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dc.contributor.author
Deiber, Julio Alcides
dc.contributor.author
Piaggio, María Virginia
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Peirotti, Marta Beatriz
dc.date.available
2017-08-14T20:22:20Z
dc.date.issued
2014-07
dc.identifier.citation
Deiber, Julio Alcides; Piaggio, María Virginia; Peirotti, Marta Beatriz; Estimation of electrokinetic and hydrodynamic global properties of relevant amyloid-beta peptides through the modeling of their effective electrophoretic mobilities and analysis of their propensities to aggregation; Wiley VCH Verlag; Journal Of Separation Science; 37; 18; 7-2014; 2618-2624
dc.identifier.issn
1615-9306
dc.identifier.uri
http://hdl.handle.net/11336/22363
dc.description.abstract
Neuronal activity loss may be due to toxicity caused by amyloid-beta peptides forming soluble oligomers. Here amyloid-beta peptides (1–42, 1–40, 1–39, 1–38, and 1–37) are characterized through the modeling of their experimental effective electrophoretic mobilities determined by a capillary zone electrophoresis method as reported in the literature. The resulting electrokinetic and hydrodynamic global properties are used to evaluate amyloid-beta peptide propensities to aggregation through pair particles interaction potentials and Brownian aggregation kinetic theories. Two background electrolytes are considered at 25 ºC, one for pH 9 and ionic strength I = 40 mM (aggregation is inhibited through NH4OH) the other for pH 10 and I = 100 mM (without NH4OH). Physical explanations of peptide oligomerization mechanisms are provided. The effect of hydration, electrostatic, and dispersion forces in the amyloidogenic process of amyloid-beta peptides (1–40 and 1–42) are quantitatively presented. The interplay among effective charge number, hydration, and conformation of chains is described. It is shown that amyloid-beta peptides (1–40 and 1–42) at pH 10, I = 100mMand 25 ºC, may form soluble oligomers, mainly of order 2 and 4, after an incubation of 48 h, which at higher times evolve and end up in complex structures (protofibrils and fibrils) found in plaques associated with Alzheimer’s disease.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Wiley VCH Verlag
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Aggregation Rates
dc.subject
Amyloid-Beta
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Electrokinetic Properties
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Electrophoretic Mobility
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Hydrodynamic Properties
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Otras Ingeniería Química
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Ingeniería Química
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INGENIERÍAS Y TECNOLOGÍAS
dc.title
Estimation of electrokinetic and hydrodynamic global properties of relevant amyloid-beta peptides through the modeling of their effective electrophoretic mobilities and analysis of their propensities to aggregation
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2017-07-31T17:49:05Z
dc.journal.volume
37
dc.journal.number
18
dc.journal.pagination
2618-2624
dc.journal.pais
Alemania
dc.description.fil
Fil: Deiber, Julio Alcides. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Desarrollo Tecnológico para la Industria Química. Universidad Nacional del Litoral. Instituto de Desarrollo Tecnológico para la Industria Química; Argentina
dc.description.fil
Fil: Piaggio, María Virginia. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas; Argentina
dc.description.fil
Fil: Peirotti, Marta Beatriz. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Desarrollo Tecnológico para la Industria Química. Universidad Nacional del Litoral. Instituto de Desarrollo Tecnológico para la Industria Química; Argentina
dc.journal.title
Journal Of Separation Science
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1002/jssc.201400533
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://onlinelibrary.wiley.com/doi/10.1002/jssc.201400533/abstract
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