Milton, Nathaniel G.N. and Harris, J. Robin (2009) Polymorphism of amyloid-ß fibrils and its effects on human erythrocyte catalase binding. Micron, 40 (8). pp. 800-810. ISSN 0968-4328Full text not available from this repository.
The Alzheimer's amyloid-? (A?) peptide exists as a number of naturally occurring forms due to differential proteolytic processing of its precursor molecule. Many of the A? peptides of different lengths form fibrils in vitro, which often show polymorphisms in the fibril structure. This study presents a TEM based analysis of fibril formation by eighteen different A? peptides ranging in length from 5 to 43 amino acids. Spectrophotometric analysis of Congo red binding to the fibrillar material has been assessed and the binding of human erythrocyte catalase (HEC) to A? fibrils has also been investigated by TEM. The results show that a diverse range of A? peptides form fibrils and also bind Congo red. The ability of both A? 1–28 and A? 29–40 to form fibrils indicates that there are at least two fibril-forming domains within the full-length A? 1–40 sequence, the ability of many A? peptides to form Congo red-binding aggregates suggests that there may be up to 4 possible aggregation promoting domains. The binding of HEC was limited to A? forms containing residues 29–32. The differing capacities of fibrillar and ribbon-like structures may reflect the accessibility of the 29–32 region and suggest that HEC may be able to discriminate between different forms of A? fibrils.
|Subjects:||University of Westminster > Science and Technology > Life Sciences, School of (No longer in use)|
|Depositing User:||Miss Nina Watts|
|Date Deposited:||26 Jan 2010 14:55|
|Last Modified:||26 Jan 2010 14:55|
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