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dc.contributor.authorSiqueira, Andrei Santos-
dc.contributor.authorLima, Alex Ranieri Jerônimo-
dc.contributor.authorSouza, Rafael Conceição de-
dc.contributor.authorSantos, Alberdan Silva-
dc.contributor.authorVianez Júnior, João Lídio da Silva Gonçalves-
dc.contributor.authorGonçalves, Evonnildo Costa-
dc.date.accessioned2019-08-16T11:59:35Z-
dc.date.available2019-08-16T11:59:35Z-
dc.date.issued2017-
dc.identifier.citationSIQUEIRA, Andrei Santos et al. In silico analysis of the cyanobacterial lectin scytovirin : new insights into binding properties. Molecular Biology Reports, v. 44, n. 1, p. 353-358, Aug. 2017.pt_BR
dc.identifier.issn0301-4851-
dc.identifier.urihttp://patua.iec.gov.br//handle/iec/3842-
dc.description.abstractScytovirin is a lectin isolated from the cyanobacterium Scytonema varium that has shown activity against HIV, SARS coronavirus and Zaire Ebola virus. Its 95 amino acids are divided into two structural domains (SD), the first spanning amino acids 1–48 (SD1) and the second 49–95 (SD2). Interestingly, the domains are nearly identical but differ in their affinities for carbohydrates. With the aim of enhancing understanding of the binding properties of scytovirin, we performed molecular dynamics (MD) simulations of scytovirin complexed with Man4. We set up three systems: (i) Man4 bound to both domains (SD1+SD2) using the full-length protein; (ii) Man4 bound to an incomplete protein, containing only SD1 and (iii) Man4 bound to an incomplete protein containing only SD2. Contrary to other reports, binding free energy results suggest that Man4 can bind simultaneously to SD1 and SD2 binding regions, but SD1 individually has the best values of energy and the best affinity for Man4. Decomposition of the binding free energy showed that the residues that interact with Man4 were different in the three systems, suggesting that the binding mechanism of Man4 varies between full-length protein, SD1 and SD2. The results presented here may help to formulate strategies to use scytovirin and promote mutagenesis studies to improve the antiviral activity of scytovirin.pt_BR
dc.description.sponsorshipWe acknowledge Fundação Amazônia de Amparo a Estudos e Pesquisas do Pará (FAPESPA) for financially supporting (ICAAF 099/2014) our project. Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq) also supported individual authors through Grant 311686/2015-0 (ECG).pt_BR
dc.language.isoengpt_BR
dc.publisherSpringer Verlagpt_BR
dc.rightsAcesso Abertopt_BR
dc.titleIn silico analysis of the cyanobacterial lectin scytovirin : new insights into binding propertiespt_BR
dc.typeArtigopt_BR
dc.subject.decsPrimaryLectinas / químicapt_BR
dc.subject.decsPrimaryLectinas / metabolismopt_BR
dc.subject.decsPrimaryProteínas de Bactérias / químicapt_BR
dc.subject.decsPrimaryProteínas de Bactérias / metabolismopt_BR
dc.subject.decsPrimaryAntivirais / químicapt_BR
dc.subject.decsPrimaryCianobactériaspt_BR
dc.subject.decsPrimarySimulação de Dinâmica Molecularpt_BR
dc.subject.decsPrimarySequência de Aminoácidospt_BR
dc.subject.decsPrimaryLigação Proteicapt_BR
dc.subject.decsPrimaryTemperatura Ambientept_BR
dc.creator.affilliationUniversidade Federal do Pará. Instituto de Ciências Biológicas. Laboratório de Tecnologia Biomolecular. Belém, PA, Brazil.pt_BR
dc.creator.affilliationUniversidade Federal do Pará. Instituto de Ciências Biológicas. Laboratório de Tecnologia Biomolecular. Belém, PA, Brazil.pt_BR
dc.creator.affilliationUniversidade Federal do Pará. Instituto de Ciências Exatas e Naturais. Laboratórios de Investigação Sistemática em Biotecnologia e Biodiversidade Molecular. Belém, PA, Brazil.pt_BR
dc.creator.affilliationUniversidade Federal do Pará. Instituto de Ciências Exatas e Naturais. Laboratórios de Investigação Sistemática em Biotecnologia e Biodiversidade Molecular. Belém, PA, Brazil.pt_BR
dc.creator.affilliationMinistério da Saúde. Secretaria de Vigilância em Saúde. Instituto Evandro Chagas. Ananindeua, PA, Brasil.pt_BR
dc.creator.affilliationUniversidade Federal do Pará. Instituto de Ciências Biológicas. Laboratório de Tecnologia Biomolecular. Belém, PA, Brazil.pt_BR
dc.identifier.doi10.1007/s11033-017-4116-1-


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