Exploiting binding-site arginines in drug design: Recent examples |
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| Affiliation: | Prelude Therapeutics, 200 Powder Mill Road, Wilmington, DE 19803, United States;College of Pharmacy, Department of Pharmacology and Toxicology, The University of Arizona, Tucson, USA;BIO-5 Oro Valley, The University of Arizona, Ora Valley, AZ 85737, USA;Department of Medicinal Chemistry, School of Pharmacy, Health Science Center, Xi’an Jiaotong University, 76 West Yanta Road, Xi’an, Shaanxi 710061, PR China;Department of Organic Chemistry, Faculty of Chemistry, Marie Curie-Sklodowska University, Gliniana 33, 20-614 Lublin, Poland;Department of Pharmacy, The First Affiliated Hospital of Zhengzhou University, Zhengzhou 450052, China;CSIR-National Chemical Laboratory, Division of Organic Chemistry, Dr. Homi Bhabha Road, Pune 411008, India |
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| Abstract: | Active or allosteric site arginines can form diverse interactions with ligands including different types of cation-π interactions, H-bond interactions and non-bond, non-canonical interactions. This provides many opportunities for creative structure-based drug design to improve potency, introduce novelty, and modulate MoA (mode of action), and even to achieve selectivity. This digest will use some recent drug targets of interest as examples to illustrate different types of interactions and how these interactions impact on potency, MoA, and selectivity. |
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| Keywords: | Structure-based drug design Protein ligand interaction Arginine Non-canonical interaction |
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