Linear and cyclic glycopeptide as HIV protease inhibitors

Eur J Med Chem. 2013 Feb:60:144-54. doi: 10.1016/j.ejmech.2012.11.018. Epub 2012 Nov 29.

Abstract

Novel linear and cyclic glycotetrapeptides were designed, synthesized and tested for inhibition of the wild type C-SA HIV-1 protease enzyme. The incorporation of β-amino acid sugar to the linear and cyclic peptides resulted in a series of fifteen novel compounds. Linear glycopeptide 4a and cyclic glycopeptide 6a displayed significant activities against the HIV protease enzyme. The experimental results were compared with a computational approach using molecular docking. The sugar hydroxyl group at the C(3) position in linear (4a) as well as cyclic glycopeptide (6a), shows hydrogen bonding interaction with the enzymatic Asp25/Asp25' residues in docking studies.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Dose-Response Relationship, Drug
  • Glycopeptides / chemical synthesis
  • Glycopeptides / chemistry
  • Glycopeptides / pharmacology*
  • HIV Protease / metabolism*
  • HIV Protease Inhibitors / chemical synthesis
  • HIV Protease Inhibitors / chemistry*
  • HIV Protease Inhibitors / pharmacology*
  • Models, Molecular
  • Molecular Structure
  • Structure-Activity Relationship

Substances

  • Glycopeptides
  • HIV Protease Inhibitors
  • HIV Protease