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• W1976024477 abstract "A series of conformationally constrained peptides were designed and synthesized as the Src SH2 domain ligands based on a tetrapeptide sequence pTyr-Glu-Glu-Ile (pYEEI). In general, the constrained peptides such as compounds 6, 7, and 11 (IC(50) = 1.1-1.5 microM) showed higher binding affinities to the Src SH2 domain relative to the corresponding linear peptides 8a, 9a, and 13a, respectively (IC(50) > 100 microM), and pYEEI (IC(50) = 6.5 microM), as evaluated by a fluorescence polarization assay. Molecular modeling studies revealed that in constrained peptides, the isoleucine side chain penetrates very deeply into the hydrophobic binding pocket (P + 3 site) of the Src SH2 domain. These constrained peptides can serve as novel templates for the design of small and nonpeptidic inhibitors of the Src SH2 domain." @default.
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• W1976024477 date "2004-05-11" @default.
• W1976024477 modified "2023-10-17" @default.
• W1976024477 title "Conformationally Constrained Peptide Analogues of pTyr-Glu-Glu-Ile as Inhibitors of the Src SH2 Domain Binding" @default.
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• W1976024477 doi "https://doi.org/10.1021/jm040008+" @default.
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