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• W2090909356 abstract "Molecules that bind to specific surface sites on proteins are of great interest from both fundamental and practical perspectives. We are exploring a ligand development strategy that is based on oligomers with discrete folding propensities (“foldamers”); we target a specific cleft on the cancer-associated protein Bcl-xL because this system is well characterized structurally. In vivo, this cleft binds to α-helical segments (BH3 domains) of other proteins. We evaluated several types of helical foldamer, built entirely from β-amino acid residues or from mixtures of α- and β-amino acid residues, and ultimately identified foldamers in the latter class that bind very tightly to Bcl-xL. Our results suggest that combining different types of foldamer backbones will be an effective and general strategy for creating high-affinity and specific ligands for protein surface sites." @default.
• W2090909356 created "2016-06-24" @default.
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• W2090909356 date "2005-08-01" @default.
• W2090909356 modified "2023-10-16" @default.
• W2090909356 title "Chimeric (α/β + α)-Peptide Ligands for the BH3-Recognition Cleft of Bcl-x_L: Critical Role of the Molecular Scaffold in Protein Surface Recognition" @default.
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• W2090909356 doi "https://doi.org/10.1021/ja053678t" @default.
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• W2090909356 hasPublicationYear "2005" @default.
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