通过N端截短增强神经肽Y的抗菌活性。
Enhancement of antimicrobial activity of neuropeptide Y by N-terminal truncation.
作者信息
Shimizu M, Shigeri Y, Tatsu Y, Yoshikawa S, Yumoto N
机构信息
Osaka National Research Institute, AIST, Ikeda, Osaka 563-8577, Japan.
出版信息
Antimicrob Agents Chemother. 1998 Oct;42(10):2745-6. doi: 10.1128/AAC.42.10.2745.
Abstract
The activity of neuropeptide Y (NPY) against Candida albicans, which was revealed to be fungicidal, was enhanced significantly by the truncation of amino acid residues at the N terminus. The most active peptides (MICs, approximately 1 microM) were about 10-fold more potent than the intact NPY (MIC, approximately 10 microM). The enhancement was weakened by the replacement of the N terminus by negatively charged residues and/or acylation of the alpha-amino group. These results suggest that only the alpha-helical region of NPY is necessary for the antimicrobial activity and that the net charge of the peptide is important for the activity.
摘要
神经肽Y（NPY）对白色念珠菌具有杀菌活性，N端氨基酸残基的截短可显著增强该活性。活性最强的肽（最小抑菌浓度约为1微摩尔/升）的效力比完整的NPY（最小抑菌浓度约为10微摩尔/升）高约10倍。用带负电荷的残基取代N端和/或α-氨基的酰化会削弱这种增强作用。这些结果表明，NPY的抗菌活性仅需要其α-螺旋区域，并且肽的净电荷对活性很重要。
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