Chlorogenic Acid Enhances the Chaperone Potential of BSA at Physiological Concentrations on Model Protein Cytochrome c.

Neurodegenerative disorders are associated with the accumulation of disease-related proteins intracellularly and extracellularly. Extracellular chaperones play a crucial role in clearing the extracellularly accumulated proteins. In this study, we observed the extracellular chaperone-like potential of BSA at physiological concentrations on model protein cytochrome c (cyt c).

Doxorubicin as a Drug Repurposing for Disruption of α-Chymotrypsinogen-A Aggregates.

Protein conformation is affected by interaction of several small molecules resulting either stabilization or disruption depending on the nature of the molecules. In our earlier communication, Hg was known to disrupt the native structure of α-Cgn A leading to aggregation (Ansari, N.K.

Methotrexate for Drug Repurposing as an Anti-Aggregatory Agent to Mercuric Treated α-Chymotrypsinogen-A.

Protein aggregation is related to numerous pathological conditions like Alzheimer's and Parkinson's disease. In our study, we have shown that an already existing FDA-approved drug; methotrexate (MTX) can be reprofiled on preformed α-chymotrypsinogen A (α-Cgn A) aggregates. The zymogen showed formation of aggregates upon interaction with mercuric ions, with increasing concentration of HgCl (0-150 µM).

Protective role of chlorogenic acid in preserving cytochrome-c stability against HFIP-induced molten globule state at physiological pH.

Numerous neurodegenerative disorders are characterized by protein misfolding and aggregation. The mechanism of protein aggregation is intricate, and it is very challenging to study at cellular level. Inhibition of protein aggregation by interfering with its pathway is one of the ways to prevent neurodegenerative diseases.