Stabilization of 11/9-helical α/β-peptide foldamers in protic solvents

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 aci...

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Veröffentlicht in:	Chemical communications (Cambridge, England) England), 2016-05, Vol.52 (35), p.5950-5952
Hauptverfasser:	Lee, Mihye, Shim, Jihyun, Kang, Philjae, Choi, Moon-Gun, Choi, Soo Hyuk
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acids - chemistry Analogue Cyclohexanecarboxylic Acids - chemistry Cyclohexylamines - chemistry Folding Models, Molecular Peptides - chemistry Polarity Protein Conformation, alpha-Helical Protein Folding - drug effects Protein Stability - drug effects Residues Solvents Solvents - chemistry Solvents - pharmacology Stabilization
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Beschreibung
Zusammenfassung:	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.
ISSN:	1359-7345 1364-548X
DOI:	10.1039/c6cc01189f