Buckwheat trypsin inhibitor with helical hairpin structure belongs to a new family of plant defence peptides

2012 ◽  
Vol 446 (2) ◽  
pp. 331-331
Author(s):  
P. B. Oparin ◽  
K. S. Mineev ◽  
Y. E. Dunaevsky ◽  
A. S. Arseniev ◽  
M. A. Belozersky ◽  
...  
Keyword(s):  
Trypsin Inhibitor ◽  
Plant Defence ◽  
Hairpin Structure ◽  
New Family ◽  
Helical Hairpin

Buckwheat trypsin inhibitor with helical hairpin structure belongs to a new family of plant defence peptides

2012 ◽  
Vol 446 (1) ◽  
pp. 69-77 ◽  
Author(s):  
Peter B. Oparin ◽  
Konstantin S. Mineev ◽  
Yakov E. Dunaevsky ◽  
Alexander S. Arseniev ◽  
Mikhail A. Belozersky ◽  
...  
Keyword(s):  
Trypsin Inhibitor ◽  
Disulfide Bonds ◽  
Plant Defence ◽  
Three Dimensional ◽  
Structural Similarity ◽  
Reversed Phase ◽  
Dimensional Structure ◽  
Amino Acid Residues ◽  
New Family ◽  
Helical Hairpin

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 Arg19. The inhibition constant was determined for BWI-2c against trypsin (1.7×10−10 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.

scholarly journals Defining the familial fold of the vicilin-buried peptide family

2020 ◽  
Author(s):  
Colton D. Payne ◽  
Grishma Vadlamani ◽  
Mark F. Fisher ◽  
Jingjing Zhang ◽  
Richard J. Clark ◽  
...  
Keyword(s):  
Disulfide Bonds ◽  
Solid Phase ◽  
Solid Phase Peptide Synthesis ◽  
Seed Storage ◽  
Structural Features ◽  
Salt Bridges ◽  
Plant Seed ◽  
Helix Loop Helix ◽  
New Family ◽  
Helical Hairpin

ABSTRACTPlants and their seeds have been shown to be a rich source of cystine-stabilized peptides. Recently a new family of plant seed peptides whose sequences are buried within precursors for seed storage vicilins was identified. Members of this Vicilin Buried Peptide (VBP) family are found in distantly related plant species including the monocot date palm, as well as dicotyledonous species like pumpkin and sesame. Genetic evidence for their widespread occurrence indicates that they are of ancient origin. Limited structural studies have been conducted on VBP family members, but two members have been shown to adopt a helical hairpin fold. We here present an extensive characterization of VBPs using solution NMR spectroscopy, to better understand their structural features. Four peptides were produced by solid phase peptide synthesis and shown to adopt a helix-loop-helix hairpin fold, as a result of the I-IV/II-III ladder-like connectivity of their disulfide bonds. Inter-helix interactions, including hydrophobic contacts and salt bridges, are critical for the fold stability and control the angle at which the anti-parallel α-helices interface. Activities reported for VBPs include trypsin inhibitory activity and inhibition of ribosomal function, however their diverse structural features despite a common fold suggest additional bioactivities yet to be revealed are likely.

Solution Structure of the Squash Trypsin Inhibitor MCoTI-II. A New Family for Cyclic Knottins†,‡

Biochemistry ◽  
2001 ◽  
Vol 40 (27) ◽  
pp. 7973-7983 ◽  
Author(s):  
Annie Heitz ◽  
Jean-François Hernandez ◽  
Jean Gagnon ◽  
Thai Trinh Hong ◽  
T. Trân Châu Pham ◽  
...  
Keyword(s):  
Trypsin Inhibitor ◽  
Solution Structure ◽  
New Family ◽  
Squash Trypsin Inhibitor

The diamondback moth, Plutella xylostella, specifically inactivates Mustard Trypsin Inhibitor 2 (MTI2) to overcome host plant defence

2009 ◽  
Vol 39 (1) ◽  
pp. 55-61 ◽  
Author(s):  
Limei Yang ◽  
Zhiyuan Fang ◽  
Marcel Dicke ◽  
Joop J.A. van Loon ◽  
Maarten A. Jongsma
Keyword(s):  
Host Plant ◽  
Trypsin Inhibitor ◽  
Plutella Xylostella ◽  
Diamondback Moth ◽  
Plant Defence

A New Family of β-Hairpin Mimetics Based on a Trypsin Inhibitor from Sunflower Seeds

ChemBioChem ◽  
2002 ◽  
Vol 3 (4) ◽  
pp. 318-323 ◽  
Author(s):  
Anne Descours ◽  
Kerstin Moehle ◽  
Annabelle Renard ◽  
John A. Robinson
Keyword(s):  
Trypsin Inhibitor ◽  
Sunflower Seeds ◽  
New Family

Solution Structure of the Macrocyclic Squash Trypsin Inhibitor MCoTI-II, the First Member of a New Family of Cyclic Knottins

2001 ◽  
pp. 387-388
Author(s):  
Annie Heitz ◽  
Jean-François Hernandez ◽  
Jean Gagnon ◽  
Thai Trinh Hong ◽  
Châu T. T. Pham ◽  
...  
Keyword(s):  
Trypsin Inhibitor ◽  
Solution Structure ◽  
New Family ◽  
Squash Trypsin Inhibitor

scholarly journals Author Correction: Octa-repeat domain of the mammalian prion protein mRNA forms stable A-helical hairpin structure rather than G-quadruplexes

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Andreas Czech ◽  
Petr V. Konarev ◽  
Ingrid Goebel ◽  
Dmitri I. Svergun ◽  
Peter R. Wills ◽  
...  
Keyword(s):  
Prion Protein ◽  
Hairpin Structure ◽  
Repeat Domain ◽  
Helical Hairpin
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