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dc.provenanceCONICET-
dc.creatorBaler, K.-
dc.creatorMartín, Osvaldo Antonio-
dc.creatorCarignano, Marcelo A.-
dc.creatorAmeer, G. A.-
dc.creatorVila, Jorge Alberto-
dc.creatorSzleifer, Igal-
dc.date2017-12-21T20:32:50Z-
dc.date2017-12-21T20:32:50Z-
dc.date2014-01-
dc.date2017-12-12T18:37:51Z-
dc.date.accessioned2019-04-29T15:38:13Z-
dc.date.available2019-04-29T15:38:13Z-
dc.date.issued2014-01-
dc.identifierSzleifer, Igal; Vila, Jorge Alberto; Ameer, G. A.; Carignano, Marcelo A.; Martín, Osvaldo Antonio; Baler, K.; et al.; Electrostatic Unfolding and Interactions of Albumin Driven by pH Changes: A Molecular Dynamics Study; American Chemical Society; Journal of Physical Chemistry B; 118; 4; 1-2014; 921-930-
dc.identifier1520-6106-
dc.identifierhttp://hdl.handle.net/11336/31294-
dc.identifierCONICET Digital-
dc.identifierCONICET-
dc.identifier.urihttp://rodna.bn.gov.ar:8080/jspui/handle/bnmm/298203-
dc.descriptionA better understanding of protein aggregation is bound to translate into<br />critical advances in several areas, including the treatment of misfolded protein disorders and the development of self-assembling biomaterials for novel commercial applications. Because of its ubiquity and clinical potential, albumin is one of the best-characterized models in protein aggregation research; but its properties in different conditions are not completely understood. Here, we carried out all-atom molecular dynamics simulations of albumin to understand how electrostatics can affect the conformation of a single albumin molecule just prior to self-assembly. We then analyzed the tertiary structure and solvent accessible surface area of albumin after electrostatically triggered partial denaturation. The data obtained from these single protein simulations allowed us to investigate the effect of electrostatic interactions between two proteins. The results of these simulations suggested that hydrophobic attractions and counterion binding may be strong enough to effectively overcome the electrostatic repulsions between the highly charged monomers. This work contributes to our general understanding of protein aggregation mechanisms, the importance of explicit consideration of free ions in protein solutions, provides critical new insights about the equilibrium conformation of albumin in its partially denatured state at low pH, and may spur significant progress in our efforts to develop biocompatible protein hydrogels driven by electrostatic partial denaturation.-
dc.descriptionFil: Baler, K.. Northwestern University; Estados Unidos-
dc.descriptionFil: Martín, Osvaldo Antonio. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis. Instituto de Matemática Aplicada de San Luis ; Argentina-
dc.descriptionFil: Carignano, Marcelo A.. Northwestern University; Estados Unidos-
dc.descriptionFil: Ameer, G. A.. Northwestern University; Estados Unidos-
dc.descriptionFil: Vila, Jorge Alberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis. Instituto de Matemática Aplicada de San Luis ; Argentina-
dc.descriptionFil: Szleifer, Igal. Northwestern University; Estados Unidos-
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dc.languageeng-
dc.publisherAmerican Chemical Society-
dc.relationinfo:eu-repo/semantics/altIdentifier/url/http://pubs.acs.org/doi/abs/10.1021/jp409936v-
dc.relationinfo:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1021/jp409936v-
dc.rightsinfo:eu-repo/semantics/restrictedAccess-
dc.rightshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/-
dc.sourcereponame:CONICET Digital (CONICET)-
dc.sourceinstname:Consejo Nacional de Investigaciones Científicas y Técnicas-
dc.sourceinstacron:CONICET-
dc.source.urihttp://hdl.handle.net/11336/31294-
dc.subjectALBUMIN-
dc.subjectELECTROSTATIC-
dc.subjectPH-
dc.subjectMOLECULAR DYNAMICS-
dc.subjectOtras Ciencias Biológicas-
dc.subjectCiencias Biológicas-
dc.subjectCIENCIAS NATURALES Y EXACTAS-
dc.titleElectrostatic Unfolding and Interactions of Albumin Driven by pH Changes: A Molecular Dynamics Study-
dc.typeinfo:eu-repo/semantics/article-
dc.typeinfo:eu-repo/semantics/publishedVersion-
dc.typeinfo:ar-repo/semantics/articulo-
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