Evaluation of triazolamers as active site inhibitors of HIV-1 protease

Andrea L. Jochim, Stephen E. Miller, Nicholas G. Angelo, Paramjit Arora

Research output: Contribution to journalArticle

Abstract

Proteases typically recognize their peptide substrates in extended conformations. General approaches for designing protease inhibitors often consist of peptidomimetics that feature this conformation. Herein we discuss a combination of computational and experimental studies to evaluate the potential of triazole-linked β-strand mimetics as inhibitors of HIV-1 protease activity.

Original languageEnglish (US)
Pages (from-to)6023-6026
Number of pages4
JournalBioorganic and Medicinal Chemistry Letters
Volume19
Issue number21
DOIs
StatePublished - Nov 1 2009

Fingerprint

Peptidomimetics
Triazoles
Protease Inhibitors
Conformations
Catalytic Domain
Peptide Hydrolases
Peptides
Substrates
Human immunodeficiency virus 1 p16 protease

Keywords

  • β-Strand mimetics
  • Peptidomimetics
  • Protease inhibitor

ASJC Scopus subject areas

  • Pharmaceutical Science
  • Drug Discovery
  • Organic Chemistry
  • Molecular Medicine
  • Molecular Biology
  • Clinical Biochemistry
  • Biochemistry

Cite this

Evaluation of triazolamers as active site inhibitors of HIV-1 protease. / Jochim, Andrea L.; Miller, Stephen E.; Angelo, Nicholas G.; Arora, Paramjit.

In: Bioorganic and Medicinal Chemistry Letters, Vol. 19, No. 21, 01.11.2009, p. 6023-6026.

Research output: Contribution to journalArticle

Jochim, Andrea L. ; Miller, Stephen E. ; Angelo, Nicholas G. ; Arora, Paramjit. / Evaluation of triazolamers as active site inhibitors of HIV-1 protease. In: Bioorganic and Medicinal Chemistry Letters. 2009 ; Vol. 19, No. 21. pp. 6023-6026.
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