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.
Northern Illinois University, Department of Chemistry and Biochemistry, DeKalb, IL 60115, USA. kshen@niu.edu
Kui
K
Shen
Lixin
L
Qi
Mohini
M
Ravula
Krzysztof
K
Klimaszewski
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