1T51
Antibiotic Activity and Structural Analysis of a Scorpion-derived Antimicrobial peptide IsCT and Its Analogs
Summary for 1T51
| Entry DOI | 10.2210/pdb1t51/pdb |
| Related | 1T52 1T54 1T55 |
| NMR Information | BMRB: 6220 |
| Descriptor | Cytotoxic linear peptide IsCT (1 entity in total) |
| Functional Keywords | coil-helix, antibiotic |
| Biological source | Opisthacanthus madagascariensis |
| Cellular location | Secreted: Q8MMJ7 |
| Total number of polymer chains | 1 |
| Total formula weight | 1503.85 |
| Authors | Lee, K.,Shin, S.Y.,Kim, K.,Lim, S.S.,Hahm, K.S.,Kim, Y. (deposition date: 2004-05-01, release date: 2004-10-19, Last modification date: 2024-11-20) |
| Primary citation | Lee, K.,Shin, S.Y.,Kim, K.,Lim, S.S.,Hahm, K.S.,Kim, Y. Antibiotic activity and structural analysis of the scorpion-derived antimicrobial peptide IsCT and its analogs Biochem.Biophys.Res.Commun., 323:712-719, 2004 Cited by PubMed Abstract: 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. PubMed: 15369808DOI: 10.1016/j.bbrc.2004.08.144 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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