Molecular assembly formation of cyclic hexa-β-peptide composed of acetylated glycosamino acids
✍ Scribed by Tatsuya Hirata; Futoshi Fujimura; Yoshiki Horikawa; Junji Sugiyama; Tomoyuki Morita; Shunsaku Kimura
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 2007
- Tongue
- English
- Weight
- 279 KB
- Volume
- 88
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
Abstract
A novel cyclic hexamer of acetylated β‐glycosamino acid was synthesized and its conformation and molecular assembly formation was investigated. Variable temperature NMR study indicated that the cyclic hexapeptide took a C~3~ symmetric conformation at room temperature, but at elevated temperatures a C~6~ symmetric one, which was not due to averaging of the C~3~ symmetric conformation, appeared. Computational geometry optimization showed that the C~6~ symmetric conformation was a highly planar structure with amide groups orienting perpendicular to the ring plane. The cyclic hexa‐β‐peptide formed rod‐shaped crystals from an N,N‐dimethyl formamide solution at elevated temperature. The optical microscopy observation with a sensitive tint plate under cross‐nicol configuration and electron diffraction analysis of the crystals revealed that the cyclic hexa‐β‐peptides were stacked one after the other to form a regular nanotube structure. © 2007 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 88: 150–156, 2007.
This article was originally published online as an accepted preprint. The ‘Published Online’ date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at [email protected]