{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Mercaldi GF"],"funding":["Financiadora de Estudos e Projetos"],"pagination":["18500"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9628480"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["12(1)"],"pubmed_abstract":["The nucleocapsid (N) protein plays critical roles in coronavirus genome transcription and packaging, representing a key target for the development of novel antivirals, and for which structural information on ligand binding is scarce. We used a novel fluorescence polarization assay to identify small molecules that disrupt the binding of the N protein to a target RNA derived from the SARS-CoV-2 genome packaging signal. Several phenolic compounds, including L-chicoric acid (CA), were identified as high-affinity N-protein ligands. The binding of CA to the N protein was confirmed by isothermal titration calorimetry, <sup>1</sup>H-STD and <sup>15</sup>N-HSQC NMR, and by the crystal structure of CA bound to the N protein C-terminal domain (CTD), further revealing a new modulatory site in the SARS"],"journal":["Scientific reports"],"pubmed_title":["Discovery and structural characterization of chicoric acid as a SARS-CoV-2 nucleocapsid protein ligand and RNA binding disruptor."],"pmcid":["PMC9628480"],"funding_grant_id":["01.20.0003.00"],"pubmed_authors":["Filho HVR","da Silva JC","Shimizu JF","Figueira ACM","Cordeiro AT","Proenca-Modena JL","Mercaldi GF","Zeri ACM","Rocco SA","Marques RE","Bezerra EHS","Tonoli CCC","Soprano AS","Lopes-de-Oliveira PS","Sforca ML","do Nascimento Faria J","Benedetti CE","da Cunha MG","Bruder M","Batista FAH","Nagai A","Bajgelman MC","Franchini KG","Nascimento AFZ","Trivella DBB"],"additional_accession":[]},"is_claimable":false,"name":"Discovery and structural characterization of chicoric acid as a SARS-CoV-2 nucleocapsid protein ligand and RNA binding disruptor.","description":"The nucleocapsid (N) protein plays critical roles in coronavirus genome transcription and packaging, representing a key target for the development of novel antivirals, and for which structural information on ligand binding is scarce. We used a novel fluorescence polarization assay to identify small molecules that disrupt the binding of the N protein to a target RNA derived from the SARS-CoV-2 genome packaging signal. Several phenolic compounds, including L-chicoric acid (CA), were identified as high-affinity N-protein ligands. The binding of CA to the N protein was confirmed by isothermal titration calorimetry, <sup>1</sup>H-STD and <sup>15</sup>N-HSQC NMR, and by the crystal structure of CA bound to the N protein C-terminal domain (CTD), further revealing a new modulatory site in the SARS","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Nov","modification":"2026-05-27T23:47:04.744Z","creation":"2024-12-04T12:33:06.027Z"},"accession":"S-EPMC9628480","cross_references":{"pubmed":["36323732"],"doi":["10.1038/s41598-022-22576-4"]}}