Effects of Lead-HSA interactions on fibrillation of protein
محل انتشار: پانزدهمین همایش بیوشیمی فیزیک ایران
سال انتشار: 1397
نوع سند: مقاله کنفرانسی
زبان: انگلیسی
مشاهده: 356
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شناسه ملی سند علمی:
CBC15_027
تاریخ نمایه سازی: 29 خرداد 1398
چکیده مقاله:
These days, general population is exposed to lead from air, food and other resources. So, lead (Pb) deserves special attention since this metal is the most toxic biochemical agent responsible for the world‟s most common environmental caused disease. Pb has high-affinity metal-binding proteins. It is reported that lead is a potent neurotoxin for human being especially for the developing children, and in the brains of patients with Alzheimer disease, Pb 2+ at high concentrations is found [1]. Protein-lead interaction shows that lead is capable of affecting the functional properties of proteins. In this study, the samples of protein were incubated at 68°C under physiologic pH in a water bath and the kinetic of fibril formation, changes in protein structure and reactive oxygen species generation were determined. Our studies showed the binding of Pb to HSA induced aggregation, fibril formation and caused rise to reactive oxygen species. Taking together our results and those of numerous other studies, we hypoth- esize that Pb-induced conformational changes enhances the neurotoxicity of proteins fibrils and lead to development of amyloidogenesis disease.
کلیدواژه ها:
نویسندگان
Mansooreh Mazaheri
aStandard Research Institute, Food Department, Karaj, Iran- Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran
Ali Akbar Moosavi-Movahedi
Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran- Center of Excellence in Biothermodynamics, University of Tehran, Tehran, Iran
Ali Akbar Saboury
Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran- Center of Excellence in Biothermodynamics, University of Tehran, Tehran, Iran