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

作者信息

Cavicchioni G, Spisani S

机构信息

Department of Pharmaceutical Sciences, University of Ferrara, Ferrara, Italy.

出版信息

J Pept Res. 2001 Sep;58(3):257-62. doi: 10.1034/j.1399-3011.2001.00917.x.

Abstract

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.

摘要

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