Modification of the N-terminus of peptidomimetic protein tyrosine phosphatase 1B (PTP1B) inhibitors: identification of analogues with cellular activity.

Article Details

Citation

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
DrugTargetPropertyMeasurementpHTemperature (°C)
N-(3-Carboxypropanoyl)-L-phenylalanyl-3-carboxy-O-(carboxymethyl)-N-pentyl-L-tyrosinamideTyrosine-protein phosphatase non-receptor type 1Ki (nM)220N/AN/ADetails