Design and inhibitory properties of synthetic Bowman-Birk loops

A cyclic tridecapeptide based on the sequence of an anti‐tryptic loop of a Bowman‐Birk inhibitor was synthesized, and demonstrated to be active as an inhibitor of trypsin. Molecular modeling of this sequence suggested an improved sequence which demonstrated an order of magnitude improvement in the i...

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Veröffentlicht in:	International Journal of Peptide and Protein Research 1992-08, Vol.40 (2), p.97-102
Hauptverfasser:	MAEDER, DENNIS L., SUNDE, MARGARET, BOTES, DAWIE P.
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Analytical, structural and metabolic biochemistry Binding, Competitive Biological and medical sciences Bowman-Birk Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Hydrolases inhibitor kinetic Kinetics macrotyloma Models, Molecular Models, Structural Molecular Sequence Data Molecular Structure peptide Peptide Fragments - chemical synthesis Peptide Fragments - chemistry Peptide Fragments - pharmacology Protein Conformation Serine - chemistry Structure-Activity Relationship synthesis Threonine - chemistry Trypsin Inhibitor, Bowman-Birk Soybean - chemical synthesis Trypsin Inhibitor, Bowman-Birk Soybean - pharmacology
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Beschreibung
Zusammenfassung:	A cyclic tridecapeptide based on the sequence of an anti‐tryptic loop of a Bowman‐Birk inhibitor was synthesized, and demonstrated to be active as an inhibitor of trypsin. Molecular modeling of this sequence suggested an improved sequence which demonstrated an order of magnitude improvement in the inhibitory constant.
ISSN:	0367-8377 1399-3011
DOI:	10.1111/j.1399-3011.1992.tb01455.x