Structure-based inhibitors of amyloid beta core suggest a common interface with tau

Griner, Sarah L.; Seidler, Paul; Bowler, Jeannette; Murray, Kevin A.; Yang, Tianxiao Peter; Sahay, Shruti; Sawaya, Michael R.; Cascio, Duilio; Rodriguez, Jose A.; Philipp, Stephan; Sosna, Justyna; Glabe, Charles G.; Gonen, Tamir; Eisenberg, David S.

doi:10.7554/elife.46924

Structure-based inhibitors of amyloid beta core suggest a common interface with tau

Journal Article · Tue Oct 15 00:00:00 EDT 2019 · eLife

DOI:https://doi.org/10.7554/elife.46924· OSTI ID:1628905

^[1]; Seidler, Paul ^[2]; ^[2]; Murray, Kevin A. ^[2]; ^[2]; Sahay, Shruti ^[2]; Sawaya, Michael R. ^[2]; Cascio, Duilio ^[2]; Rodriguez, Jose A. ^[2]; Philipp, Stephan ^[3]; Sosna, Justyna ^[3]; Glabe, Charles G. ^[4]; ^[5]; ^[2]

Univ. of California, Los Angeles, CA (United States). DOE Inst. Howard Hughes Medical Inst. Molecular Biology Inst. Dept. of Biological Chemistry; DOE/OSTI
Univ. of California, Los Angeles, CA (United States). DOE Inst. Howard Hughes Medical Inst. Molecular Biology Inst. Dept. of Biological Chemistry
Univ. of California, Irvine, CA (United States). Dept. of Molecular Biology and Biochemistry
Univ. of California, Irvine, CA (United States). Dept. of Molecular Biology and Biochemistry; King Abdulaziz Univ., Jeddah (Saudi Arabia). King Fahd Medical Research Center. Faculty of Science and Experimental Biochemistry Unit. Biochemistry Dept.
Howard Hughes Medical Inst., Ashburn, VA (United States). Janelia Research Campus

Alzheimer’s disease (AD) pathology is characterized by plaques of amyloid beta (Aβ) and neurofibrillary tangles of tau. Aβ aggregation is thought to occur at early stages of the disease, and ultimately gives way to the formation of tau tangles which track with cognitive decline in humans. Here, we report the crystal structure of an Aβ core segment determined by MicroED and in it, note characteristics of both fibrillar and oligomeric structure. Using this structure, we designed peptide-based inhibitors that reduce Aβ aggregation and toxicity of already-aggregated species. Unexpectedly, we also found that these inhibitors reduce the efficiency of Aβ-mediated tau aggregation, and moreover reduce aggregation and self-seeding of tau fibrils. The ability of these inhibitors to interfere with both Aβ and tau seeds suggests these fibrils share a common epitope, and supports the hypothesis that cross-seeding is one mechanism by which amyloid is linked to tau aggregation and could promote cognitive decline.

View Accepted Manuscript (DOE)

Research Organization:: Univ. of California, Los Angeles, CA (United States)

Sponsoring Organization:: USDOE Office of Science (SC), Biological and Environmental Research (BER). Biological Systems Science Division

Grant/Contract Number:: FG02-00ER41132

OSTI ID:: 1628905

Journal Information:: eLife, Journal Name: eLife Vol. 8; ISSN 2050-084X

Publisher:: eLife Sciences Publications, Ltd.Copyright Statement

Country of Publication:: United States

Language:: English

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Structure-based inhibitors of amyloid beta core suggest a common interface with tau

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