title: Detection and analysis of amorphous aggregates and fibrils of cytochrome c in the presence of phenolic acids.
abstract: 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.
authors.affiliation: Department of Biochemistry, Faculty of Life Science, Aligarh Muslim University, Aligarh, India.
authors.forename: Samreen
authors.initials: S
authors.lastname: Amani
authors.forename: Aabgeena
authors.initials: A
authors.lastname: Naeem
mesh_terms: D000818:Animals; D000975:Antioxidants / Q000737:chemistry*; D052160:Benzothiazoles; D003373:Coumaric Acids / Q000737:chemistry*; D045304:Cytochromes c / Q000737:chemistry* / Q000648:ultrastructure; D005456:Fluorescent Dyes / Q000737:chemistry; D005707:Gallic Acid / Q000737:chemistry*; D006736:Horses; D008856:Microscopy, Fluorescence; D046912:Multiprotein Complexes / Q000737:chemistry / Q000648:ultrastructure; D055503:Protein Multimerization; D055550:Protein Stability; D020836:Protein Structure, Quaternary; D017433:Protein Structure, Secondary; D057165:Proteostasis Deficiencies; D059010:Single-Cell Analysis; D013844:Thiazoles / Q000737:chemistry; D014364:Tryptophan / Q000737:chemistry
chemical_list: D000975:Antioxidants; D052160:Benzothiazoles; D003373:Coumaric Acids; D005456:Fluorescent Dyes; D046912:Multiprotein Complexes; D013844:Thiazoles; C009462:thioflavin T; D005707:Gallic Acid; D014364:Tryptophan; D045304:Cytochromes c; C004999:ferulic acid