An old target revisited: Two new privileged skeletons and an unexpected binding mode for HIV-protease inhibitors

Edgar Specker, Jark Böttcher, Hauke Lilie, Andreas Heine, Andreas Schoop, Gerhard Müller, Nils Griebenow, Gerhard Klebe

Research output: Contribution to journalArticlepeer-review

38 Scopus citations

Abstract

Favored entrance for the privileged. Two inhibitor structures to address the active site of aspartic proteases have been developed. They are equipped with a central hydroxysulfone unit and, alternatively, a pyrrolidine moiety and decorated with rationally designed side chains. The hydroxysulfones bind to HIV protease as expected, whereas the pyrrolidines display a surprising, previously unreported binding mode. (Chemical Equation Presented)

Original languageEnglish
Pages (from-to)3140-3144
Number of pages5
JournalAngewandte Chemie International Edition in English
Volume44
Issue number20
DOIs
StatePublished - 13 May 2005
Externally publishedYes

Keywords

  • Drug design
  • HIV protease
  • Inhibitors
  • Proteins
  • Structure determination

Fingerprint

Dive into the research topics of 'An old target revisited: Two new privileged skeletons and an unexpected binding mode for HIV-protease inhibitors'. Together they form a unique fingerprint.

Cite this