Cross-linking strategy for molecular recognition and fluorescent sensing of a multi-phosphorylated peptide in aqueous solution.
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.
Ojida
Akio
A
Department of Chemistry and Biochemistry, Graduate School of Engineering, Kyushu University, Fukuoka, 812-8581, Japan.
Inoue
Masa-aki
MA
Mito-Oka
Yasuko
Y
Hamachi
Itaru
I
D002942:Circular Dichroism; D003432:Cross-Linking Reagents / Q000737:chemistry*; D005456:Fluorescent Dyes / Q000737:chemistry*; D007700:Kinetics; D009942:Organometallic Compounds / Q000737:chemistry; D010748:Phosphopeptides / Q000032:analysis*; D017433:Protein Structure, Secondary; D012996:Solutions; D013050:Spectrometry, Fluorescence / Q000379:methods; D014867:Water / Q000737:chemistry; D015032:Zinc / Q000737:chemistry
D003432:Cross-Linking Reagents; D005456:Fluorescent Dyes; D009942:Organometallic Compounds; D010748:Phosphopeptides; D012996:Solutions; D014867:Water; D015032:Zinc