Detection and analysis of amorphous aggregates and fibrils of cytochrome c in the presence of phenolic acids.

Cytochrome c (cyt c) exists as a partially unfolded intermediate at 45 mM gallic acid (GA) possessing disrupted secondary structure, altered Trp environment and high ANS binding. Increasing the concentration of either GA or ferulic acid (FA) up to 50 mM results in cyt c aggregation as confirmed by shift in Congo red, increase thioflavin T, decrease ANS and Trp fluorescence. SEM confirmed the formation of fibrils and amorphous aggregates of cyt c in presence of 50 mM FA and GA respectively. Single cell gel electrophoresis establishes very less probability of this noble protein to cause misfolding and aggregation-prone diseases.