immunology & Biochemistry
hassan Ramshini
Volume 28, Issue 2 , May and June 2021, , Pages 232-241
Abstract
Introduction: The accumulation of amyloid aggregates in the brain are associated with numerous neurodegenerative disorders. Several nanoparticles (NP) have been using for treatment of neurological disease. Metal nanoparticles can be modified through the construction of bimetallic architectures consisting ...
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Introduction: The accumulation of amyloid aggregates in the brain are associated with numerous neurodegenerative disorders. Several nanoparticles (NP) have been using for treatment of neurological disease. Metal nanoparticles can be modified through the construction of bimetallic architectures consisting of two distinct metals that their properties can be dramatically different from those of the corresponding single-component particles. At the present study, we evaluated the effect of the bimetallic Au/Ag nanoparticles on hen lysozyme amyloid aggregation as a model protein for amyloid formation . Materials and Methods: In this experimental study, to induce amyloid formation, Acidic pH and high temperatures were used. Hen egg white lysozyme (HEWL) was dissolved at 2 mg/mL in 50mM glycine buffer (pH 2.5), and then incubated at 57 °C for the specified durations. The inhibitory effect of the nanoparticles against HEWL fibrillation using and ThT (thioflavin T), Congo red and MTT assay was investigated . Results: ThT assay showed that the particles are able to inhibit HEWL aggregation in a pattern of inverse dose-dependent inhibition and with the best inhibitory concentration 0.01 µg/ml. Kinetic study of showed that the particles caused lag phase do not change but stationary phase decreased and also cytotoxic activity of HEWL aggregates in presence of Au/Ag nanoparticleswas significantly diminished (P˂0.05) . Conclusions: We anticipate that based on obtained insights in design of new bimetallic nanoparticles, rationally design of effective NP-based therapeutics for neurodegenerative diseases may be a feasible perspective .
immunology & Biochemistry
Hassan Ramshini; Shahryar Saeidian; Leila Nazemian
Volume 27, Issue 1 , May and June 2020, , Pages 55-63
Abstract
Backgrounds & Objectives: Alzheimer's disease is of major concern all over the world due to a number of factors including (i) an aging population (ii) increasing life span and (iii) lack of effective pharmacotherapy options. Aromatic small molecules have been found to play a neuroprotective role ...
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Backgrounds & Objectives: Alzheimer's disease is of major concern all over the world due to a number of factors including (i) an aging population (ii) increasing life span and (iii) lack of effective pharmacotherapy options. Aromatic small molecules have been found to play a neuroprotective role by inhibiting and/or modifying the self-assembly of peptide or proteins into oligomers and fibrils, which are linked to the pathogenesis of the diseases. In this study, the inhibitory effects of 1,3, 5 triphenyl benzene as an aromatic molecule on aggregation and neurotoxicity of hen egg white lysozyme (HEWL) was investigated.Methods: Acidic pH and high temperatures were used to drive the protein towards amyloid formation. Lysozyme was dissolved at 2 mg/mL in 50mM glycine buffer (pH 2.5), and then incubated at 57 °C for the specified durations. The inhibitory effect of the compounds against hen egg white lysozyme (HEWL) fibrillation using AFM (atomic force microscope), ThT (thioflavin T), Congo red and MTT assay was investigated.Results: We found that the compounds is able to inhibit HEWL aggregation in a dose-dependent manner with IC50 0.1 µM. Kinetic study of the compound caused lag phase prolonged and stationary phase decreased and also cytotoxic activity of HEWL aggregates in presence of the compounds was diminished.Conclusions: These observations suggest that 1,3,5 triphenyl benzene is capable to insert directly into amyloidogenic core of early aggregates and inhibiting amyloid fibril formation.