Conformational studies on peptides having dipropylglycine (Dpg) or 1‐aminocycloheptanecarboxylic acid (Ac7c) within the sequence of l‐leucine (Leu) residues. Issue 2 (March 2016)

• Record Type: Journal Article
• Authors: Oba, Makoto; Nonaka, Hikaru; Doi, Mitsunobu; Tanaka, Masakazu
• Is Part Of: Biopolymers. Volume 106:Issue 2(2016)
• Page Start: 210
• Page End: 218
• Publication Date: 2016-03
• Subjects: conformation -- peptides -- α, α‐disubstituted α‐amino acid -- helix; Biopolymers -- Periodicals; Peptides -- Periodicals; Spectrum analysis -- Periodicals; 572.33
• DOI: 10.1002/bip.22810
• Languages: English
• ISSNs: 0006-3525

Abstract

ABSTRACT: A conformational analysis of peptides having dipropylglycine (Dpg) or 1‐aminocycloheptanecarboxylic acid (Ac7 c) withinl ‐leucine (Leu) residues was conducted in solution and in a crystal state. Dpg and Ac7 c had similar structures with acyclic and cyclic side chains, respectively. FTIR, 1 H NMR, and CD spectra measurements revealed that the preferred conformations of Dpg‐ and Ac7 c‐containingl ‐Leu peptides in solution were similar; both had a right‐handed ( P ) 310 ‐helix. The Dpg‐containing octapeptide adopted a right‐handed ( P ) α‐helix in the crystal state. Dpg and Ac7 c homopeptides had planar and helical structures as their preferred conformations, respectively; however, Dpg‐ and Ac7 c‐containingl ‐Leu peptides adopted similar structures in solution. © 2016 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 106: 210–218, 2016.