Non-chaperone Proteins Can Inhibit Aggregation and Cytotoxicity of Alzheimer Amyloid beta Peptide

Luo, Jinghui and Wärmländer, Sebastian K. T. S. and Gräslund, Astrid and Abrahams, Jan Pieter. (2014) Non-chaperone Proteins Can Inhibit Aggregation and Cytotoxicity of Alzheimer Amyloid beta Peptide. Journal of Biological Chemistry, 289 (40). pp. 27766-27775.

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Official URL: https://edoc.unibas.ch/75903/

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Many factors are known to influence the oligomerization,
fibrillation, and amyloid formation of the A peptide that is
associated with Alzheimer disease. Other proteins that are present when A peptides deposit in vivo are likely to have an effect
on these aggregation processes. To separate specific versus
broad spectrum effects of proteins on A aggregation, we tested
a series of proteins not reported to have chaperone activity: catalase, pyruvate kinase, albumin, lysozyme, -lactalbumin, and
-lactoglobulin. All tested proteins suppressed the fibrillation
of Alzheimer A(1– 40) peptide at substoichiometric ratios,
albeit some more effectively than others. All proteins bound
non-specifically to A, stabilized its random coils, and reduced
its cytotoxicity. Surprisingly, pyruvate kinase and catalase were
at least as effective as known chaperones in inhibiting A aggregation. We propose general mechanisms for the broad-spectrum inhibition A fibrillation by proteins. The mechanisms we
discuss are significant for prognostics and perhaps even for prevention and treatment of Alzheimer disease.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Structural Biology & Biophysics > Nano-diffraction of Biological Specimen (Abrahams)
UniBasel Contributors:Abrahams, Jan Pieter
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:American Society for Biochemistry and Molecular Biology
Note:Publication type according to Uni Basel Research Database: Journal article
Identification Number:
Last Modified:06 Nov 2020 08:22
Deposited On:06 Nov 2020 08:22

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