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Biopolymers. 2002;66(2):79-92.

Peptide mimics of the Bowman-Birk inhibitor reactive site loop.

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  • 1Department of Immunology and Molecular Pathology, Windeyer Institute of Medical Sciences, University College London, 46 Cleveland St., London W1T 4JF, UK.

Abstract

Bowman-Birk Inhibitors (BBIs) are small highly cross-linked proteins that typically display an almost symmetrical "double-headed" structure. Each "head" contains an independent proteinase binding domain. The realization that one BBI molecule could form a 1:1:1 complex with two enzymes led early workers to dissect this activity. Now, after three decades of research, it has been possible to isolate the antiproteinase activity as small ( approximately 11 residues), cyclic, synthetic peptides, which display most of the functional aspects of the protein. More recently, it has been found that these peptide fragments are not just a synthetic curiosity-a natural 14-residue cyclic peptide (SFTI-1), which too encapsulates the BBI inhibitory motif, is found to occur in sunflowers. This article reviews the properties of BBI-based peptides (including SFTI-1) and discusses the features that are important for inhibitory activity.

Copyright 2002 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 66: 79-92, 2002

PMID:
12325158
[PubMed - indexed for MEDLINE]
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