Skip to main content
. 2021 Aug 2;12(4):1652–1661. doi: 10.1016/j.apsb.2021.07.026

Figure 1.

Figure 1

Design of the dePEGylated lipopeptide-based pan-CoV fusion inhibitors. (A) Schematic representation of spike (S) protein of a human coronavirus (HCoV). Signal peptide (SP), N-terminal domain (NTD), receptor-binding domain (RBD), fusion peptide (FP), heptad repeat 1 (HR1) domain, HR2 domain, transmembrane domain (TM), and cytoplasmic domain (CP). (B) a: The model of interaction of a lipopeptide-based pan-CoV fusion inhibitor with the HR1 domain in S protein of an HCoV. b: PEG spacer as a flexible linker allowing the lipopeptide to overcome steric hindrance after binding. c: Replacement of the PEG linker with natural amino acids in the HR2 C-terminal fragment (HR2-CF) to facilitate the binding of dePEGylated lipopeptide to the primary binding site in the HR1 domain of viral S protein. (C) Sequence alignment of conserved HR2 sequences of several HCoVs. (D) Amino acid sequences of the dePEGylated lipopeptides and their corresponding peptides without lipid groups, and those of EK1 and EK1C4.