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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
Author(s) -
Deiber Julio A.,
Piaggio Maria V.,
Peirotti Marta B.
Publication year - 2014
Publication title -
journal of separation science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.72
H-Index - 102
eISSN - 1615-9314
pISSN - 1615-9306
DOI - 10.1002/jssc.201400533
Subject(s) - chemistry , electrokinetic phenomena , electrophoresis , peptide , amyloid beta , ionic strength , fibril , amyloid (mycology) , amylin , amyloid disease , capillary electrophoresis , biophysics , protein aggregation , amyloid fibril , chromatography , amyloid β , biochemistry , organic chemistry , aqueous solution , medicine , inorganic chemistry , disease , islet , pathology , insulin , biology , endocrinology
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°C, one for pH 9 and ionic strength I = 40 mM (aggregation is inhibited through NH 4 OH) the other for pH 10 and I = 100 mM (without NH 4 OH). 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 = 100 mM and 25°C, 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.