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Materials

Foldamers Mimic Disordered Proteins

Synthetic polymers tacked onto the ends of oligomer chains equilibrate between unstructured and helical conformations

by Celia Henry Arnaud
December 5, 2011 | A version of this story appeared in Volume 89, Issue 49

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Credit: J. Am. Chem. Soc.
A foldamer with attached polymer chains equilibrates between unstructured and helical conformations.
A diagram showing a foldamer with attached polymer chains equilibrates between unstructured and helical conformations.
Credit: J. Am. Chem. Soc.
A foldamer with attached polymer chains equilibrates between unstructured and helical conformations.

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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