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Title: Effect of curcumin on amyloid-like aggregates generated from methionine-oxidized apolipoprotein A-I

Journal Article · · FEBS Open Bio
 [1];  [2];  [3];  [4];  [4];  [3];  [5]
  1. Univ. of California, Berkeley, CA (United States). Dept. of Nutritional Sciences and Toxicology
  2. Children's Hospital Oakland Research Inst., Oakland, CA (United States); Univ. of Tehran (Iran). Dept. of Biotechnology and College of Science
  3. Children's Hospital Oakland Research Inst., Oakland, CA (United States)
  4. Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States). The Molecular Foundry
  5. Univ. of California, Berkeley, CA (United States). Dept. of Nutritional Sciences and Toxicology; Children's Hospital Oakland Research Inst., Oakland, CA (United States); Univ. of Nevada, Reno, NV (United States). Dept. of Biochemistry and Molecular Biology
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Curcumin is a polyphenolic phytonutrient that has antineurodegenerative properties. Here, we investigated the anti-amyloidogenic properties of curcumin. Following incubation with curcumin, intrinsic tryptophan fluorescence emission of apolipoprotein (apo) A-I was strongly quenched. At the same time, curcumin fluorescence emission was enhanced. The fluorescence emission spectra of curcumin in the presence of amyloid-like aggregates formed by methionine-oxidized (ox) apoA-I varied, depending on whether curcumin was added before, or after, aggregate formation. The impact of curcumin on the structure of the aggregating material was revealed by the lower amount of β-structure in ox-apoA-I amyloid-like aggregates formed in the presence of curcumin, compared to aggregates formed without curcumin. However, the kinetics of ox-apoA-I amyloid-like aggregate formation was not altered by the presence of curcumin. Moreover, electron microscopy analysis detected no discernable differences in amyloid morphology when ox-apoA-I amyloid-like aggregates were formed in the presence or absence of curcumin. In conclusion, curcumin interacts with apoA-I and alters the structure of ox-apoA-I amyloid-like aggregates yet does not diminish the propensity of ox-apoA-I to form aggregates.

Research Organization:
Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States)
Sponsoring Organization:
USDOE Office of Science (SC), Basic Energy Sciences (BES); National Institutes of Health (NIH)
Grant/Contract Number:
AC02-05CH11231; R37‐HL64159; R01‐HL113059; HL115153; GM104427
OSTI ID:
1416461
Alternate ID(s):
OSTI ID: 1416605; OSTI ID: 1433116
Journal Information:
FEBS Open Bio, Journal Name: FEBS Open Bio Vol. 8 Journal Issue: 2; ISSN 2211-5463
Publisher:
Wiley Blackwell (John Wiley & Sons)Copyright Statement
Country of Publication:
Netherlands
Language:
English
Citation Metrics:
Cited by: 7 works
Citation information provided by
Web of Science

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Related Subjects

59 BASIC BIOLOGICAL SCIENCES
37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY
amyloid‐like aggregate
Apolipoprotein A‐I
curcumin
electron microscopy
fluorescence spectroscopy
methionine oxidation