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Fine structure study of A beta(1-42) fibrillogenesis with atomic force microscopy

Authordc.contributor.authorArimon, M. 
Authordc.contributor.authorDiez Pérez, I. es_CL
Authordc.contributor.authorKogan Bocian, Marcelo es_CL
Authordc.contributor.authorDurany, N. es_CL
Authordc.contributor.authorGiralt, Ernest es_CL
Authordc.contributor.authorSanz, F. es_CL
Authordc.contributor.authorFernández Busquets, X. es_CL
Admission datedc.date.accessioned2010-09-07T15:13:33Z
Available datedc.date.available2010-09-07T15:13:33Z
Publication datedc.date.issued2005-05
Cita de ítemdc.identifier.citationFASEB JOURNAL 19(7): 1344-1362en_US
Identifierdc.identifier.issn0892-6638
Identifierdc.identifier.urihttp://repositorio.uchile.cl/handle/2250/121033
Abstractdc.description.abstractOne of the hallmarks of Alzheimer's disease is the self-aggregation of the amyloid beta peptide (A beta) in extracellular amyloid fibrils. Among the different forms of A beta, the 42-residue fragment (A beta(1-42)) readily self-associates and forms nucleation centers from where fibrils can quickly grow. The strong tendency of A beta(1-42) to aggregate is one of the reasons for the scarcity of data on its fibril formation process. We have used atomic force microscopy (AFM) to visualize in liquid environment the fibrillogenesis of synthetic A beta(1-42) on hydrophilic and hydrophobic surfaces. The results presented provide nanometric resolution of the main structures characteristic of the several steps from monomeric A beta(1-42) to mature fibrils in vitro. Oligomeric globular aggregates of A beta(1-42) precede the appearance of protofibrils, the first fibrillar species,although we have not obtained direct evidence of oligomer-protofibril interconversion. The protofibril dimensions deduced from our AFM images are consistent with a model that postulates the stacking of the peptide in a hairpin conformation perpendicular to the long axis of the protofibril, forming single-sheets ribbon-shaped. The most abundant form of A beta(1-42) fibril exhibits a nodular structure with a similar to 100-nm periodicity. This length is very similar 1) to the length of protofibril bundles that are the dominant feature at earlier stages in the aggregation process,2) to the period of helical structures that have been observed in the core of fibrils, and 3) to the distance between regularly spaced, structurally weak fibril points. Taken together, these data are consistent with the existence of a similar to 100-nm long basic protofibril unit that is a key fibril building block.en_US
Lenguagedc.language.isoenen_US
Publisherdc.publisherFEDERATION AMER SOC EXP BIOL.en_US
Keywordsdc.subjectAlzheimers diseaseen_US
Títulodc.titleFine structure study of A beta(1-42) fibrillogenesis with atomic force microscopyen_US
Document typedc.typeArtículo de revistaen_US


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