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Effect of curcumin on amyloid-like aggregates generated from methionine-oxidized apolipoprotein A-I.
Krishnamoorthy, Aparna; Tavoosi, Narjes; Chan, Gary K L; Liu, Jianfang; Ren, Gang; Cavigiolio, Giorgio; Ryan, Robert O.
Afiliação
  • Krishnamoorthy A; Department of Nutritional Sciences and Toxicology University of California Berkeley CA USA.
  • Tavoosi N; Children's Hospital Oakland Research Institute CA USA.
  • Chan GKL; Present address: Department of Biotechnology College of Science University of Tehran Iran.
  • Liu J; Children's Hospital Oakland Research Institute CA USA.
  • Ren G; Lawrence Berkeley National Laboratory The Molecular Foundry Berkeley CA USA.
  • Cavigiolio G; Lawrence Berkeley National Laboratory The Molecular Foundry Berkeley CA USA.
  • Ryan RO; Children's Hospital Oakland Research Institute CA USA.
FEBS Open Bio ; 8(2): 302-310, 2018 02.
Article em En | MEDLINE | ID: mdl-29435420
Curcumin is a polyphenolic phytonutrient that has antineurodegenerative properties. In this study, 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 ß-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.
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Texto completo: 1 Bases de dados: MEDLINE Idioma: En Revista: FEBS Open Bio Ano de publicação: 2018 Tipo de documento: Article

Texto completo: 1 Bases de dados: MEDLINE Idioma: En Revista: FEBS Open Bio Ano de publicação: 2018 Tipo de documento: Article