Modification of the N-terminus of peptidomimetic protein tyrosine phosphatase 1B (PTP1B) inhibitors: identification of analogues with cellular activity.
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Larsen SD, Stevens FC, Lindberg TJ, Bodnar PM, O'Sullivan TJ, Schostarez HJ, Palazuk BJ, Bleasdale JE
Modification of the N-terminus of peptidomimetic protein tyrosine phosphatase 1B (PTP1B) inhibitors: identification of analogues with cellular activity.
Bioorg Med Chem Lett. 2003 Mar 10;13(5):971-5.
- PubMed ID
- 12617932 [ View in PubMed]
- Abstract
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.
DrugBank Data that Cites this Article
- Binding Properties
Drug Target Property Measurement pH Temperature (°C) N-(3-Carboxypropanoyl)-L-phenylalanyl-3-carboxy-O-(carboxymethyl)-N-pentyl-L-tyrosinamide Tyrosine-protein phosphatase non-receptor type 1 Ki (nM) 220 N/A N/A Details