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Fig 1.

SARS-CoV-2 receptor binding motif–ACE2 protein-protein interaction binding interface.

Amino acids in red highlight SARS-CoV-2 receptor binding motif (RBM) contact residues with ACE2.–adapted from (Lan, et al. 2020) [7]. ACE2 receptor–Grey. SARS-CoV-2 RBD–Orange. Green structures represent glycoproteins. Structure generated using PyMol software.

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Fig 1 Expand

Table 1.

Primers.

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Table 1 Expand

Fig 2.

Selecting a potential RBD–ACE2 PPI inhibitor peptide derived from SARS-CoV-2 RBM S438 –K462 peptide.

(A) N-terminal and (B) C-terminal stepwise truncation peptide array of RBM S438 –K462, overlaid with ACE2-Fc human purified protein. Underlined (blue) sequence represents shorter sequence peptide selected for assessment in vitro. (C) Structure of S443 –K458 SARS-CoV-2 RBM and the respective binding interface of ACE2 receptor; RBM interacting residues highlighted in red–adapted [7].

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Fig 3.

Selecting a potential RBD–ACE2 PPI inhibitor peptide derived from SARS-CoV-2 RBM E484 –Y508.

(A) N-terminal and (B) C-terminal stepwise truncation peptide array of RBM E484 –Y508, overlaid with ACE2-Fc human purified protein. Underlined (blue) sequence represents shorter sequence peptide selected for assessment in vitro. (C) ACE2 binding to short sequence RBM 20mer; F486 –Y505. (D) Structure of F486 –Y505 SARS-CoV-2 RBM and the respective binding interface of ACE2 receptor; RBM interacting residues highlighted in red–adapted [7].

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Fig 4.

Direct binding assay for ACE2 and RBM-derived peptides (FP; fluorescent polarisation).

Increasing concentrations of ACE2-Fc or GST purified recombinant protein (0.012 nM– 6 μM) were incubated with 500 nM of RBM peptide (FITC labelled) at room temperature, FP measured at 2 hours and binding affinities calculated via non-linear regression analysis (A). Binding saturation curves of (B) RBM1, (C) RBM2A and RBM2A-Sc, (D) RBM2B binding. GST represents negative protein control. Binding affinity (Kd, red vertical line) measurements represented as MEAN ± SEM, N = 3 independent experiments.

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Table 2.

ACE2 interacting SARS-CoV-2 RBM peptides.

Peptides synthesised with and without a C-terminal FITC tag.

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Table 2 Expand

Fig 5.

SRBD internalisation in human ACE2 overexpressing human cell lines.

(A) western immunoblot detection of internalised SRBD protein in ACE2 overexpressing (stable) A549 cells following 30 minutes pre-treatment with (i) vehicle only (lane 4), (ii) RBM2A-Sc (lane 5), (iii) RBM2A (lane 6), (iv) RBM2B (lane 7), (v) RBM1 (lane 8), RBM1 + RBM2B (lane 9). (B) Changes to SRBD mediated internalisation in transiently overexpressing ACE2 (luciferase) HEK293T cells were measured following co-treatment with SRBD (100 nM) and (i) RBM1, (ii) RBM2A, (iii) RBM2B peptides (0.5, 5 and 50 μM). Levels of internalised SRBD measured as % difference of vehicle only control. All data represented as MEAN ± SEM, N = 3 independent experiments. * P < 0.05, ** P < 0.01, *** P < 0.001, n.s. not significant.

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Fig 6.

Spike protein (full-length trimer, Wuhan-Hu-1 strain) pseudovirus neutralisation assay in human ACE2 overexpressing HEK293T cells.

RBM peptides were pre-treated (1 hour) at 300 μM, 100 μM, 30 μM, 10 μM, 3 μM and 1 μM, followed by 48-hour co-incubation with spike protein PsV (luciferase labelled) and subsequent luminescence detection. sACE2 (human ACE2 protein) represents positive PsV neutralisation control. Data represented as MEAN % difference of DMSO only negative control (100%) ± SEM, N = 3 independent experiments. PsV, Pseudovirus.

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Fig 7.

Effect of RBM peptides on recombinant S1 protein-induced inflammation in ACE2 endogenously expressing human coronary microvascular endothelial cells.

Total RNA extracted from CMEC and gene expression of (A) IL-1β, (B) IL-6, (C) VCAM-1, (D) MCP-1 pro-inflammatory markers determined via RT-PCR (normalised to GAPDH). RBM peptides treated alone (10 μM) or pre-treated (10 μM, 1 hour) following S1 protein 5-hour incubation (9 nM). Data represented as MEAN ± SEM, N ≥ 3 independent experiments. * P < 0.05, *** P < 0.001, **** P < 0.0001, n.s. not significant. C, Control; S1, spike protein S1 subunit; V, vehicle only control; 1, RBM1 peptide; 2B, RBM2B peptide; Sc, RBM2A-Scrambled peptide.

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