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Updated: Jan 15, 2026
Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
Published on: November 21, 2013
Conformational Analysis of Helical Peptides Incorporating Azepane-Based β-Amino Acids Prepared by an
Ingyu Han1, Chae Na Lim1, Soo Hyuk Choi1
1Department of Chemistry, Yonsei University, 50 Yonsei-Ro, Seodaemun-Gu, Seoul 03722, Republic of Korea.
Abstract:
We report the synthesis of cis-5-aminoazepane-4-carboxylic acid (cis-AAzC) and its conformational behavior in nontraditional helical peptides. An ultrasound-assisted reductive amination method improves chemical yields and reduces solvent usage compared with previous methods. Incorporation of cis-AAzC into unnatural peptides promotes the 11/9-helix in 1:1 α/β-peptides and the 12/10-helix in β-peptides with enhanced aqueous solubility. The circular dichroism and the crystal structure data for these peptides suggest that additional functionalization at the azepane moiety is tolerated without disrupting helical propensity.
