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铜-淀粉样蛋白复合物催化的不对称迈克尔加成反应。

Asymmetric Michael addition catalysed by copper-amyloid complexes.

作者信息

Fujieda Nobutaka, Tonomura Atsushi, Mochizuki Tomofumi, Itoh Shinobu

机构信息

Department of Applied Biological Chemistry, Graduate School of Agriculture, Osaka Metropolitan University 1-1 Gakuen-cho, Naka-ku Sakai-shi Osaka 599-8531 Japan

Department of Molecular Chemistry, Division of Applied Chemistry, Graduate School of Engineering, Osaka University 2-1 Yamada-oka Suita Osaka 565-0871 Japan.

出版信息

RSC Adv. 2024 Jan 2;14(1):206-210. doi: 10.1039/d3ra07900g.

Abstract

We developed self-assembled peptides containing a partial amyloid β protein sequence and a metal-coordination site. The amyloid fibril-copper complexes exhibited excellent reactivity and moderate enantioselectivity in Michael addition reactions with 2-azachalcone and dimethylmalonate. The catalytic amyloids were characterized using various measurements to confirm their amyloid-like nanofibre structures.

摘要

我们开发了包含部分淀粉样β蛋白序列和金属配位位点的自组装肽。淀粉样纤维-铜复合物在与2-氮杂查耳酮和丙二酸二甲酯的迈克尔加成反应中表现出优异的反应活性和适度的对映选择性。使用各种测量方法对催化淀粉样蛋白进行表征,以确认其类淀粉样纳米纤维结构。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ece3/10759172/fbe85e727a3f/d3ra07900g-f1.jpg

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