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一种合成抗菌肽P18及其截短肽的结构与杀菌活性

Structure and fungicidal activity of a synthetic antimicrobial peptide, P18, and its truncated peptides.

作者信息

Lee Dong Gun, Hahm Kyung-Soo, Shin Song Yub

机构信息

School of Life Science and Biotechnology, College of Natural Sciences, Kyungpook National University, 1370 Sankyuk-dong, Puk-ku, Taegu 702-701, Korea.

出版信息

Biotechnol Lett. 2004 Feb;26(4):337-41. doi: 10.1023/b:bile.0000015472.09542.6d.

Abstract

P18 (KWKLFKKIPKFLHLAKKF-NH2) is an antimicrobial peptide designed from a cecropin A-magainin 2 hybrid that has potent antibacterial activity without hemolytic activity against human erythrocytes. In this study, P18 displayed potent fungicidal activity (MIC: 12.5 approximately 25 microM) against pathogenic fungi, Candida albicans, Trichosporon beigelii, Aspergillus flavus and Fusarium oxyspovrum. The central Pro9 residue and the entire sequence of P18 are essential for its full fungicidal activity. Circular dichroism analysis suggested that the higher alpha-helical content of the peptides did not correlate with the stronger fungicidal activity.

摘要

P18(KWKLFKKIPKFLHLAKKF-NH2)是一种由天蚕素A-蛙皮素2杂合体设计而成的抗菌肽,对人类红细胞具有强大的抗菌活性且无溶血活性。在本研究中,P18对致病性真菌白色念珠菌、白吉利丝孢酵母、黄曲霉和尖孢镰刀菌显示出强大的杀真菌活性(最低抑菌浓度:约12.5至25微摩尔)。P18的中心Pro9残基及其整个序列对其完全杀真菌活性至关重要。圆二色性分析表明,肽的较高α-螺旋含量与较强的杀真菌活性无关。

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