Conformational studies on peptides having dipropylglycine (Dpg) or 1‐aminocycloheptanecarboxylic acid (Ac 7 c) within the sequence of  l ‐leucine (Leu) residues | Zendy

Oba Makoto | Zendy; aka Hikaru | Zendy; Doi Mitsunobu | Zendy; Tanaka Masakazu | Zendy

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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.

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