ArticleFrontiers in pharmacology2025
Identification of a novel dual-targeting peptide inhibitor of SARS-CoV-2 RBD and NRP1 through structure-based virtual screening.
Article in Frontiers in pharmacology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Background: The continuous mutations of SARS-CoV-2 have enhanced its transmissibility and immune escape capabilities. Its invasion into cells relies on the binding of the receptor-binding domain (RBD) of the spike (S) protein to host receptors, while NRP1, as a key host cofactor, promotes viral attachment and internalization by recognizing the S protein. Therefore, dual targeting of RBD and NRP1 represents a potentially effective antiviral strategy. Methods: In this study, a multi-step screening strategy combining molecular docking, MST assays, molecular dynamics simulations, pseudovirus neutralization assays, MTT assays, and Results: Five peptide inhibitors (peptides 1-5) that simultaneously target RBD and NRP1 were identified through structure-based virtual screening. MST assays showed that peptides 1-5 all exhibited nanomolar affinity for both RBD and NRP1, with peptide-1 showing the strongest affinity for RBD ( Conclusion: In conclusion, peptide-1 is a highly effective and low-toxicity antiviral inhibitor that dual-targets RBD and NRP1.
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