Issue Date: December 5, 2011
Foldamers Mimic Disordered Proteins
Foldamers are synthetic oligomers that can adopt an ordered structure in solution. By covalently linking synthetic polymers to the ends of a foldamer, Jeffrey S. Moore and Koushik Ghosh of the University of Illinois, Urbana-Champaign, report they can cause the foldamer to collapse into a helical structure (J. Am. Chem. Soc., DOI: 10.1021/ja2087163). Such systems could be used as models to investigate the fundamental macromolecular physics of intrinsically disordered proteins (IDPs), the researchers suggest. IDPs lack well-defined secondary and tertiary structure, but they can assist in structuring globular proteins. Moore and Ghosh mimicked an IDP using a phenylene-ethynylene dodecamer with poly(methyl acrylate) polymers covalently bound at both ends. Poly(methyl acrylate) chains larger than 50 kilodaltons cause the foldamer to adopt a helical structure, even in solvents that would normally denature it. Such behavior is observed only if the polymers are covalently linked to the dodecamer; simply physically mixing them together is not sufficient to induce structure. Moore and Ghosh propose that the polymers promote folding by altering the solvent environment around the foldamer.
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