Caged cysteine and thiophosphoryl peptides.
Caged cysteine and thiophosphoryl peptides.
复制标题
笼状半胱氨酸和硫代磷酰肽。
DOI：
10.1016/s0014-5793(97)00165-8
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发表时间：
1997
期刊：
影响因子：
3.5
通讯作者：
Bayley,H
中科院分区：
文献类型：
--
作者：
Pan,P;Bayley,H
Photoreleasable molecules are important in studies of various biological phenomena, especially cell signaling. Here we report a generally applicable approach for `caging' unprotected cysteine-containing or thiophosphorylated peptides in aqueous solution with 2-nitrobenzyl bromides. Photolysis of the caged peptides was achieved with near UV light with product quantum efficiencies of 0.06–0.62 under conditions that produced no damage to attendant biological macromolecules. Yields of uncaged peptides were 55–70%. Selective reaction of the side-chain of thiophosphoryl serine with 2-nitrobenzyl bromide in the presence of a cysteinyl residue was also demonstrated, establishing a means for functional caging of various signal transduction proteins without prior modification or mutagenesis. © 1997 Federation of European Biochemical Societies.
