Foldamers Mimic Disordered Proteins | Chemical & Engineering News
Volume 89 Issue 49 | p. 35 | Concentrates
Issue Date: December 5, 2011

Foldamers Mimic Disordered Proteins

Synthetic polymers tacked onto the ends of oligomer chains equilibrate between unstructured and helical conformations
Department: Science & Technology
News Channels: Biological SCENE, JACS In C&EN
Keywords: foldamers, intrinsically disordered proteins, protein structure
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A foldamer with attached polymer chains equilibrates between unstructured and helical conformations.
Credit: J. Am. Chem. Soc.
A diagram showing a foldamer with attached polymer chains equilibrates between unstructured and helical conformations.
 
A foldamer with attached polymer chains equilibrates between unstructured and helical conformations.
Credit: J. Am. Chem. Soc.

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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