Conformational studies on peptides having dipropylglycine (Dpg) or 1-aminocycloheptanecarboxylic acid (Ac7 c) within the sequence of l-leucine (Leu) residues

Biopolymers
Makoto ObaMasakazu Tanaka

Abstract

A conformational analysis of peptides having dipropylglycine (Dpg) or 1-aminocycloheptanecarboxylic acid (Ac7 c) within l-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-containing l-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-containing l-Leu peptides adopted similar structures in solution. © 2016 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 106: 210-218, 2016.

References

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Sep 3, 2014·The Journal of Organic Chemistry·Makoto ObaMasakazu Tanaka
Jun 7, 2015·Bioorganic & Medicinal Chemistry·Makoto ObaMasakazu Tanaka

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Citations

Jul 6, 2017·Organic & Biomolecular Chemistry·Kaori FurukawaMasakazu Tanaka
Apr 2, 2019·Yakugaku zasshi : Journal of the Pharmaceutical Society of Japan·Makoto Oba

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