Rational drug discovery strategy requires a design of small molecules as candidate drugs which can specifically inhibit a target protein or any other macromolecule and effectively interfere in a defined physiological process. One of the important bacterial protein targets aimed toward developing new antibiotics is peptidyl-tRNA hydrolase (Pth). The discovery that cytarabine, a known anticancer drug, binds to Pth from Acinetobacter baumannii in a cleft located away from the catalytic site of this enzyme, published in Biochemical Journal, opens up interesting new avenues for drug design. An approach involving crystallographic identification of multiple ligand-binding sites on a target protein surface could enable iterative optimization of multiple high-affinity ligands, which may synergistically interfere in the target function with enhanced effect.
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March 2018
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The human immunodeficiency virus. In this issue of the Biochemical Journal, Parajuli et al. report that restricted the HIV Env (envelope glycoprotein) glycan engagement by a lectin reengineered DAVEI protein chimera is sufficient for virolysis. For details, see pages 931–957.
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March 09 2018
Multiple target sites for designing candidate drugs
Dinakar M. Salunke
1International Centre for Genetic Engineering and Biotechnology, Aruna Asaf Ali Marg, New Delhi 110 067, India
Correspondence: Dinakar M. Salunke ([email protected])
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Publisher: Portland Press Ltd
Received:
February 11 2018
Revision Received:
February 20 2018
Accepted:
February 20 2018
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© 2018 The Author(s). Published by Portland Press Limited on behalf of the Biochemical Society
2018
Biochem J (2018) 475 (5): 977–979.
Article history
Received:
February 11 2018
Revision Received:
February 20 2018
Accepted:
February 20 2018
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Citation
Dinakar M. Salunke; Multiple target sites for designing candidate drugs. Biochem J 15 March 2018; 475 (5): 977–979. doi: https://doi.org/10.1042/BCJ20180007
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