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Conformational studies on peptides having dipropylglycine (Dpg) or 1‐aminocycloheptanecarboxylic acid (Ac 7 c) within the sequence of l ‐leucine (Leu) residues
Author(s) -
Oba Makoto,
aka Hikaru,
Doi Mitsunobu,
Tanaka Masakazu
Publication year - 2016
Publication title -
peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.22810
Subject(s) - chemistry , helix (gastropod) , leucine , stereochemistry , sequence (biology) , crystallography , crystal structure , amino acid residue , peptide , amino acid , peptide sequence , biochemistry , ecology , snail , biology , gene
A conformational analysis of peptides having dipropylglycine (Dpg) or 1‐aminocycloheptanecarboxylic acid (Ac 7 c) within l ‐leucine (Leu) residues was conducted in solution and in a crystal state. Dpg and Ac 7 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 Ac 7 c‐containing l ‐Leu peptides in solution were similar; both had a right‐handed ( P ) 3 10 ‐helix. The Dpg‐containing octapeptide adopted a right‐handed ( P ) α‐helix in the crystal state. Dpg and Ac 7 c homopeptides had planar and helical structures as their preferred conformations, respectively; however, Dpg‐ and Ac 7 c‐containing l ‐Leu peptides adopted similar structures in solution. © 2016 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 106: 210–218, 2016.