Thermodynamic analysis of the interactions between human ACE2 and spike RBD of Betacoronaviruses (SARS-CoV-1 and SARS-CoV-2)

被引：7
作者：
Rombel-Bryzek, Agnieszka [1 ]
Miller, Adriana [2 ]
Witkowska, Danuta [3 ]
机构：
[1] Univ Opole, Inst Med Sci, Opole, Poland
[2] Univ Wroclaw, Fac Chem, Wroclaw, Poland
[3] Univ Opole, Inst Hlth Sci, Katowicka 68, PL-45060 Opole, Poland
来源：
FEBS OPEN BIO | 2023年 / 13卷 / 01期
关键词：
binding interactions; human ACE2; isothermal titration alorimetry; receptor-binding domain; SARS-CoV-1; SARS-CoV-2; RECEPTOR-BINDING; SARS-COV; PROTEIN; DOMAIN;
D O I：
10.1002/2211-5463.13525
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
There are many scientific reports on the interaction of the SARS-CoV-2 virus S protein (and its RBD) with the human ACE2 receptor protein. However, there are no reliable data on how this interaction differs from the interaction of the receptor binding domain of SARS-CoV-1 with ACE2, in terms of binding strength and changes in reaction enthalpy and entropy. Our studies have revealed these differences and the impact of zinc ions on this interaction. Intriguingly, the binding affinity of both RBDs (of SARS-CoV-1 and of SARS-CoV-2) to the ACE2 receptor protein is almost identical; however, there are some differences in the entropic and enthalpic contributions to these interactions.
引用
收藏
页码：174 / 184
页数：11
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