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A Cactus-Derived Toxin-Like Cystine Knot Peptide with Selective Antimicrobial Activity
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Medicinal Chemistry, Division of Pharmacognosy. (Ulf Goransson)
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Medicinal Chemistry, Division of Pharmacognosy. (Ulf Goransson)ORCID iD: 0000-0001-9070-6944
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Medicinal Chemistry, Division of Pharmacognosy. (Ulf Goransson)
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Medicinal Chemistry, Division of Pharmacognosy.
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2015 (English)In: ChemBioChem (Print), ISSN 1439-4227, E-ISSN 1439-7633, Vol. 16, no 7, 1068-1077 p.Article in journal (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
2015. Vol. 16, no 7, 1068-1077 p.
Keyword [en]
antibiotics, C6-type AMP, Cactaceae, cystine knot, drug discovery, plant antimicrobial peptide
National Category
Biochemistry and Molecular Biology Pharmaceutical Sciences
Identifiers
URN: urn:nbn:se:uu:diva-253232DOI: 10.1002/cbic.201402704ISI: 000353502300009PubMedID: 25821084OAI: oai:DiVA.org:uu-253232DiVA: diva2:824560
Available from: 2015-06-22 Created: 2015-05-25 Last updated: 2017-12-04Bibliographically approved

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Strömstedt, Adam A.Gunasekera, SunithiBruhn, Jan G.El-Seedi, HeshamGöransson, Ulf

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