Highly sensitive peptide-based probes for protein tyrosine phosphatase activity utilizing a fluorogenic mimic of phosphotyrosine.
Fluorescent probes that can be incorporated into peptides and proteins are in high demand, with applications ranging from cellular imaging to binding and activity assays. Here, we report the high yielding synthesis of an enantiomerically pure phosphocoumarin-based amino acid and its incorporation into peptides via standard solid-phase peptide synthesis methodologies. Peptides containing this new amino acid serve as highly sensitive fluorogenic probes for protein tyrosine phosphatase activity.
Mitra
Sayantan
S
Department of Chemistry, University of Southern California, Los Angeles, CA 90089, USA.
Barrios
Amy M
AM
D003374:Coumarins / Q000737:chemistry*; D005456:Fluorescent Dyes / Q000737:chemistry*; D006801:Humans; D018716:Molecular Mimicry; D009943:Organophosphorus Compounds / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry; D019000:Phosphotyrosine / Q000737:chemistry; D017027:Protein Tyrosine Phosphatases / Q000032:analysis* / Q000378:metabolism; D012680:Sensitivity and Specificity
D003374:Coumarins; D005456:Fluorescent Dyes; D009943:Organophosphorus Compounds; D010455:Peptides; D019000:Phosphotyrosine; D017027:Protein Tyrosine Phosphatases