{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["20(2)"],"submitter":["Saeed A"],"pubmed_abstract":["Vicilins are major seed storage proteins and show differential binding affinities toward sugar moieties of fungal cell wall and insect gut epithelium. Hence, purpose of study is the thorough <i>in-silico</i> characterization of interactions between vicilin and chitin oligomer followed by fungal and insecticidal bioassays. This work covers the molecular simulation studies explaining the interactions between <i>Pisum sativum</i> vicilin (<i>Ps</i>V) and chitin oligomer followed by protein bioassay against different pathogens. LC-MS/MS of purified <i>Ps</i>V (∼50 kDa) generated residual data along high pea vicilin homology (UniProtKB ID; P13918). Predicted model (<i>Ps</i>V) indicated the characteristic homotrimer joined through head-to-tail association and each monomer is containing a bicupi"],"journal":["Dose-response : a publication of International Hormesis Society"],"pagination":["15593258221108280"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9208065"],"repository":["biostudies-literature"],"pubmed_title":["<i>In-silico</i> Studies Calculated a New Chitin Oligomer Binding Site Inside Vicilin: A Potent Antifungal and Insecticidal Agent."],"pmcid":["PMC9208065"],"pubmed_authors":["Akrem A","Imran M","Hussain S","Rafiq Z","Saeed MQ","Khaliq B","Iqbal RK","Saeed A","Saeed Q","Ali Z","Mehmood S"],"additional_accession":[]},"is_claimable":false,"name":"<i>In-silico</i> Studies Calculated a New Chitin Oligomer Binding Site Inside Vicilin: A Potent Antifungal and Insecticidal Agent.","description":"Vicilins are major seed storage proteins and show differential binding affinities toward sugar moieties of fungal cell wall and insect gut epithelium. Hence, purpose of study is the thorough <i>in-silico</i> characterization of interactions between vicilin and chitin oligomer followed by fungal and insecticidal bioassays. This work covers the molecular simulation studies explaining the interactions between <i>Pisum sativum</i> vicilin (<i>Ps</i>V) and chitin oligomer followed by protein bioassay against different pathogens. LC-MS/MS of purified <i>Ps</i>V (∼50 kDa) generated residual data along high pea vicilin homology (UniProtKB ID; P13918). Predicted model (<i>Ps</i>V) indicated the characteristic homotrimer joined through head-to-tail association and each monomer is containing a bicupi","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Apr-Jun","modification":"2026-05-27T22:23:00.344Z","creation":"2024-11-05T20:32:52.724Z"},"accession":"S-EPMC9208065","cross_references":{"pubmed":["35734395"],"doi":["10.1177/15593258221108280"]}}