{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Jalily PH"],"funding":["Natural Sciences and Engineering Research Council of Canada","Heart and Stroke Foundation","Heart and Stroke Foundation of Canada","Natural Sciences and Engineering Research Council","Canadian Institutes of Health Research","CIHR"],"pagination":["10647"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9503309"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["23(18)"],"pubmed_abstract":["The coronavirus E proteins are small membrane proteins found in the virus envelope of alpha and beta coronaviruses that have a high degree of overlap in their biochemical and functional properties despite minor sequence variations. The SARS-CoV-2 E is a 75-amino acid transmembrane protein capable of acting as an ion channel when assembled in a pentameric fashion. Various studies have found that hexamethylene amiloride (HMA) can inhibit the ion channel activity of the E protein in bilayers and also inhibit viral replication in cultured cells. Here, we use the available structural data in conjunction with homology modelling to build a comprehensive model of the E protein to assess potential binding sites and molecular interactions of HMA derivatives. Furthermore, we employed an iterative cyc"],"journal":["International journal of molecular sciences"],"pubmed_title":["In Silico Evaluation of Hexamethylene Amiloride Derivatives as Potential Luminal Inhibitors of SARS-CoV-2 E Protein."],"pmcid":["PMC9503309"],"funding_grant_id":["PJT-156181","RGPIN-2016-05422","G-17-0018392","PJT-175024","G-21-0031566","00-00"],"pubmed_authors":["Jalily PH","Fedida D","Jalily Hasani H"],"additional_accession":[]},"is_claimable":false,"name":"In Silico Evaluation of Hexamethylene Amiloride Derivatives as Potential Luminal Inhibitors of SARS-CoV-2 E Protein.","description":"The coronavirus E proteins are small membrane proteins found in the virus envelope of alpha and beta coronaviruses that have a high degree of overlap in their biochemical and functional properties despite minor sequence variations. The SARS-CoV-2 E is a 75-amino acid transmembrane protein capable of acting as an ion channel when assembled in a pentameric fashion. Various studies have found that hexamethylene amiloride (HMA) can inhibit the ion channel activity of the E protein in bilayers and also inhibit viral replication in cultured cells. Here, we use the available structural data in conjunction with homology modelling to build a comprehensive model of the E protein to assess potential binding sites and molecular interactions of HMA derivatives. Furthermore, we employed an iterative cyc","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Sep","modification":"2026-04-08T11:50:05.526Z","creation":"2025-02-19T00:44:03.92Z"},"accession":"S-EPMC9503309","cross_references":{"pubmed":["36142556"],"doi":["10.3390/ijms231810647"]}}