Phosphorylation State-Responsive Lanthanide Peptide Conjugates: A Luminescence Switch Based on Reversible Complex Reorganization
- 25 May 2006
- journal article
- research article
- Published by American Chemical Society (ACS) in Organic Letters
- Vol. 8 (13) , 2723-2726
- https://doi.org/10.1021/ol060614u
Abstract
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.Keywords
This publication has 11 references indexed in Scilit:
- Fluoromorphic Substrates for Fatty Acid Metabolism: Highly Sensitive Probes for Mammalian Medium‐Chain Acyl‐CoA DehydrogenaseAngewandte Chemie International Edition in English, 2006
- Chemical approaches for investigating phosphorylation in signal transduction networksTrends in Cell Biology, 2005
- A New Fluorogenic Transformation: Development of an Optical Probe for Coenzyme QOrganic Letters, 2005
- Critical evaluation of stability constants of metal complexes of complexones for biomedical and environmental applications* (IUPAC Technical Report)Pure and Applied Chemistry, 2005
- Structural Origin of the High Affinity of a Chemically Evolved Lanthanide‐Binding PeptideAngewandte Chemie International Edition in English, 2004
- Being Excited by Lanthanide Coordination Complexes: Aqua Species, Chirality, Excited-State Chemistry, and Exchange DynamicsChemical Reviews, 2002
- Mono- and polymetallic lanthanide-containing functional assemblies: a field between tradition and noveltyChemical Society Reviews, 1999
- Imaging of cAMP‐dependent protein kinase activity in living neural cells using a novel fluorescent substrateFEBS Letters, 1997
- Pre-steady-state kinetics of the activation of rabbit skeletal muscle myosin light chain kinase by Ca2+/calmodulin.Journal of Biological Chemistry, 1992
- Lanthanide ion luminescence probes of the structure of biological macromoleculesAccounts of Chemical Research, 1981