ASSESSING THE DRUGABILITY OF PTP1B NON-CATALYTIC SITES WITH MASS SPECTROMETRY

摘要

The identification of therapeutic inhibitors for protein tyrosine phosphatase 1B (PTP1B) is an attractive approach to treat type II diabetes, but it has failed so far due to insufficient selectivity [1]. Covalent inhibitors that target residues only present in PTP1B might overcome these limitations. We studied the reactivity of cysteines in PTP1B and designed and characterized potential ligands.