Export to Refworks Export to EndNote Email
Report an Issue

Effect of curcumin on amyloid-like aggregates generated from methionine-oxidized apolipoprotein A-I [electronic resource].

Published:
Washington, D.C. : United States. Dept. of Energy. Office of Basic Energy Sciences, 2018.
Oak Ridge, Tenn. : Distributed by the Office of Scientific and Technical Information, U.S. Dept. of Energy
Physical Description:
pages 302-310 : digital, PDF file
Additional Creators:
Lawrence Berkeley National Laboratory, United States. Department of Energy. Office of Basic Energy Sciences, National Institutes of Health (U.S.), and United States. Department of Energy. Office of Scientific and Technical Information
Access Online

Availability

I Want It

Finding items...

Restrictions on Access:
Free-to-read Unrestricted online access
Summary:
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.
Report Numbers:
E 1.99:1433116
Subject(s):
Other Subject(s):
Note:
Published through SciTech Connect.
01/10/2018.
"ark:/13030/qt1kn0m90d"
FEBS Open Bio 8 2 ISSN 2211-5463 AM
Aparna Krishnamoorthy; Narjes Tavoosi; Gary K. L. Chan; Jianfang Liu; Gang Ren; Giorgio Cavigiolio; Robert O. Ryan.
Funding Information:
AC02-05CH11231
R37‐HL64159
R01‐HL113059
HL115153
GM104427
View MARC record | catkey: 23498658