Fine structure study of Aß 1-42 fibrillogenesis with atomic force microscopy Muriel Arimon * , Ismael Díez-Pérez † , Marcelo J. Kogan ‡ , Núria Durany § , Ernest Giralt ‡ ,¶ , Fausto Sanz † and Xavier Fernàndez-Busquets * ,1 * Laboratori de Recerca en Nanobioenginyeria, Parc Científic de Barcelona (PCB), Universitat de Barcelona (UB), Spain; † Departament de Química Física, UB; ‡ Institut de Recerca Biomèdica de Barcelona, PCB; § Facultat de Ciències de la Salut, Universitat Internacional de Catalunya, Barcelona; and ¶ Departament de Química Orgànica, UB 1 Correspondence: E-mail: xfernandez_busquets@ub.edu <h3>SPECIFIC AIMS</h3> Pathogenesis in Alzheimer’s disease (AD) is linked to the accumulation of the highly amyloidogenic self-associating amyloid ß 1-42 peptide (Aß 1-42 ). We have used atomic force microscopy (AFM) visualization on hydrophilic and hydrophobic surfaces in liquid environment to study in vitro the fibrillogenesis process of synthetic Aß 1-42 , with the aim of obtaining nanometric resolution of the main structures characteristic of the several steps of fibril formation from monomeric Aß 1-42 to mature fibrils. <h3>PRINCIPAL FINDINGS</h3> 1. Globular oligomers of Aß 1-42 are the dominant species at early stages of aggregation and deposit best on hydrophilic surfaces Aß 1-42 was
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Fine structure study of Aß1-42 fibrillogenesis with atomic force microscopy
Arimon, Muriel; Díez-Pérez, Ismael; Kogan, Marcelo J.; Durany, Núria; Giralt, Ernest; Sanz, Fausto; Fernàndez-Busquets, Xavier
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, Volume 19 (10): 1344
Fed of American Socs for Experimental Biology – Aug 1, 2005
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