,
A.
,
Deptuch
,
T.
,
Penderecka
,
K.
,
Jastrzebska
,
K.
,
Mackiewicz
,
A.
et al (
2020
)
Drug affinity and targeted delivery: double functionalization of silk spheres for controlled doxorubicin delivery into Her2-positive cancer cells
.
J. Nanobiotechnol.
18
,
56
114
Whittall
,
D.R.
,
Baker K
,
V.
,
Breitling
,
R.
and
Takano
,
E.
(
2020
)
Host systems for the production of recombinant spider silk
.
Trends Biotechnol
S0167-7799(20)30244-4
115
Maity
,
B.
,
Samanta
,
S.
,
Sarkar
,
S.
,
Alam
,
S.
and
Govindaraju
,
T.
(
2020
)
Injectable silk fibroin-based hydrogel for sustained insulin delivery in diabetic rats
.
ACS Appl. Bio Mater.
3
,
3544
3552
116
Zhu
,
M.
,
Liu
,
Y.
,
Jiang
,
F.
,
Cao
,
J.
,
Kundu
,
S.C.
and
Lu
,
S.
(
2020
)
Combined silk fibroin microneedles for insulin delivery
.
ACS Biomater. Sci. Eng.
6
,
3422
3429
117
Kuo
,
C.Y.
,
Guo
,
T.
,
Cabrera-Luque
,
J.
,
Arumugasaamy
,
N.
,
Bracaglia
,
L.
,
Garcia-Vivas
,
A.
et al (
2018
)
Placental basement membrane proteins are required for effective cytotrophoblast invasion in a three-dimensional bioprinted placenta model
.
J. Biomed. Mater. Res. A
106
,
1476
1487
118
Fan
,
Z.
,
Cheng
,
P.
,
Yin
,
G.
,
Wang
,
Z.
and
Han
,
J.
(
2020
)
In situ forming oxidized salecan/gelatin injectable hydrogels for vancomycin delivery and 3D cell culture
.
J. Biomater. Sci. Polym. Ed.
31
,
762
780
119
Bloise
,
N.
,
Patrucco
,
A.
,
Bruni
,
G.
,
Montagna
,
G.
,
Caringella
,
R.
,
Fassina
,
L.
et al (
2020
)
In vitro production of calcified bone matrix onto wool keratin scaffolds via osteogenic factors and electromagnetic stimulus
.
Materials (Basel)
13
,
3052
120
Naderi
,
P.
,
Zarei
,
M.
,
Karbasi
,
S.
and
Salehi
,
H.
(
2020
)
Evaluation of the effects of keratin on physical, mechanical and biological properties of poly (3-hydroxybutyrate) electrospun scaffold: potential application in bone tissue engineering
.
Eur. Polym. J.
124
,
109502
121
Dias
,
G.J.
,
Ramesh
,
N.
,
Neilson
,
L.
,
Cornwall
,
J.
,
Kelly
,
R.J.
and
Anderson
,
G.M.
(
2020
)
The adaptive immune response to porous regenerated keratin as a bone graft substitute in an ovine model
.
Int. J. Biol. Macromol.
165
,
100
106
122
Ghazanfari
,
S.
,
Alberti
,
K.A.
,
Xu
,
Q.
and
Khademhosseini
,
A.
(
2019
)
Evaluation of an elastic decellularized tendon-derived scaffold for the vascular tissue engineering application
.
J. Biomed. Mater. Res. A
107
,
1225
1234
123
Khalili
,
S.
,
Khorasani
,
S.N.
,
Razavi
,
S.M.
,
Hashemibeni
,
B.
and
Tamayol
,
A.
(
2019
)
Nanofibrous scaffolds with biomimetic composition for skin regeneration
.
Appl. Biochem. Biotechnol.
187
,
1193
1203
124
Tytgat
,
L.
,
Markovic
,
M.
,
Qazi
,
T.H.
,
Vagenende
,
M.
,
Bray
,
F.
,
Martins
,
J.C.
et al (
2019
)
Photo-crosslinkable recombinant collagen mimics for tissue engineering applications
.
J. Mater. Chem. B
7
,
3100
3108
125
Cao
,
J.
,
Wang
,
P.
,
Liu
,
Y.
,
Zhu
,
C.
and
Fan
,
D.
(
2020
)
Double crosslinked HLC-CCS hydrogel tissue engineering scaffold for skin wound healing
.
Int. J. Biol. Macromol.
155
,
625
635
126
Vázquez
,
J.J.
and
Martíinez
,
E.S.M.
(
2019
)
Collagen and elastin scaffold by electrospinning for skin tissue engineering applications
.
J. Mater. Res.
34
,
2819
2827
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