Dissecting the Aggregation Events of Alzheimer’s disease Associated Aβ peptide Variants by the Combined use of Different Fluorescent Probes

Göransson, Anna-Lena (author): Linköpings universitet,Molekylär Bioteknik,Tekniska högskolan

Otieno, Mildred (author): Linköpings universitet,Molekylär Bioteknik,Tekniska högskolan

Nilsson, Peter (author): Linköpings universitet,Organisk Kemi,Tekniska högskolan

Johansson, Leif B. G. (author): Linköpings universitet,Organisk Kemi,Tekniska högskolan

Nilsson, K. Peter R (author): Linköpings universitet,Biomolekylär och Organisk Elektronik,Tekniska högskolan

Brorsson, Ann-Christin (author): Linköpings universitet,Molekylär Bioteknik,Tekniska högskolan

(creator_code:org_t)

Abstract Subject headings

The formation of soluble prefibrillar oligomeric species of the amyloid β peptide (Aβ) has been implicated as a causative agent in the development of Alzheimer’s disease (AD). It is therefore important to characterize the properties of these aggregates, which precede the formation of amyloid fibrils. We studied the in vitro aggregation process of two Aβ40 peptide variants through the combined use of four different fluorescent probes and transmission electron microscopy. Previous studies have shown that these two studied Aβ40 variants exhibit different levels of neurodegeneration when expressed in the central nervous system of Drosophila melanogaster. In the present study, we demonstrate distinct differences in aggregate morphology and their binding properties to different fluorescent probes during in vitro fibrillation of these Aβ peptides. Our results indicate a potential link between the observed neurodegenerative properties and the biophysical properties of distinct aggregated Aβ species.

By the author/editor: Göransson, Anna- ...; Otieno, Mildred; Nilsson, Peter; Johansson, Leif ...; Nilsson, K. Pete ...; Brorsson, Ann-Ch ...

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