1t52 | pdb_00001t52

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

spinqualitylabelsall models 1t52, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1t52 is a 1 chain structure with sequence from Opima. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. NonStd Res: NH2 Related: 1t51, 1t54, 1t55 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [NDB52_OPIMA] Cytotoxic linear peptide IsCT: shows weak hemolytic activity and antibacterial activity against both Gram-positive and Gram-negative bacteria probably by forming pores in the cell membrane. IsCT adopts an amphipathic alpha-helical structure. Cytotoxic linear peptide IsCTf: shows neither hemolytic, nor antibacterial activities, probably because it cannot adopt amphipathic alpha-helical structure. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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