A Computational–Experimental Investigation of the Molecular Mechanism of Interleukin-6-Piperine Interaction

Registro completo de metadados
MetadadosDescriçãoIdioma
Autor(es): dc.contributorScience and Technology of Mato Grosso-
Autor(es): dc.contributorUniversity of Birmingham-
Autor(es): dc.contributorUniversidade Estadual Paulista (UNESP)-
Autor(es): dc.creatorPovinelli, Ana Paula Ribeiro-
Autor(es): dc.creatorZazeri, Gabriel-
Autor(es): dc.creatorJones, Alan M.-
Autor(es): dc.creatorCornélio, Marinônio Lopes-
Data de aceite: dc.date.accessioned2025-08-21T18:26:01Z-
Data de disponibilização: dc.date.available2025-08-21T18:26:01Z-
Data de envio: dc.date.issued2023-03-01-
Data de envio: dc.date.issued2023-03-01-
Data de envio: dc.date.issued2022-07-01-
Fonte completa do material: dc.identifierhttp://dx.doi.org/10.3390/ijms23147994-
Fonte completa do material: dc.identifierhttp://hdl.handle.net/11449/241599-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/11449/241599-
Descrição: dc.descriptionHerein, we elucidate the biophysical aspects of the interaction of an important protein, Interleukin-6 (IL6), which is involved in cytokine storm syndrome, with a natural product with anti-inflammatory activity, piperine. Despite the role of piperine in the inhibition of the transcriptional protein NF-κB pathway responsible for activation of IL6 gene expression, there are no studies to the best of our knowledge regarding the characterisation of the molecular interaction of the IL6-piperine complex. In this context, the characterisation was performed with spectroscopic experiments aided by molecular modelling. Fluorescence spectroscopy alongside van’t Hoff analyses showed that the complexation event is a spontaneous process driven by non-specific interactions. Circular dichroism aided by molecular dynamics revealed that piperine caused local α-helix reduction. Molecular docking and molecular dynamics disclosed the microenvironment of interaction as non-polar amino acid residues. Although piperine has three available hydrogen bond acceptors, only one hydrogen-bond was formed during our simulation experiments, reinforcing the major role of non-specific interactions that we observed experimentally. Root mean square deviation (RMSD) and hydrodynamic radii revealed that the IL6-piperine complex was stable during 800 ns of simulation. Taken together, these results can support ongoing IL6 drug discovery efforts.-
Descrição: dc.descriptionFederal Institute of Education Science and Technology of Mato Grosso-
Descrição: dc.descriptionSchool of Pharmacy Institute of Clinical Sciences College of Medical and Dental Sciences University of Birmingham, Edgbaston-
Descrição: dc.descriptionDepartamento de Física Instituto de Biociências Letras e Ciências Exatas (IBILCE) UNESP, Rua Cristovão Colombo 2265-
Descrição: dc.descriptionDepartamento de Física Instituto de Biociências Letras e Ciências Exatas (IBILCE) UNESP, Rua Cristovão Colombo 2265-
Idioma: dc.languageen-
Relação: dc.relationInternational Journal of Molecular Sciences-
???dc.source???: dc.sourceScopus-
Palavras-chave: dc.subjectfluorescence spectroscopy-
Palavras-chave: dc.subjectIL6-
Palavras-chave: dc.subjectInterleukin-6-
Palavras-chave: dc.subjectmolecular biophysics-
Palavras-chave: dc.subjectmolecular docking-
Palavras-chave: dc.subjectpiperine-
Palavras-chave: dc.subjectumbrella sampling-
Título: dc.titleA Computational–Experimental Investigation of the Molecular Mechanism of Interleukin-6-Piperine Interaction-
Tipo de arquivo: dc.typelivro digital-
Aparece nas coleções:Repositório Institucional - Unesp

Não existem arquivos associados a este item.