Inhibition of SARS-CoV-2 infection (previously 2019-nCoV) by a highly potent pan-coronavirus fusion inhibitor targeting its spike protein that harbors a high capacity to mediate membrane fusion

Shuai Xia; Meiqin Liu; Chao Wang; Wei Xu; Qiaoshuai Lan; Siliang Feng; Feifei Qi; Linlin Bao; Lanying Du; Shuwen Liu; Chuan Qin; Fei Sun; Zhengli Shi; Yun Zhu; Shibo Jiang; Lu Lu

However, the mechanism of this enhancement, especially the role of cholesterol group 403 in the C-terminal tail of entry inhibitor, is still unclear. There is a possibility that the 404 cholesterol group could anchor to the target membrane to facilitate the binding of 405 inhibitor to the HR1 targets. However, we noticed that binding affinity between 406 EK1C4 and SARS-CoV-2-HR1P is significantly enhanced than EK1 peptide alone, 407 which suggested that cholesterol group may be involved in binding to HR1P directly 408 (Fig. S4) . Therefore, using structural simulation and docking method, we predicted a 409 possible model of EK1C4 in binding with SARS-CoV-2 HR1P (Fig. S8) . In this The copyright holder for this preprint (which was not peer-reviewed) is the . https://doi.org/10.1101/2020.03.09.983247 doi: bioRxiv preprint