Mohsen Mahdavimehr - Department of biological sciences, institute for advanced studies in basic sciences (IASBS), Zanjan ۴۵۱۳۷-۶۶۷۳۱, Iran
Ali Akbar Meratan - Department of biological sciences, institute for advanced studies in basic sciences (IASBS), Zanjan ۴۵۱۳۷-۶۶۷۳۱, Iran
Atiyeh Ghasemi - Institute of biochemistry and biophysics, University of Tehran, Tehran, Iran
Ali Akbar Saboury - Institute of biochemistry and biophysics, University of Tehran, Tehran, Iran

Protein misfolding and aggregation is related to a large number of neurodegenerative disorders including Alzheimer‟s, Parkinson‟s, and Huntington‟s diseases. Here, we exploited Graphene Oxides (GO) as an efficient inhibitor of hen egg white lysozyme (HEWL) amyloid fibrillation. A range of amyloid-specific techniques, including thioflavin T (ThT) and 1-anilino-naphthalene 8-sulfonate (ANS) fluorescence measurements and Congo red binding assay were employed to investigate the efficacy of GO for inhibition of HEWL amyloid fibrillation. Additionally, the morphology of resultant aggregates in the absence and presence of GO were analyzed by Atomic Force Microscopy (AFM). Kinetics of HEWL amyloid formation in the absence and presence of GO demonstrated a concentration-dependent decrease in ThT fluorescence. Similarly, a pronounced dose-dependent decrease in ANS fluorescence intensity and Congo red absorbance were also observed. These results were more confirmed by AFM images, suggesting that in the presence of GO formation of mature fibrillar structures was strongly inhibited. Based on obtained results, it is concluded that GO are able to act as an effective inhibitor of HEWL amyloid fibrillation.

Hen egg white lysozyme, Graphene Oxides, Thioflavin T, Atomic force microscopy