Caged cysteine and thiophosphoryl peptides.
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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Worcester Foundation for Biomedical Research, Shrewsbury, MA 01545, USA.
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D003545:Cysteine / Q000737:chemistry*; D009842:Oligopeptides / Q000737:chemistry; D009943:Organophosphorus Compounds / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry*; D010749:Phosphoprotein Phosphatases / Q000378:metabolism; D010782:Photolysis; D014466:Ultraviolet Rays
D009842:Oligopeptides; D009943:Organophosphorus Compounds; D010455:Peptides; C037642:kemptide; D010749:Phosphoprotein Phosphatases; D003545:Cysteine