Synthesis and peptide incorporation of an unnatural amino acid containing activity-based probe for protein tyrosine phosphatases

Kui Shen; Lixin Qi; Mohini Ravula; Krzysztof Klimaszewski

doi:10.1016/j.bmcl.2009.04.081

Synthesis and peptide incorporation of an unnatural amino acid containing activity-based probe for protein tyrosine phosphatases

Bioorg Med Chem Lett. 2009 Jun 15;19(12):3264-7. doi: 10.1016/j.bmcl.2009.04.081. Epub 2009 Apr 23.

Authors

Kui Shen¹, Lixin Qi, Mohini Ravula, Krzysztof Klimaszewski

Affiliation

¹ Northern Illinois University, Department of Chemistry and Biochemistry, DeKalb, IL 60115, USA. kshen@niu.edu

PMID: 19423347
DOI: 10.1016/j.bmcl.2009.04.081

Abstract

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acids / chemical synthesis*
Amino Acids / chemistry
Humans
Jurkat Cells
Molecular Probe Techniques
Molecular Probes / chemical synthesis*
Neoplasm Proteins
Peptides / chemistry*
Protein Tyrosine Phosphatase, Non-Receptor Type 1 / analysis
Protein Tyrosine Phosphatases / analysis*
Substrate Specificity

Substances

Amino Acids
Molecular Probes
Neoplasm Proteins
Peptides
PTP4A3 protein, human
PTPN1 protein, human
Protein Tyrosine Phosphatase, Non-Receptor Type 1
Protein Tyrosine Phosphatases