Abstract
This review discusses the development of the active site-directed protein tyrosine phosphatase (PTP) inhibitors based on peptides and some closely related nonpeptidic scaffolds. A straightforward approach is to substitute various nonhydrolyzable analogs for the phosphotyrosine (pTyr) of optimal or physiological phosphopeptide substrates of PTPs. The advances in small molecule peptidic PTP inhibitors and their nonpeptidic derivatives have been greatly aided by X-ray crystallographic and NMR spectrometric studies. Given the importance of PTPs in disease-associated signal transduction and the continuing progress in PTP drug discovery, some clinically useful PTP inhibitors may emerge in the near future.
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