Journal
ORGANIC LETTERS
Volume 8, Issue 13, Pages 2723-2726Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ol060614u
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- NHGRI NIH HHS [HG002806] Funding Source: Medline
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A luminogenic probe for peptide dephosphorylation has been developed. It consists of a serine-/tyrosine-containing peptide modified on the N-terminus with a tryptophan residue and a DTPA chelate capable of binding Tb3+. We propose a mechanistic model for the luminescence enhancement based on the interconversion of monomeric and dimeric lanthanide species, which is affected by the phosphorylation state of the serine or tyrosine residue. The optical switch reports effectively on phosphatase-catalyzed dephosphorylation in vitro.
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