Ionic polypeptides with unusual helical stability

Hua Lu, Jing Wang, Yugang Bai, Jason W. Lang, Shiyong Liu, Yao Lin () and Jianjun Cheng ()
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Hua Lu: University of Illinois at Urbana-Champaign
Jing Wang: Polymer Program, Institute of Materials Science, University of Connecticut
Yugang Bai: University of Illinois at Urbana-Champaign
Jason W. Lang: University of Illinois at Urbana-Champaign
Shiyong Liu: CAS Key Laboratory of Soft Matter Chemistry, Hefei National Laboratory for Physical Sciences at Microscale, University of Science and Technology of China
Yao Lin: Polymer Program, Institute of Materials Science, University of Connecticut
Jianjun Cheng: University of Illinois at Urbana-Champaign

Nature Communications, 2011, vol. 2, issue 1, 1-9

Abstract: Abstract Water-soluble peptides that adopt stable helical conformations are attractive motifs because of their importance in basic science and their broad utility in medicine and biotechnology. Incorporating charged amino-acid residues to improve peptide solubility, however, usually leads to reduced helical stability because of increased side-chain charge repulsion, reduced side-chain hydrophobicity and the disruption of intramolecular hydrogen bonding. Here, we show that water-soluble, ultra-stable α-helical polypeptides can be produced by elongating charge-containing amino-acid side chains to position the charges distally from the polypeptide backbone. The strategy has been successfully applied to the design and synthesis of water-soluble polypeptides bearing long, charged side chains and various functional moieties that possess unusual helical stability against changing environmental conditions, including changes in the pH and temperature and the presence of denaturing reagents.

Date: 2011
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DOI: 10.1038/ncomms1209

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