Caged cysteine and thiophosphoryl peptides.

P Pan; H Bayley

doi:10.1016/s0014-5793(97)00165-8

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Caged cysteine and thiophosphoryl peptides.

P Pan·H Bayley

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Abstract

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 0.064-0.62 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.

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Cysteine Oligopeptides Organophosphorus Compounds Peptides Phosphoprotein Phosphatases Photolysis Ultraviolet Rays Journal Article Research Support, U.S. Gov't, Non-P.H.S.Research Support, U.S. Gov't, P.H.S.

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P Pan, H Bayley. 1997-03-17. Caged cysteine and thiophosphoryl peptides.. https://doi.org/10.1016/s0014-5793(97)00165-8

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