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Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
Published on: November 21, 2013
Stabilization of 11/9-helical α/β-peptide foldamers in protic solvents
Mihye Lee1, Jihyun Shim, Philjae Kang
1Department of Chemistry, Yonsei University, Seoul, 03722, Republic of Korea. sh-choi@yonsei.ac.kr.
Abstract:
α/β-Peptides with alternating α-amino acid and cis-2-aminocyclohexanecarboxylic acid (cis-ACHC) residues adopt 11/9-helical conformations, the folding propensity of which decreases as the solvent polarity increases. We report a new cis-ACHC analogue, cis-2-amino-cis-4-methylcyclohexanecarboxylic acid, which significantly stabilizes the 11/9-helix propensity in protic solvents.
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