A cactus-derived toxin-like cystine knot peptide with selective antimicrobial activity

Aboye, Teshome L, Stromstedt, Adam A, Gunasekera, Sunithi, Bruhn, Jan G, El-Seedi, Hesham, Rosengren K.J. and Goransson, Ulf (2015) A cactus-derived toxin-like cystine knot peptide with selective antimicrobial activity. ChemBioChem, 16 7: 1068-1077. doi:10.1002/cbic.201402704


Author Aboye, Teshome L
Stromstedt, Adam A
Gunasekera, Sunithi
Bruhn, Jan G
El-Seedi, Hesham
Rosengren K.J.
Goransson, Ulf
Title A cactus-derived toxin-like cystine knot peptide with selective antimicrobial activity
Journal name ChemBioChem   Check publisher's open access policy
ISSN 1439-7633
1439-4227
Publication date 2015-05-04
Year available 2015
Sub-type Article (original research)
DOI 10.1002/cbic.201402704
Volume 16
Issue 7
Start page 1068
End page 1077
Total pages 10
Place of publication Weinheim, Germany
Publisher Wiley - V C H Verlag GmbH & Co
Collection year 2016
Language eng
Abstract Naturally occurring cystine knot peptides show a wide range of biological activity, and as they have inherent stability they represent potential scaffolds for peptide-based drug design and biomolecular engineering. Here we report the discovery, sequencing, chemical synthesis, three-dimensional solution structure determination and bioactivity of the first cystine knot peptide from Cactaceae (cactus) family: Ep-AMP1 from Echinopsis pachanoi. The structure of Ep-AMP1 (35 amino acids) conforms to that of the inhibitor cystine knot (or knottin) family but represents a novel diverse sequence; its activity was more than 500 times higher against bacterial than against eukaryotic cells. Rapid bactericidal action and liposome leakage implicate membrane permeabilisation as the mechanism of action. Sequence homology places Ec-AMP1 in the plant C6-type of antimicrobial peptides, but the three dimensional structure is highly similar to that of a spider neurotoxin.
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2016 Collection
School of Biomedical Sciences Publications
 
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