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Peptide mimics of the Bowman–Birk inhibitor reactive site loop
Author(s) -
McBride Jeffrey D.,
Watson Emma M.,
Brauer Arnd B. E.,
Jaulent Agnès M.,
Leatherbarrow Robin J.
Publication year - 2002
Publication title -
peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.10228
Subject(s) - cyclic peptide , chemistry , peptide , residue (chemistry) , biochemistry , oligopeptide , enzyme , stereochemistry
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 (∼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. © 2002 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 66: 79–92, 2002