Affiliations: Radboud University Nijmegen Medical Centre, Department of Neurology, Department of Laboratory Medicine, Donders Institute for Brain, Cognition and Behaviour, Alzheimer Centre Nijmegen, Nijmegen, The Netherlands
Correspondence:
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Correspondence to: Dr. Ir. Marcel M. Verbeek, Department of Neurology, 830 LGEM, Radboud University Nijmegen Medical Centre, P.O. Box 9101, 6500 HB Nijmegen, The Netherlands. Tel.: +31 243615192; Fax: +31 312 436 68754; Email: [email protected]; Website: www.neurochemistry.nl.
Note: [1] These authors contributed equally to this review.
Abstract: Amyloid-β protein (Aβ) accumulation is one of the major hallmarks of Alzheimer's disease and plays a crucial role in its pathogenesis. Aβ aggregates into fibrils, but rather than these end-products of the aggregation process, intermediate species, referred to as oligomers, have been identified as the most neurotoxic Aβ aggregates. To characterize the different Aβ species and to study the aggregation process, a wide range of techniques has been applied over the past years. These techniques aim to visualize the different Aβ species and study their structure, to separate them, and to quantify the aggregated Aβ forms by immunology-based methods. In this review, we provide an overview and discussion of the most important techniques used for these aims. Often a combination of techniques will be appropriate to obtain the most optimal information.
