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A redox cycle meets insulin fibrillation in vitro

Wang, Haojie, Ding, Han, Ma, Benhua, Chen, Zhijun
International journal of biological macromolecules 2019 v.138 pp. 89-96
amyloid, drugs, dyes, electrostatic interactions, image analysis, insulin, models, pH, spectroscopy, toxicity
Studies of amyloid proteins have gradually become a hot topic. Nevertheless, very few effective drugs and treatments is available to cope with amyloid diseases. New molecules that can inhibit the protein fibrillation are highly anticipated. Insulin is one of the popular amyloid protein research models. On the other hand, resazurin and resorufin are widely known as a redox pair. We describes here an unexpected finding that resazurin plays a role in modulating insulin fibrillation, whereas resorufin doesn't. We hypothesize that the positively charged insulin at low pH can combine with the negatively charged resazurin due to electrostatic interaction, through which resazurin inhibited the process of insulin fibrillation. This effect was characterized and verified by using various biochemical, spectroscopic and imaging tools. This inhibition of this biocompatible dye can be achieved at various stages of fibrillation, suggesting the toxicity of the protein fibrils can be eliminated by using resazurin.