Hydrogen Sulfide Limits Amyloids Development in Myoglobin and Hemoglobin
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abstract
Conformational diseases are characterized by structural conversion of proteins to alternative forms, which subsequently convert into protein fibrils. The accumulation of these protein fibrils as amyloid deposits in the brain is implicated in a number of neurodegenerative diseases, including Alzheimer's, Parkinson's and Huntington's, among others. The levels of hydrogen sulfide (H2S) is notoriously low in brain tissue of patients with Alzheimer's disease compare to healthy people. These outcomes encouraged to study the effects of H2S on the formation of amyloids in vitro, using model proteins myoglobin (Mb) and Hemoglobin (Hb). Amyloid formation of Mb and Hb upon addition of 2,2,2-trifluoroethanol (TFE) in 45 %v/v were analyzed using Thioflavin T (ThT) fluorescence spectroscopy and Circular Dichroism (CD). ThT data of Mb and Hb in presence of 45 %v/v TFE reveals the rapid increment in fluorescence intensity after 180 minutes, indicating the formation of amyloid fibrils under the studied conditions. Furthermore, CD spectra of Mb and Hb confirms ?-sheet conformation indicating the formation of amyloid fibrils. Overall, the data suggest that under the previous conditions Mb and Hb can transform their structures to fibrils derivatives. It was also studied the effect of H2S in the formation of amyloid-like fibrils. The addition of H2S completely inhibits the formation of ?-sheet and amyloid fibrils in Mb and Hb, as revealed by Circular dichroism spectroscopy and ThT fluorescence intensity. The data indicates that H2S inhibition effect is concentration-dependent for myoglobin and hemoglobin fibril formation.
