Cupiennin 1a, an antimicrobial peptide from the venom of the neotropical wandering spider Cupiennius salei, also inhibits the formation of nitric oxide by neuronal nitric oxide synthase

Pukala, Tara; Doyle, Jason; Llewellyn, Lyndon; Kuhn-Nentwig, Lucia; Apponyi, Margit; Separovic, Frances; Bowie, John (2007). Cupiennin 1a, an antimicrobial peptide from the venom of the neotropical wandering spider Cupiennius salei, also inhibits the formation of nitric oxide by neuronal nitric oxide synthase. FEBS journal, 7(274), pp. 1778-1784. Oxford: Wiley-Blackwell 10.1111/j.1742-4658.2007.05726.x

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Cupiennin 1a (GFGALFKFLAKKVAKTVAKQAAKQGAKYVVNKQME-NH2) is a potent venom component of the spider Cupiennius salei. Cupiennin 1a shows multifaceted activity. In addition to known antimicrobial and cytolytic properties, cupiennin 1a inhibits the formation of nitric oxide by neuronal nitric oxide synthase at an IC50 concentration of 1.3 +/- 0.3 microM. This is the first report of neuronal nitric oxide synthase inhibition by a component of a spider venom. The mechanism by which cupiennin 1a inhibits neuronal nitric oxide synthase involves complexation with the regulatory protein calcium calmodulin. This is demonstrated by chemical shift changes that occur in the heteronuclear single quantum coherence spectrum of 15N-labelled calcium calmodulin upon addition of cupiennin 1a. The NMR data indicate strong binding within a complex of 1 : 1 stoichiometry.

Item Type:

Journal Article (Original Article)

Division/Institute:

08 Faculty of Science > Department of Biology > Institute of Ecology and Evolution (IEE) > Community Ecology

UniBE Contributor:

Kuhn-Nentwig, Lucia

Subjects:

500 Science > 570 Life sciences; biology
500 Science > 590 Animals (Zoology)
500 Science > 580 Plants (Botany)

ISSN:

1742-464X

Publisher:

Wiley-Blackwell

Language:

English

Submitter:

Factscience Import

Date Deposited:

04 Oct 2013 14:58

Last Modified:

24 Mar 2014 04:05

Publisher DOI:

10.1111/j.1742-4658.2007.05726.x

PubMed ID:

17313650

Web of Science ID:

000244883400014

URI:

https://boris.unibe.ch/id/eprint/24811 (FactScience: 52976)

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