2021年9月
Fragment molecular orbital based interaction analyses on complexes between SARS-CoV-2 RBD variants and ACE2
JAPANESE JOURNAL OF APPLIED PHYSICS
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- 巻
- 60
- 号
- 9
- 開始ページ
- 090901
- 終了ページ
- 090901
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.35848/1347-4065/ac1857
- 出版者・発行元
- IOP Publishing Ltd
The SARS-CoV-2 virus initiates infection of human cells by recognizing the human angiotensin-converting enzyme 2 (ACE2) with the receptor binding domain (RBD) of the viral spike protein. Thus, the variant of concern (VOC) with mutations on RBD is of special interest. Here, we present a series of interaction analyses for the RBD-ACE2 complex of the wild-type (PDB ID: 6M0J) and those of B.1.1.7 (alpha), B.1.351 (beta) and P.1 (gamma) VOCs, based on the fragment molecular orbital (FMO) calculations. The results revealed that the RBD variants have a higher affinity for ACE2 than the wild type does.
- リンク情報
- ID情報
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- DOI : 10.35848/1347-4065/ac1857
- ISSN : 0021-4922
- eISSN : 1347-4065
- ORCIDのPut Code : 98434649
- Web of Science ID : WOS:000684700300001