Publication | Closed Access
Cross-Linking Strategy for Molecular Recognition and Fluorescent Sensing of a Multi-phosphorylated Peptide in Aqueous Solution
108
Citations
9
References
2003
Year
Signal TransductionBiochemistryProtein FoldingNatural SciencesPeptide LibraryCross-linking StrategyMolecular BiologyPeptide SynthesisProtein EngineeringFluorescent SensingChemical ProbeMolecular RecognitionMedicineNon-peptide LigandBiophysics
In the research field of molecular recognition, selective recognition and sensing of phosphorylated protein surfaces is strongly desirable both for elucidation of protein-protein recognition at the molecular level and for regulation of signal transduction through protein surfaces. Here we describe a new strategy for molecular recognition of a multi-phosphorylated peptide using intrapeptide cross-linking on the basis of coordination chemistry. The present artificial receptor can selectively bind to doubly phosphorylated peptide through multiple-point interactions and fluorescently sense the binding event with an association constant of more than 106 M-1 in neutral aqueous solution.
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