Al (III) metal augment thermal aggregation and fibrillation in protein: Role of metal toxicity in neurological diseases.

ABSTRACT: Protein fibrillation is a leading cause of innumerable neurodegenerative diseases. The exact underlying mechanism associated with the formation of fibrils is yet to be known. Recently, the role of metal ions resulting into fibrillation of proteins has gained attention of the scientific community. In this piece of work, we have investigated the effect of the aluminum (Al) metal ion on the kinetics of aggregation of bovine serum albumin (BSA) protein under physiological conditions by employing several biophysical and microscopic techniques. Quenching of tryptophan fluorescence was observed along with 9 nm blue shift, demonstrating BSA becomes more hydrophobic during unfolding pathway of thermal denaturation. Moreover, ANS (8-Anilino-1-naphthalene sulfonic acid) binding shows quenching in flu

SUBMITTER: Shahnawaz Khan M 

PROVIDER: S-EPMC7451595 | biostudies-literature | 2020 Sep

REPOSITORIES: biostudies-literature