Hosted by: Ignace Jarrige

SARS-CoV-2 uses a common viral strategy for fusing the viral envelope with a host cell membrane. The resulting fusion event is paramount to the infection process and this common strategy is known as a type I viral fusion mechanism. The energetically unfavorable membrane fusion event is driven by a large conformational change of the spike protein that occurs when the spike protein comes into contact with its target receptor on the host cell surface. One possible way to prevent this viral fusion event involves disrupting this conformational change by blocking the formation of the 6 helix bundle complex formed by the spike protein with synthetic polypeptide inhibitors. In this talk I will discuss preliminary structures of these polypeptide inhibitors in complex with fragments of the SARS-CoV-2 spike protein that were obtained at NSLS-II during min-safe operations. These structures provide some insight into important design considerations for future generation of SARS-CoV-2 membrane fusion inhibitors.