Curcumin mitigates the fibrillation of human serum albumin and diminishes the formation of reactive oxygen species.

Publications // Sheibani Lab // Jan 01 2015

PubMed ID: 25666039

Author(s): Mazaheri M, Moosavi-Movahedi AA, Saboury AA, Rezaei MH, Shourian M, Farhadi M, Sheibani N. Curcumin mitigates the fibrillation of human serum albumin and diminishes the formation of reactive oxygen species. Protein Pept Lett. 2015;22(4):348-53. PMID 25666039

Journal: Protein And Peptide Letters, Volume 22, Issue 4, 2015

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.