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Exploiting binding-site arginines in drug design: Recent examples.

Hong Lin1, Juan I Luengo1

  • 1Prelude Therapeutics, 200 Powder Mill Road, Wilmington, DE 19803, United States.

Bioorganic & Medicinal Chemistry Letters
|July 31, 2020
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Summary
This summary is machine-generated.

Arginine residues in drug targets enable diverse interactions like cation-π and H-bonds. This insight aids structure-based drug design for enhanced potency, novel drugs, and improved selectivity.

Keywords:
ArginineNon-canonical interactionProtein ligand interactionStructure-based drug design

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Area of Science:

  • Medicinal Chemistry
  • Structural Biology
  • Drug Discovery

Background:

  • Active and allosteric sites of drug targets feature arginine residues.
  • Arginine interactions with ligands are diverse, including cation-π, hydrogen bonds, and non-canonical interactions.

Purpose of the Study:

  • To illustrate how arginine interactions influence drug properties.
  • To highlight opportunities in structure-based drug design using arginine interactions.

Main Methods:

  • Review of recent drug targets and their interactions with arginine residues.
  • Analysis of how these interactions affect drug potency, mechanism of action (MoA), and selectivity.

Main Results:

  • Arginine's diverse interactions offer significant potential for drug design.
  • Specific examples demonstrate impact on potency, MoA, and selectivity.

Conclusions:

  • Understanding arginine interactions is crucial for creative drug design.
  • Leveraging these interactions can lead to improved drug efficacy and specificity.