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Tytuł pozycji:

Label-Free Infrared Spectroscopic Imaging Reveals Heterogeneity of β-Sheet Aggregates in Alzheimer's Disease.

Tytuł:
Label-Free Infrared Spectroscopic Imaging Reveals Heterogeneity of β-Sheet Aggregates in Alzheimer's Disease.
Autorzy:
Confer MP; Department of Chemistry and Biochemistry, University of Alabama, Tuscaloosa AL-35401, United States.
Holcombe BM; Department of Chemistry and Biochemistry, University of Alabama, Tuscaloosa AL-35401, United States.
Foes AG; Department of Chemistry and Biochemistry, University of Alabama, Tuscaloosa AL-35401, United States.
Holmquist JM; Department of Chemistry and Biochemistry, University of Alabama, Tuscaloosa AL-35401, United States.
Walker SC; Department of Chemistry and Biochemistry, University of Alabama, Tuscaloosa AL-35401, United States.
Deb S; Department of Chemistry and Biochemistry, University of Alabama, Tuscaloosa AL-35401, United States.
Ghosh A; Department of Chemistry and Biochemistry, University of Alabama, Tuscaloosa AL-35401, United States.
Źródło:
The journal of physical chemistry letters [J Phys Chem Lett] 2021 Oct 07; Vol. 12 (39), pp. 9662-9671. Date of Electronic Publication: 2021 Sep 30.
Typ publikacji:
Journal Article
Język:
English
Imprint Name(s):
Original Publication: Washington, D.C. : American Chemical Society
MeSH Terms:
Spectrophotometry, Infrared*
Amyloid beta-Peptides/*chemistry
Alzheimer Disease/metabolism ; Alzheimer Disease/pathology ; Brain/metabolism ; Humans ; Protein Aggregates ; Protein Conformation, beta-Strand
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Grant Information:
R35 GM138162 United States GM NIGMS NIH HHS
Substance Nomenclature:
0 (Amyloid beta-Peptides)
0 (Protein Aggregates)
Entry Date(s):
Date Created: 20210930 Date Completed: 20211027 Latest Revision: 20220322
Update Code:
20240105
PubMed Central ID:
PMC8933041
DOI:
10.1021/acs.jpclett.1c02306
PMID:
34590866
Czasopismo naukowe
The aggregation of the amyloid beta (Aβ) protein into plaques is a pathological feature of Alzheimer's disease (AD). While amyloid aggregates have been extensively studied in vitro, their structural aspects and associated chemistry in the brain are not fully understood. In this report, we demonstrate, using infrared spectroscopic imaging, that Aβ plaques exhibit significant heterogeneities in terms of their secondary structure and phospholipid content. We show that the capabilities of discrete frequency infrared imaging (DFIR) are ideally suited for characterization of amyloid deposits in brain tissues and employ DFIR to identify nonplaque β-sheet aggregates distributed throughout brain tissues. We further demonstrate that phospholipid-rich β-sheet deposits exist outside of plaques in all diseased tissues, indicating their potential clinical significance. This is the very first application of DFIR toward a characterization of protein aggregates in an AD brain and provides a rapid, label-free approach that allows us to uncover β-sheet heterogeneities in the AD, which may be significant for targeted therapeutic strategies in the future.

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