| Structural highlights
Function
[TXC1A_CUPSA] Has antimicrobial activity against B.subtilis, E.coli, E.faecalis, P.denitrificans, P.aeruginosa, P.putida, S.aureus, and S.epidermidis. Has insecticidal and hemolytic activities. Probably acts by disturbing membrane function with its amphipathic structure. Synergistically increases the insecticidal activity of CSTX-1, CSTX-9, and CSTX-13 by up to 65%. Also inhibits the formation of nitric oxide by neuronal nitric oxide synthase.[1] [2] [3] [4]
Publication Abstract from PubMed
The solution structure of cupiennin 1a, a 35 residue, basic antibacterial peptide isolated from the venom of the spider Cupiennius salei, has been determined by nuclear magnetic resonance (NMR) spectroscopy. The peptide was found to adopt a helix-hinge-helix structure in a membrane mimicking solvent. The hinge may play a role in allowing the amphipathic N-terminal helix and polar C-terminal helix to orient independently upon membrane binding, in order to achieve maximal antibacterial efficacy. Solid-state 31P and 2H NMR was used to further study the effects of cupiennin 1a on the dynamic properties of lipid membranes, using zwitterionic chain deuterated dimyristoylphosphatidylcholine (d54-DMPC) and anionic dimyristoylphosphatidylglycerol (DMPG) multilamellar vesicles. In d54-DMPC alone, cupiennin 1a caused a decrease in the 31P chemical shift anisotropy, indicating some interaction with the lipid head groups, and a decrease in order over the entire acyl chain. In contrast, for the mixed (d54-DMPC/DMPG) lipid system cupiennin 1a appeared to induce lateral separation of the two lipids as evidenced by the 31P spectra, in which the peptide preferentially interacted with DMPG. Little effect was observed on the deuterated acyl chain order parameters in the d54-DMPC/DMPG model membranes. Furthermore, 31P NMR relaxation measurements confirmed a differential effect on the lipid motions depending upon the membrane composition. Therefore, subtle differences are likely in the mechanism by which cupiennin 1a causes membrane lysis in either prokaryotic or eukaryotic cells, and may explain the specific spectrum of activity.
Solution structure and interaction of cupiennin 1a, a spider venom peptide, with phospholipid bilayers.,Pukala TL, Boland MP, Gehman JD, Kuhn-Nentwig L, Separovic F, Bowie JH Biochemistry. 2007 Mar 20;46(11):3576-85. Epub 2007 Feb 24. PMID:17319697[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kuhn-Nentwig L, Muller J, Schaller J, Walz A, Dathe M, Nentwig W. Cupiennin 1, a new family of highly basic antimicrobial peptides in the venom of the spider Cupiennius salei (Ctenidae). J Biol Chem. 2002 Mar 29;277(13):11208-16. Epub 2002 Jan 15. PMID:11792701 doi:http://dx.doi.org/10.1074/jbc.M111099200
- ↑ Haeberli S, Kuhn-Nentwig L, Schaller J, Nentwig W. Characterisation of antibacterial activity of peptides isolated from the venom of the spider Cupiennius salei (Araneae: Ctenidae). Toxicon. 2000 Mar;38(3):373-80. PMID:10669026
- ↑ Wullschleger B, Nentwig W, Kuhn-Nentwig L. Spider venom: enhancement of venom efficacy mediated by different synergistic strategies in Cupiennius salei. J Exp Biol. 2005 Jun;208(Pt 11):2115-21. PMID:15914655 doi:http://dx.doi.org/208/11/2115
- ↑ Pukala TL, Doyle JR, Llewellyn LE, Kuhn-Nentwig L, Apponyi MA, Separovic F, Bowie JH. 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 J. 2007 Apr;274(7):1778-84. Epub 2007 Feb 22. PMID:17313650 doi:http://dx.doi.org/10.1111/j.1742-4658.2007.05726.x
- ↑ Pukala TL, Boland MP, Gehman JD, Kuhn-Nentwig L, Separovic F, Bowie JH. Solution structure and interaction of cupiennin 1a, a spider venom peptide, with phospholipid bilayers. Biochemistry. 2007 Mar 20;46(11):3576-85. Epub 2007 Feb 24. PMID:17319697 doi:10.1021/bi062306+
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