Fig. 2: Biophysical characterization of synthetic helix-hairpin peptides. | Nature Chemical Biology

Fig. 2: Biophysical characterization of synthetic helix-hairpin peptides.

From: A dimeric proteomimetic prevents SARS-CoV-2 infection by dimerizing the spike protein

Fig. 2

a, Competitive inhibition of SARS-CoV-2 RBD binding to immobilized ACE2 by the peptides determined by SPR. b, The direct binding affinity of peptides to SARS-CoV-2 RBD was assessed by SPR. Data are depicted as mean from two separate experiments ± s.d. n.d.*, No dissociation. c, The thermal stability of peptide–RBD complex was monitored by nanoDSF. Two independent measurements were done for each sample. d, The binding stoichiometry of the peptide–RBD complex determined through SEC–MALS. e, Negative staining, the data analysis was carried out in three sets with independent purification of Spike–SIH-5 complex. f, Cryo-EM reference-free 2D class averages of spike (S) protein in the presence of SIH-5. The experiment was repeated twice with similar results. The scale bar represents 10 nm.

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