1t54

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Antibiotic Activity and Structural Analysis of a Scorpion-derived Antimicrobial peptide IsCT and Its Analogs

Overview

IsCT is a non-cell-selective antimicrobial peptide isolated from the, scorpion Opisthacanthus madagascariensis that has potent cytolytic, activity against both mammalian and bacterial cells. To investigate the, structure-activity relationships of IsCT and to design novel peptide, antibiotics with bacterial cell selectivity, we synthesized several, analogs of IsCT and determined their three-dimensional structures in, solution by 2D-NMR spectroscopy. IsCT has a linear alpha-helical structure, from Gly3 to Phe13, and [K7]-IsCT has a linear alpha-helical structure, from Leu2 to Phe13. [K7, P8, K11]-IsCT, which has a bend in its middle, region, exhibited the highest antibacterial activity without hemolytic, activity, suggesting that its proline-induced bend is an important, determinant of this selectivity. Tryptophan fluorescence showed that the, high selectivity of [K7, P8, K11]-IsCT toward bacterial cells is closely, correlated with its highly selective interaction with negatively charged, phospholipids. Its potent activity against antibiotic-resistant bacteria, suggests that [K7, P8, K11]-IsCT may serve as a promising lead candidate, in the development of new peptide antibiotics.

About this Structure

1T54 is a Single protein structure of sequence from Opisthacanthus madagascariensis with NH2 as ligand. Full crystallographic information is available from OCA.

Reference

Antibiotic activity and structural analysis of the scorpion-derived antimicrobial peptide IsCT and its analogs., Lee K, Shin SY, Kim K, Lim SS, Hahm KS, Kim Y, Biochem Biophys Res Commun. 2004 Oct 15;323(2):712-9. PMID:15369808

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