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Protein & Peptide Letters

Editor-in-Chief

ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

Curcumin Mitigates the Fibrillation of Human Serum Albumin and Diminishes the Formation of Reactive Oxygen Species

Author(s): Mansooreh Mazaheri, Ali Akbar Moosavi-Movahedi, Ali Akbar Saboury, Mehran Habibi Rezaei, Mostafa Shourian, Mohammad Farhadi and Nader Sheibani

Volume 22, Issue 4, 2015

Page: [348 - 353] Pages: 6

DOI: 10.2174/0929866522666150209150004

Price: $65

Abstract

The formation of amyloid fibrils are thought to contribute to pathogenesis of many amyloids associated human diseases. Here the impact of curcumin on amyloid formation of human serum albumin (HSA) was studied. Incubation of HSA at 68°C under physiologic pH led to amyloid fibril formation. Thioflavin T (ThT) fluorescence was used for determination of amyloid fibril formation. Atomic force microscopy experiments indicated different fibril structure of HSA incubated with or without curcumin. The monitoring of the changes in reactive oxygen species (ROS) levels upon incubation of curcumin with HSA showed a significant decrease in ROS levels. Similar experiments were also carried out in the presence of aflatoxin M1 (AFM1) and lead (Pb) ions. Our results indicated that AFM1 and Pb ions promote the fibrillation of HSA and accelerate ROS production, which were inhibited in the presence of curcumin. Thus, curcumin mitigates protein fibrillation activity and diminishes ROS generation.

Keywords: Aflatoxin M1, curcumin, fibrillation, HSA, lead ions, ROS.

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