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• W1005057205 abstract "Structure-based drug design (SBDD) has developed as a consequence of the emergence of detailed structural information on drug target molecules, chiefly from advances in protein crystallography. The general principles of SBDD are that the ligand should efficiently fill the space in its binding site, that electrostatic complementarity and hydrogen bond formation between the ligand and its receptor should be maximized, and that the structural water molecules in the active site should be retained. SBDD has been applied to anticancer drug design, including antimetabolites, protease inhibitors, protein kinase inhibitors, and other targets. SBDD may indirectly address some of these pharmacologic aspects of drug design by suggesting novel designs for chemically unrelated inhibitors, without the loss of binding affinity. Several X-ray crystal structures of protein kinases with bound inhibitors have subsequently been solved, and SBDD techniques have been widely used in this field. The future potential of the SDBB process is most likely to be an iterative one with several cycles of design, synthesis, screening, and structural elucidation, requiring close interaction among medicinal chemists, computational chemists, and biologists." @default.
• W1005057205 created "2016-06-24" @default.
• W1005057205 creator A5079739797 @default.
• W1005057205 date "2002-01-01" @default.
• W1005057205 modified "2023-09-25" @default.
• W1005057205 title "STRUCTURE-BASED DRUG DESIGN AND ITS CONTRIBUTIONS TO CANCER CHEMOTHERAPY" @default.
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• W1005057205 doi "https://doi.org/10.1016/b978-012072651-6/50011-5" @default.
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