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对甲砜基杯[n]芳烃封端的银纳米粒子挑战了新型人肠道丝氨酸蛋白酶抑制剂的催化效率和稳定性。

para-Sulphonato-calix[n]arene capped silver nanoparticles challenge the catalytic efficiency and the stability of a novel human gut serine protease inhibitor.

机构信息

Micalis Institute, INRA, AgroParisTech, Université Paris-Saclay, F-78350 Jouy-en-Josas, France.

Laboratory of Molecular Biology of Eukaryotes, Center of Biotechnology of Sfax, University of Sfax, 3038, Sfax, Tunisia.

出版信息

Chem Commun (Camb). 2019 Aug 7;55(61):8935-8938. doi: 10.1039/c9cc03183a. Epub 2019 Jul 9.

Abstract

The Eubacterium saburreum serine protease inhibitor from the human gut microbiota inhibits the eukaryotic pancreatic elastase associated with acute pancreatitis. Interestingly, the inhibition efficiency and stability are markedly increased by the para-sulphonato-calix[8]arene capped silver nanoparticles. Moreover, this enzyme is distinguishable by its high inhibitory effect at broad pH range between 2-10 and temperatures from 10 to 40 °C, in the presence of para-sulphonato-calix[8]arene capped silver nanoparticles the enzyme remains active even at 70 °C.

摘要

人肠道微生物群中的真核菌丝氨酸蛋白酶抑制剂来源于埃希氏菌属,可抑制与急性胰腺炎相关的胰腺弹性蛋白酶。有趣的是,para-sulphonato-calix[8]arene 封端的银纳米粒子明显提高了抑制效率和稳定性。此外,该酶在 2-10 pH 值范围和 10-40°C 温度下具有很高的抑制效果,在 para-sulphonato-calix[8]arene 封端的银纳米粒子存在的情况下,即使在 70°C 时,该酶仍然保持活性。

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