Abstract
The ant spider Lachesena tarabaevi produces one of the most potent venom that is largely composed of membrane active peptides. A group of seven linear antimicrobial peptides isolated from the venom of this spider which belong to the latarcin family are reported to be cytolytic and highly membrane active[1]. However, there is no single study where the secondary structure, membrane alignment of all peptides have been systematically addressed. Here, using circular dichroism(CD) spectroscopy, oriented CD, solid-state 15N-NMR and fluorescence spectroscopy, we have characterized the secondary structure and helix alignment of all seven peptides in their membrane-bound state [2].
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