Binding of kunitz and eglin c inhibitors to serine proteinases: thermodynamic, kinetic and molecular aspects

Paolo Ascenzi, Gino Amiconi, Martino Bolognesi, Enea Menegatti, Mario Guarneri

Research output: Contribution to journalArticle

Abstract

Protein-protein recognition is not a simple process, but consists of a space-time series of events involving among other aspects: molecular flexibility; induced fit; entropy, enthalpy and free energy changes; solvent; as well as hydrophobic, van der Waals and electrostatic interactions. Since the reaction of serine proteinases with macromolecular inhibitors appears to be a good model for studying protein-protein interactions, thermodynamics and kinetics for BPTI and eglin c binding to human γ-thrombin, human leukocyte elastase, bovine β-trypsin, bovine α-chymotrypsin and/or subtilisin Carlsberg have been investigated and analyzed in the light of the available molecular models. Analysis of the data indicates that proteinase: inhibitor interactions follow multi-step processes involving various intermediates, until the system leads to the final adduct.

Original languageEnglish
Pages (from-to)297-306
Number of pages10
JournalJournal of Molecular Catalysis
Volume47
Issue number2-3
DOIs
Publication statusPublished - Sep 26 1988

ASJC Scopus subject areas

  • Engineering(all)

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