Unraveling sub-site specificities of peptidic serine protease inhibitors by substitutional and structural analysis

Protein Pept Lett. 2005 Jul;12(5):449-56. doi: 10.2174/0929866054395374.

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.

Publication types

  • Review

MeSH terms

  • Amino Acid Substitution
  • Crystallography, X-Ray
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Serine Endopeptidases / metabolism*
  • Serine Proteinase Inhibitors / chemistry
  • Serine Proteinase Inhibitors / physiology*
  • Structure-Activity Relationship

Substances

  • Serine Proteinase Inhibitors
  • Serine Endopeptidases