@article{fc00ce8aa0ec459fa7c3c795ffb15d8c,
title = "Computational Ab Initio Interaction Analyses between Neutralizing Antibody and SARS-CoV-2 Variant Spike Proteins Using the Fragment Molecular Orbital Method",
abstract = "The interaction energies between the receptor-binding domain of SARS-CoV-2 spike proteins and neutralizing antibody CC12.1 Fab were calculated using the fragment molecular orbital method. South African and Brazilian variants showed weaker interactions than the wild-type. Mutations, K417N/T and E484K, were considered to be responsible for escape from the antibody.",
keywords = "Antibody, Fragment molecular orbital method, SARS-CoV-2 variant",
author = "Kazuki Watanabe and Chiduru Watanabe and Teruki Honma and Tian, {Yu Shi} and Yusuke Kawashima and Norihito Kawashita and Kaori Fukuzawa and Tatsuya Takagi",
note = "Funding Information: This work was supported by JSPS KAKENHI Grant Number (JP20K06987 and JP17K082350). Part of this research was conducted using the FMO drug design consortium (FMODD, https://fmodd.jp/). The FMO calculations were performed using the Oakforest-PACS supercomputer (project ID: hp200101). PIEDA calculations were performed using the MIZUHO/ BioStation software package. This research was partially supported by the Platform Project for Supporting Drug Discovery and Life Science Research [Basis for Supporting Innovative Drug Discovery and Life Science Research (BINDS)] from AMED under Grant Number JP20am0101113. C.W. acknowledges the support from JST PRESTO, Grant Number JPMJPR18GD, Japan. Y. S. T. acknowledges the support from Hirose International Scholarship Foundation research grant. Publisher Copyright: {\textcopyright} 2021 Chemical Society of Japan. All rights reserved.",
year = "2021",
month = jun,
day = "1",
doi = "10.1246/bcsj.20210104",
language = "English",
volume = "94",
pages = "1794--1798",
journal = "Bulletin of the Chemical Society of Japan",
issn = "0009-2673",
publisher = "Chemical Society of Japan",
number = "6",
}