Tripeptides as selective inhibitors of src-SH2 phosphoprotein interactions
β Scribed by Marc Rodriguez; Renae Crosby; Krystal Alligood; Tona Gilmer; Judd Berman
- Book ID
- 104630501
- Publisher
- Springer Netherlands
- Year
- 1995
- Tongue
- English
- Weight
- 313 KB
- Volume
- 2
- Category
- Article
- ISSN
- 1573-3149
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β¦ Synopsis
This paper describes the synthesis of phosphorylated peptides of the general structure Ac-Tyr(PO3HR)-Glu-Xaa-NH 2, where Xaa represents a hydrophobic 7-amino acid of D-configuration. These peptides displayed activities in the micromolar range in inhibiting src-SH2 domain/epidermal growth factor receptor interactions.
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A number of epoxysuccinyl amino acid benzyl esters (HO-Eps-AA-OBzl, 1) in which the amino acid (AA) had been systematically varied were tested as inhibitors of cathepsins \(\mathrm{L}\) and S. These E-64 analogs were designed to investigate whether selectivity for cathepsin \(\mathbf{L}\) or catheps