Abstract
[reaction: see text] 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 Tb(3+). 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.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Alkaline Phosphatase / metabolism*
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Amino Acid Sequence
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Lanthanoid Series Elements / chemistry*
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Luminescence*
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Luminescent Measurements / methods
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Models, Molecular
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Pentetic Acid / chemistry
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Peptides / chemical synthesis
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Peptides / chemistry*
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Peptides / metabolism
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Phosphorylation
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Serine / chemistry
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Terbium / chemistry
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Tryptophan / chemistry
Substances
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Lanthanoid Series Elements
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Peptides
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Terbium
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Serine
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Pentetic Acid
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Tryptophan
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Alkaline Phosphatase