1T55

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

1T55 の概要

• エントリーDOI: 10.2210/pdb1t55/pdb
• 関連するPDBエントリー: 1T51 1T52 1T54
• NMR情報: BMRB: 6217
• 分子名称: Cytotoxic linear peptide IsCT (1 entity in total)
• 機能のキーワード: coil-helix, antibiotic
• 由来する生物種: Opisthacanthus madagascariensis
• 細胞内の位置: Secreted: Q8MMJ7
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 1586.08

構造登録者

Lee, K.,Shin, S.Y.,Kim, K.,Lim, S.S.,Hahm, K.S.,Kim, Y. (登録日: 2004-05-02, 公開日: 2004-10-19, 最終更新日: 2024-11-13)

主引用文献

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

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: 15369808
DOI: 10.1016/j.bbrc.2004.08.144

実験手法

SOLUTION NMR