αB-crystallin, a small heat-shock protein, prevents the amyloid fibril growth of an amyloid β-peptide and β2-microglobulin
نویسندگان
چکیده
Bakthisaran RAMAN*†, Tadato BAN†, Miyo SAKAI†, Saloni Y. PASTA*, Tangirala RAMAKRISHNA*, Hironobu NAIKI‡, Yuji GOTO†1 and Ch. Mohan RAO*1 *Centre for Cellular and Molecular Biology, Uppal Road, Hyderabad 500 007, India, †Institute for Protein Research, Osaka University, and CREST, Japan Science and Technology Agency, Yamadaoka 3-2, Suita, Osaka 565–0871, Japan, and ‡Faculty of Medical Science, University of Fukui, and CREST, Japan Science and Technology Agency, Matsuoka, Fukui 910-1193, Japan
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Binding of the molecular chaperone αB-crystallin to Aβ amyloid fibrils inhibits fibril elongation.
The molecular chaperone αB-crystallin is a small heat-shock protein that is upregulated in response to a multitude of stress stimuli, and is found colocalized with Aβ amyloid fibrils in the extracellular plaques that are characteristic of Alzheimer's disease. We investigated whether this archetypical small heat-shock protein has the ability to interact with Aβ fibrils in vitro. We find that αB-...
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