Adsorption of lysozyme into a charged confining pore

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Autor(es): dc.contributorUniversidade Estadual de Campinas (UNICAMP)-
Autor(es): dc.contributorUniversity of Potsdam-
Autor(es): dc.contributorHumboldt-Universität zu Berlin-
Autor(es): dc.contributorUniversidade Estadual Paulista (UNESP)-
Autor(es): dc.creatorCaetano, Daniel L. Z.-
Autor(es): dc.creatorMetzler, Ralf-
Autor(es): dc.creatorCherstvy, Andrey G.-
Autor(es): dc.creatorde Carvalho, Sidney J.-
Data de aceite: dc.date.accessioned2025-08-21T19:18:23Z-
Data de disponibilização: dc.date.available2025-08-21T19:18:23Z-
Data de envio: dc.date.issued2022-04-29-
Data de envio: dc.date.issued2022-04-29-
Data de envio: dc.date.issued2021-12-27-
Fonte completa do material: dc.identifierhttp://dx.doi.org/10.1039/d1cp03185f-
Fonte completa do material: dc.identifierhttp://hdl.handle.net/11449/230121-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/11449/230121-
Descrição: dc.descriptionSeveral applications arise from the confinement of proteins on surfaces because their stability and biological activity are enhanced. It is also known that the way in which a protein adsorbs on the surface is important for its biological function since its active sites should not be obstructed. In this study, the adsorption properties of hen egg-white lysozyme, HEWL, into a negatively charged silica pore is examined by employing a coarse-grained model and constant-pH Monte Carlo simulations. The role of electrostatic interactions is taken into accountviaincluding the Debye-Hückel potentials into the Cα structure-based model. We evaluate the effects of pH, salt concentration, and pore radius on the protein preferential orientation and spatial distribution of its residues regarding the pore surface. By mapping the residues that stay closer to the pore surface, we find that the increase of pH leads to orientational changes of the adsorbed protein when the solution pH gets closer to the HEWL isoelectric point. Under these conditions, the pKashift of these important residues caused by the adsorption into the charged confining surface results in a HEWL charge distribution that stabilizes the adsorption in the observed protein orientation. We compare our observations to the results of the pKashift for HEWL available in the literature and to some experimental data.-
Descrição: dc.descriptionInstitute of Chemistry State University of Campinas (UNICAMP)-
Descrição: dc.descriptionCenter for Computational Engineering and Sciences State University of Campinas (UNICAMP)-
Descrição: dc.descriptionInstitute for Physics & Astronomy University of Potsdam-
Descrição: dc.descriptionInstitut für Physik Humboldt-Universität zu Berlin-
Descrição: dc.descriptionDepartment of Physics São Paulo State University (UNESP) Institute of Biosciences Humanities and Exact Sciences São José do Rio Preto-
Descrição: dc.descriptionDepartment of Physics São Paulo State University (UNESP) Institute of Biosciences Humanities and Exact Sciences São José do Rio Preto-
Formato: dc.format27195-27206-
Idioma: dc.languageen-
Relação: dc.relationPhysical Chemistry Chemical Physics-
???dc.source???: dc.sourceScopus-
Título: dc.titleAdsorption of lysozyme into a charged confining pore-
Tipo de arquivo: dc.typelivro digital-
Aparece nas coleções:Repositório Institucional - Unesp

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