A caged sperm-activating peptide that has a photocleavable protecting group on the backbone amide

被引：55

作者：

Tatsu, Y

Nishigaki, T

Darszon, A

Yumoto, N ^{[1
]}

机构：

[1] Univ Nacl Autonoma Mexico, Inst Biotecnol, Dept Genet & Fisiol Mol, Cuernavaca 62250, Morelos, Mexico

[2] Natl Inst Adv Ind Sci & Technol, AIST, Ikeda, Osaka 5638577, Japan

来源：

FEBS LETTERS | 2002年 / 525卷 / 1-3期

关键词：

caged peptide; speract; backbone amide; sperm;

D O I：

10.1016/S0014-5793(02)03000-4

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A backbone-caged sperm-activating peptide (caged speract) that has a 2-nitrobenzyl group at a backbone amide and a vastly reduced affinity for its receptor (IC50 = 950 nM) was synthesized. UV irradiation of caged speract photocleaves the 2-nitrobenzyl group (tau(1/2)= 26 mus), restoring its affinity (IC50 = 0.67 nM) and ability to increase sperm intracellular pH and Ca2+, as intact speract. Backbone caging of the biological activity was more efficient than side chain caging, which adds a nitrobenzyl group on the peptide side chain. The backbone caging strategy described can be used as a general procedure to cage biologically active peptides, which have no side chain for introduction of a caging group. (C) 2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.

引用

页码：20 / 24

页数：5

共 23 条

[1] ((9-FLUORENYLMETHYL)OXY)CARBONYL (FMOC) AMINO-ACID FLUORIDES - CONVENIENT NEW PEPTIDE COUPLING REAGENTS APPLICABLE TO THE FMOC/TERT-BUTYL STRATEGY FOR SOLUTION AND SOLID-PHASE SYNTHESES [J].