553668-06-7Relevant articles and documents
Modification of the N-terminus of peptidomimetic protein tyrosine phosphatase 1B (PTP1B) inhibitors: Identification of analogues with cellular activity
Larsen, Scott D.,Stevens, F. Craig,Lindberg, Thomas J.,Bodnar, Paul M.,O'Sullivan, Theresa J.,Schostarez, Heinrich J.,Palazuk, Barbara J.,Bleasdale, John E.
, p. 971 - 975 (2003)
Low molecular weight peptidomimetic compounds based on O-malonyl tyrosine and O-carboxymethyl salicylic acid are potent inhibitors of PTP1B. Modifications of the N-terminal Boc-Phe moiety were undertaken in an effort to improve physical chemical properties and to achieve cellular activity. Although Phe ultimately proved to be the optimal N-terminal amino acid, several viable replacements for the Boc group were identified, two of which afforded analogues that were effective at enhancing the insulin-stimulated uptake of 2-deoxyglucose by L6 myocytes.
