Enzyme isoselective inhibitors: A tool for binding-trend analysis

Rachel Ozeri, Netaly Khazanov, Nurit Perlman, Michael Shokhen, Amnon Albeck

Research output: Contribution to journalArticlepeer-review

8 Scopus citations


A transition-state analogue inhibitor that covalently reversibly binds to an enzyme formally consists of two parts: the chemical site, CS and the recognition site, RS. We have experimentally and theoretically demonstrated that the trend of binding affinity in a series of isoselective inhibitors (with identical RS and different CS fragments) depends mainly on their CS fragments. Isoselective inhibitors have the same affinity trend toward different enzymes of the same family with a common catalytic mechanism. Thus, very good correlation between experimentally determined and theoretically calculated K, values was demonstrated. A practical outcome is the application of the described method as a tool for an expert analysis in virtual screening of inhibitor libraries and in the design of new enzyme inhibitors.

Original languageEnglish
Pages (from-to)631-638
Number of pages8
Issue number6
StatePublished - Jun 2006


  • Binding trends
  • Drug design
  • Quantum chemistry
  • Serine proteases
  • Transition-state analogues


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