Conformational studies on peptides as enzyme inhibitors: chymotrypsin inhibitors using Bowman–Birk type as models
- 1 January 1994
- journal article
- research article
- Published by Royal Society of Chemistry (RSC) in Journal of the Chemical Society, Perkin Transactions 2
- No. 5,p. 1047-1053
- https://doi.org/10.1039/p29940001047
Abstract
A complete structural characterization in solution, by NMR spectroscopy, and in vacuo, by molecular dynamic simulations, of two synthetic peptide fragments from SBBI (Soybean Bowman–Birk Inhibitor) is reported. Peptide 197, corresponding to the SBBI(41–49) chymotrypsin recognition site, has free N- and C-terminal groups, while peptide 212, corresponding to the Leu 16-SBBI(14–22) has uncharged and fully protected terminal ends. Peptide 212 shows significant anti-chymotryptic activity while peptide 197 is inactive. Neither of the two peptides shows anti-tryptic activity. The structural information obtained in the present paper suggests a quantitative structure–activity relationship which may help both in understanding the mechanism of action of protease inhibitors, and in providing new directions for the rational design of more specific and potent inhibitors.Keywords
This publication has 54 references indexed in Scilit:
- Binding of the bovine basic pancreatic trypsin inhibitor (Kunitz) to human Glu1-, Lys77-, Val442- and Val561-plasmin: a comparative studyBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1990
- Protein inhibitors of hydrolases in plant foodstuffsFood Reviews International, 1990
- Binding of kunitz and eglin c inhibitors to serine proteinases: thermodynamic, kinetic and molecular aspectsJournal of Molecular Catalysis, 1988
- Binding of the bovine basic pancreatic trypsin inhibitor (Kunitz) to human α-, β- and γ-thrombin; a kinetic and thermodynamic studyBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1988
- Binding of the Recombinant Proteinase Inhibitor Eglin C from LeechHzrudo Medzcznalzsto Human Leukocyte Elastase, Bovine α-Chymotrypsin and Subtilisin Carlsberg: Thermodynamic StudyJournal of Enzyme Inhibition, 1988
- Structure of bovine pancreatic trypsin inhibitorJournal of Molecular Biology, 1984
- Protein Inhibitors of ProteinasesAnnual Review of Biochemistry, 1980
- Structural basis of the activation and action of trypsinAccounts of Chemical Research, 1978
- Crystallographic refinement of the structure of bovine pancreatic trypsin inhibitor at l.5 Å resolutionActa Crystallographica Section B: Structural Science, Crystal Engineering and Materials, 1975
- Structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitorJournal of Molecular Biology, 1974