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Selective protein-protein interactions driven by a phenylalanine interface.

Nicholas C Yoder·Krishna Kumar
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Abstract

Highly specific protein-protein interfaces have been the subject of considerable study for their potential utility in disrupting or interrogating cellular signaling and control networks. We report that coiled-coil sequences decorated with phenylalanine core residues fold into stable alpha-helical bundles and that these self-sort from similar peptide assemblies with aliphatic core side chains. For self-assembled ensembles derived from 30-residue monomeric peptides, the DeltaG of specificity is -1.5 kcal/mol, comparable with earlier self-sorting coiled-coil systems. Intriguingly, although this interface is constructed from canonical amino acids, it does not appear to have been exploited in native proteins.

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Amino Acid SequenceCircular DichroismMolecular Sequence DataPeptidesPhenylalanineProtein ConformationSubstrate SpecificityThermodynamicsJournal ArticleResearch Support, N.I.H., ExtramuralResearch Support, Non-U.S. Gov'tResearch Support, U.S. Gov't, Non-P.H.S.

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Nicholas C Yoder, Krishna Kumar. 2006-01-11. Selective protein-protein interactions driven by a phenylalanine interface.. https://doi.org/10.1021/ja055494k

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