Document Detail

Buckwheat trypsin inhibitor with helical hairpin structure belongs to a new family of plant defence peptides.
MedLine Citation:
PMID:  22612157     Owner:  NLM     Status:  MEDLINE    
A new peptide trypsin inhibitor named BWI-2c was obtained from buckwheat (Fagopyrum esculentum) seeds by sequential affinity, ion exchange and reversed-phase chromatography. The peptide was sequenced and found to contain 41 amino acid residues, with four cysteine residues involved in two intramolecular disulfide bonds. Recombinant BWI-2c identical to the natural peptide was produced in Escherichia coli in a form of a cleavable fusion with thioredoxin. The 3D (three-dimensional) structure of the peptide in solution was determined by NMR spectroscopy, revealing two antiparallel α-helices stapled by disulfide bonds. Together with VhTI, a trypsin inhibitor from veronica (Veronica hederifolia), BWI-2c represents a new family of protease inhibitors with an unusual α-helical hairpin fold. The linker sequence between the helices represents the so-called trypsin inhibitory loop responsible for direct binding to the active site of the enzyme that cleaves BWI-2c at the functionally important residue Arg(19). The inhibition constant was determined for BWI-2c against trypsin (1.7×10(-1)0 M), and the peptide was tested on other enzymes, including those from various insect digestive systems, revealing high selectivity to trypsin-like proteases. Structural similarity shared by BWI-2c, VhTI and several other plant defence peptides leads to the acknowledgement of a new widespread family of plant peptides termed α-hairpinins.
Peter B Oparin; Konstantin S Mineev; Yakov E Dunaevsky; Alexander S Arseniev; Mikhail A Belozersky; Eugene V Grishin; Tsezi A Egorov; Alexander A Vassilevski
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  The Biochemical journal     Volume:  446     ISSN:  1470-8728     ISO Abbreviation:  Biochem. J.     Publication Date:  2012 Aug 
Date Detail:
Created Date:  2012-07-27     Completed Date:  2012-10-29     Revised Date:  2012-11-02    
Medline Journal Info:
Nlm Unique ID:  2984726R     Medline TA:  Biochem J     Country:  England    
Other Details:
Languages:  eng     Pagination:  69-77     Citation Subset:  IM    
M. M. Shemyakin and Yu. A. Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya, 16/10, 117997 Moscow, Russia.
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MeSH Terms
Amino Acid Sequence
Chromatography, Reverse-Phase
Fagopyrum / chemistry*,  physiology
Magnetic Resonance Spectroscopy
Molecular Sequence Data
Peptides / chemistry*,  genetics,  metabolism
Plant Proteins / chemistry*,  genetics,  metabolism
Protein Conformation
Protein Folding
Recombinant Proteins / genetics,  metabolism
Seeds / chemistry
Trypsin Inhibitors / chemistry*,  isolation & purification
Reg. No./Substance:
0/Peptides; 0/Plant Proteins; 0/Recombinant Proteins; 0/Trypsin Inhibitors
Erratum In:
Biochem J. 2012 Sep 1;446(2):331

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