{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,20]],"date-time":"2025-10-20T00:44:05Z","timestamp":1760921045163,"version":"build-2065373602"},"reference-count":51,"publisher":"Wiley","issue":"18","license":[{"start":{"date-parts":[[2014,7,30]],"date-time":"2014-07-30T00:00:00Z","timestamp":1406678400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"name":"Universidad Nacional del Litoral, Santa Fe, Argentina","award":["CAI+D-2011","PIP-112-201101-00060"],"award-info":[{"award-number":["CAI+D-2011","PIP-112-201101-00060"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["J of Separation Science"],"published-print":{"date-parts":[[2014,9]]},"abstract":"<jats:p>Neuronal activity loss may be due to toxicity caused by amyloid\u2010beta peptides forming soluble oligomers. Here amyloid\u2010beta peptides (1\u201342, 1\u201340, 1\u201339, 1\u201338, and 1\u201337) 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\u2010beta peptide propensities to aggregation through pair particles interaction potentials and Brownian aggregation kinetic theories. Two background electrolytes are considered at 25\u00b0C, one for pH 9 and ionic strength <jats:italic>I<\/jats:italic> = 40 mM (aggregation is inhibited through NH<jats:sub>4<\/jats:sub>OH) the other for pH 10 and <jats:italic>I<\/jats:italic> = 100 mM (without NH<jats:sub>4<\/jats:sub>OH). Physical explanations of peptide oligomerization mechanisms are provided. The effect of hydration, electrostatic, and dispersion forces in the amyloidogenic process of amyloid\u2010beta peptides (1\u201340 and 1\u201342) are quantitatively presented. The interplay among effective charge number, hydration, and conformation of chains is described. It is shown that amyloid\u2010beta peptides (1\u201340 and 1\u201342) at pH 10, <jats:italic>I<\/jats:italic> = 100 mM and 25\u00b0C, 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.<\/jats:p>","DOI":"10.1002\/jssc.201400533","type":"journal-article","created":{"date-parts":[[2014,6,27]],"date-time":"2014-06-27T07:58:18Z","timestamp":1403855898000},"page":"2618-2624","source":"Crossref","is-referenced-by-count":5,"title":["Estimation of electrokinetic and hydrodynamic global properties of relevant amyloid\u2010beta peptides through the modeling of their effective electrophoretic mobilities and analysis of their propensities to aggregation"],"prefix":"10.1002","volume":"37","author":[{"given":"Julio A.","family":"Deiber","sequence":"first","affiliation":[{"name":"Instituto de Desarrollo Tecnol\u00f3gico para la Industria Qu\u00edmica (INTEC) Universidad Nacional del Litoral (UNL) Consejo Nacional de Investigaciones Cient\u00edficas y T\u00e9cnicas (CONICET)  Santa Fe Argentina"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Maria V.","family":"Piaggio","sequence":"additional","affiliation":[{"name":"C\u00e1tedra de Bioqu\u00edmica B\u00e1sica de Macromol\u00e9culas Facultad de Bioqu\u00edmica y Ciencias Biol\u00f3gicas, UNL  Santa Fe Argentina"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Marta B.","family":"Peirotti","sequence":"additional","affiliation":[{"name":"Instituto de Desarrollo Tecnol\u00f3gico para la Industria Qu\u00edmica (INTEC) Universidad Nacional del Litoral (UNL) Consejo Nacional de Investigaciones Cient\u00edficas y T\u00e9cnicas (CONICET)  Santa Fe 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