Peptide mimics of the Bowman-Birk inhibitor reactive site loop
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 work...
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| Veröffentlicht in: | Biopolymers 2002, Vol.66 (2), p.79-92 |
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| creator | McBride, Jeffrey D. Watson, Emma M. Brauer, Arnd B. E. Jaulent, Agnès M. Leatherbarrow, Robin J. |
| description | 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 |
| doi_str_mv | 10.1002/bip.10228 |
| format | Article |
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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. 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E.</creatorcontrib><creatorcontrib>Jaulent, Agnès M.</creatorcontrib><creatorcontrib>Leatherbarrow, Robin J.</creatorcontrib><title>Peptide mimics of the Bowman-Birk inhibitor reactive site loop</title><title>Biopolymers</title><addtitle>Biopolymers</addtitle><description>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</description><subject>Amino Acid Sequence</subject><subject>antiproteinase</subject><subject>Binding Sites</subject><subject>Bowman-Birk inhibitors</subject><subject>Combinatorial Chemistry Techniques - methods</subject><subject>cross-linked proteins</subject><subject>Models, Molecular</subject><subject>Oligopeptides - chemistry</subject><subject>Oligopeptides - pharmacology</subject><subject>Protein Conformation</subject><subject>proteinase binding domain</subject><subject>SFTI-1</subject><subject>Structure-Activity Relationship</subject><subject>synthetic peptides</subject><subject>Trypsin - chemistry</subject><subject>Trypsin - metabolism</subject><subject>Trypsin Inhibitor, Bowman-Birk Soybean - chemistry</subject><subject>Trypsin Inhibitor, Bowman-Birk Soybean - pharmacology</subject><issn>0006-3525</issn><issn>1097-0282</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kF1LwzAUhoMobk4v_APSK8GLupM0absbwQ03B0OHH-hdSNOERdulJp1z_95qp155dQ6H5305PAgdYzjHAKSfmapZCEl3UBfDIAmBpGQXdQEgDiNGWAcdeP8CQGmEYR91MIkIwyztoou5qmqTq6A0pZE-sDqoFyoY2nUpluHQuNfALBcmM7V1gVNC1uZdBd7UKiisrQ7RnhaFV0fb2UOP46uH0XU4u51MR5ezUFIGaShVlOksj3IJOiZaaAmAk-ZKE5zkOWYyFlLTGKhOxSAfyJgJRhs0o1GaSBb10GnbWzn7tlK-5qXxUhWFWCq78jwhmACLkwY8a0HprPdOaV45Uwq34Rj4lyzeyOLfshr2ZFu6ykqV_5FbOw3Qb4G1KdTm_yY-nM5_KsM2YXytPn4Twr3y5rmE8aebCcej8R19ju85iT4Bz1iCAA</recordid><startdate>2002</startdate><enddate>2002</enddate><creator>McBride, Jeffrey D.</creator><creator>Watson, Emma M.</creator><creator>Brauer, Arnd B. 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| subjects | Amino Acid Sequence antiproteinase Binding Sites Bowman-Birk inhibitors Combinatorial Chemistry Techniques - methods cross-linked proteins Models, Molecular Oligopeptides - chemistry Oligopeptides - pharmacology Protein Conformation proteinase binding domain SFTI-1 Structure-Activity Relationship synthetic peptides Trypsin - chemistry Trypsin - metabolism Trypsin Inhibitor, Bowman-Birk Soybean - chemistry Trypsin Inhibitor, Bowman-Birk Soybean - pharmacology |
| title | Peptide mimics of the Bowman-Birk inhibitor reactive site loop |
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