A hydrophilic residue at position 2 can improve specific biological responses in fMLP-OMe analogs

被引:9
作者
Cavicchioni, G
Spisani, S
机构
[1] Univ Ferrara, Dipartimento Sci Farmaceut, I-44100 Ferrara, Italy
[2] Univ Ferrara, Dept Biochem & Mol Biol, I-44100 Ferrara, Italy
来源
JOURNAL OF PEPTIDE RESEARCH | 2001年 / 58卷 / 03期
关键词
chemotaxis; human neutrophils; lysozyme release; N-formylmethionyl peptides; superoxide anion generation;
D O I
10.1034/j.1399-3011.2001.00917.x
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
The peptides for-Met-Ser-Phe-OMe 1, for-Met-Cys-Phe-OMe 2, for-Met-Lys-Phe-OMe 3, and for-Met-Tyr-Phe-OMe 4 were synthesized in order to investigate the importance of a hydrophilic side-chain on the residue at position 2 on biological activities of human neutrophils. Our results seem to highlight that this type of substitution does not facilitate good chemotaxis, although it elicits both superoxide anion production and particularly lysozyme release, in some cases even more potent than the parent fMLP-OMe, if the hydrophilicity is associated with steric hindrance.
引用
收藏
页码:257 / 262
页数:6
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