The nature of the bilayer motif coupled with the ability of lipids and proteins to diffuse freely through this structure is crucial to the viability of cells and their ability to compartmentalize domains contained therein. It seems surprising to find then that biological as well as model membranes exist in a dynamic state of mechanical stress. The stresses within such membranes are surprisingly large, typically reaching up to 50 atm (1 atm=101.325 kPa) at the core of the membrane and vary as a function of depth. The uneven distribution of lateral pressures within monolayer leaflets causes them to bend away from or towards the water interface. This can result in the formation of complex, self-assembled mesophases, many of which occur in vivo. Our knowledge of the principles underlying membrane mechanics has reached the point where we are now able to manipulate them and create nano-structures with reasonable predictability. In addition, they can be used both to explain and control the partitioning of amphipathic proteins on to membranes. The dependence of the dynamics of membrane-bound proteins and the chemical reactivity of amphipathic drug molecules on membrane stresses suggests that Nature itself takes advantage of this. Understanding and manipulating these internal forces will be a key element in creating self-assembled, biocompatible, nanoscale cell-like systems.
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June 2007
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Conference Article|
May 22 2007
Using membrane stress to our advantage
G.C. Shearman;
G.C. Shearman
*Chemical Biology Centre, Department of Chemistry, Imperial College London, Exhibition Road, London SW7 2AZ, U.K.
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G.S. Attard;
G.S. Attard
†Department of Chemistry, University of Southampton, Southampton SO17 1BJ, U.K.
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A.N. Hunt;
A.N. Hunt
‡Department of Child Health, University of Southampton, Southampton SO17 1BJ, U.K.
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S. Jackowski;
S. Jackowski
§Department of Infectious Diseases, St. Jude Children's Research Hospital, Memphis, TH 38105-2794, U.S.A.
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M. Baciu;
M. Baciu
*Chemical Biology Centre, Department of Chemistry, Imperial College London, Exhibition Road, London SW7 2AZ, U.K.
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S.C. Sebai;
S.C. Sebai
*Chemical Biology Centre, Department of Chemistry, Imperial College London, Exhibition Road, London SW7 2AZ, U.K.
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X. Mulet;
X. Mulet
*Chemical Biology Centre, Department of Chemistry, Imperial College London, Exhibition Road, London SW7 2AZ, U.K.
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J.A. Clarke;
J.A. Clarke
*Chemical Biology Centre, Department of Chemistry, Imperial College London, Exhibition Road, London SW7 2AZ, U.K.
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R.V. Law;
R.V. Law
*Chemical Biology Centre, Department of Chemistry, Imperial College London, Exhibition Road, London SW7 2AZ, U.K.
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C. Plisson;
C. Plisson
∥GSK Clinical Imaging Centre, Imperial College London, Hammersmith Hospital, Du Cane Road, London W12 0NN, U.K.
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C.A. Parker;
C.A. Parker
∥GSK Clinical Imaging Centre, Imperial College London, Hammersmith Hospital, Du Cane Road, London W12 0NN, U.K.
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A. Gee;
A. Gee
*Chemical Biology Centre, Department of Chemistry, Imperial College London, Exhibition Road, London SW7 2AZ, U.K.
∥GSK Clinical Imaging Centre, Imperial College London, Hammersmith Hospital, Du Cane Road, London W12 0NN, U.K.
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O. Ces;
O. Ces
*Chemical Biology Centre, Department of Chemistry, Imperial College London, Exhibition Road, London SW7 2AZ, U.K.
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R.H. Templer
R.H. Templer
1
*Chemical Biology Centre, Department of Chemistry, Imperial College London, Exhibition Road, London SW7 2AZ, U.K.
1To whom correspondence should be addressed (email [email protected]).
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Publisher: Portland Press Ltd
Received:
January 24 2007
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© 2007 Biochemical Society
2007
Biochem Soc Trans (2007) 35 (3): 498–501.
Article history
Received:
January 24 2007
Citation
G.C. Shearman, G.S. Attard, A.N. Hunt, S. Jackowski, M. Baciu, S.C. Sebai, X. Mulet, J.A. Clarke, R.V. Law, C. Plisson, C.A. Parker, A. Gee, O. Ces, R.H. Templer; Using membrane stress to our advantage. Biochem Soc Trans 1 June 2007; 35 (3): 498–501. doi: https://doi.org/10.1042/BST0350498
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