Synthesis and peptide incorporation of an unnatural amino acid containing activity-based probe for protein tyrosine phosphatases.
An unnatural amino acid was synthesized to incorporate a quinone methide-generating activity-based probe for protein tyrosine phosphatases (PTPs) and then integrated into a PTP1B-specific substrate. The resulting probe led to preferential labeling of PTP1B in cell lysates in the presence of PTP4A3.
Shen
Kui
K
Northern Illinois University, Department of Chemistry and Biochemistry, DeKalb, IL 60115, USA. kshen@niu.edu
Qi
Lixin
L
Ravula
Mohini
M
Klimaszewski
Krzysztof
K
D000596:Amino Acids / Q000138:chemical synthesis* / Q000737:chemistry; D006801:Humans; D019169:Jurkat Cells; D015336:Molecular Probe Techniques; D015335:Molecular Probes / Q000138:chemical synthesis*; D009363:Neoplasm Proteins; D010455:Peptides / Q000737:chemistry*; D054562:Protein Tyrosine Phosphatase, Non-Receptor Type 1 / Q000032:analysis; D017027:Protein Tyrosine Phosphatases / Q000032:analysis*; D013379:Substrate Specificity
D000596:Amino Acids; D015335:Molecular Probes; D009363:Neoplasm Proteins; D010455:Peptides; C484730:PTP4A3 protein, human; C516607:PTPN1 protein, human; D054562:Protein Tyrosine Phosphatase, Non-Receptor Type 1; D017027:Protein Tyrosine Phosphatases