2025-04-03 東京科学大学
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- https://www.isct.ac.jp/ja/news/jc6ehxh85qn4#top
- https://www.isct.ac.jp/plugins/cms/component_download_file.php?type=2&pageId=&contentsId=1&contentsDataId=1249&prevId=&key=b44df40f68838df170db011f5b776a09.pdf
- https://pubs.acs.org/doi/10.1021/jacs.5c01458
金属-ペプチドトーラス構造のらせん方向制御による Ag 21 L 14編組ペプチドナノチューブの折り畳みと組み立て Helical Sense Control of Metal–Peptide Torus Frameworks Leading to the Folding and Assembly of a Ag21L14 Braided Peptide Nanotube
Sota Oguma,Yuuki Inomata,Akihiro Hayakawa,Takahiro Nakama,Makoto Fujita,and Tomohisa Sawada
Journal of the American Chemical Society Published: March 6, 2025
DOI:https://doi.org/10.1021/jacs.5c01458
Abstract
The chirality of helical polypeptides is correlated to that of their constituent amino acid residues. For polypeptides with non-natural backbones, however, such correlations are less clear. Here, circular double helices with torus knot/link topologies were assembled from non-natural metal–peptide chains composed of Ag(I) ions and ditopic tripeptides with Gly-Gly-Ala and Gly-Ala-Gly sequences. We found that the chirality of the assembled helical structures is determined by the l-Ala’s dihedral angles. A tubular dimeric structure with an M21L14 composition was further achieved via additional metal cross-linking, showing rational design potential for artificial peptide helices.