Abstract
The interaction of peptidic inhibitors with serine proteases is investigated using peptide spot synthesis on cellulose sheets. This method permits a highly parallel analysis of subsite specificities and an optimization of peptidic inhibitors towards higher affinity and specificity for a given target protease. Information from crystal structures of corresponding protease/inhibitor complexes may help to explain the observed binding pattern.
Keywords: serine protease, elastase, peptidic inhibitor, ovomucoid inhibitor, peptide spot synthesis, substitutional analysis, subsite specificity, x-ray structure
Protein & Peptide Letters
Title: Unraveling Sub-Site Specificities of Peptidic Serine Protease Inhibitors by Substitutional and Structural Analysis
Volume: 12 Issue: 5
Author(s): Wolfgang Hohne and Kai Hilpert
Affiliation:
Keywords: serine protease, elastase, peptidic inhibitor, ovomucoid inhibitor, peptide spot synthesis, substitutional analysis, subsite specificity, x-ray structure
Abstract: The interaction of peptidic inhibitors with serine proteases is investigated using peptide spot synthesis on cellulose sheets. This method permits a highly parallel analysis of subsite specificities and an optimization of peptidic inhibitors towards higher affinity and specificity for a given target protease. Information from crystal structures of corresponding protease/inhibitor complexes may help to explain the observed binding pattern.
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Cite this article as:
Hohne Wolfgang and Hilpert Kai, Unraveling Sub-Site Specificities of Peptidic Serine Protease Inhibitors by Substitutional and Structural Analysis, Protein & Peptide Letters 2005; 12 (5) . https://dx.doi.org/10.2174/0929866054395374
DOI https://dx.doi.org/10.2174/0929866054395374 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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