Interaction of basic amphiphilic polypeptide antimicrobials, gramicidin S, tyrocidin and efrapeptin with endotoxic lipid

David, A. S. A. ; Balaram, P. ; Mathan, V. I. (1992) Interaction of basic amphiphilic polypeptide antimicrobials, gramicidin S, tyrocidin and efrapeptin with endotoxic lipid Medical Microbiology Letters, 2 (1). pp. 42-47. ISSN 1018-4627

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Abstract

Gramicidin S, Tyrocidinand Efrapeptin, basic hydrophobic peptide antimicrobials, bind lipid A with apparent Kds is of 1.68 µM, 2.65 µM and 4.92 µM respectively, and inhibit lipid A activity in the Limulus amoebocyte lysate gelation and splenocyte proliferation assays.The results suggest that endotoxin binding properties may be a general property of cationic amphiphilic peptides.

Item Type:Article
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Deposited On:21 May 2012 08:41
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