DOPAC as a modulator of α-Synuclein and E46K interactions with membrane: Insights into binding dynamics.

α-Synuclein (Syn) is an intrinsically disordered protein, abundant in presynaptic neurons. It is a constituent of the Lewis Body inclusions as amyloid fibrils, in Parkinson's disease patients. It populates an ensemble of conformations and floats between the free random coil and the membrane-bound α-helical species.

Light exacerbates local and global effects induced by pH unfolding of Ipilimumab.

Monoclonal antibodies (mAbs) are an essential class of therapeutic proteins for the treatment of cancer, autoimmune and rare diseases. During their production, storage, and administration processes, these proteins encounter various stressors such as temperature fluctuations, vibrations, and light exposure, able to induce chemico-physical modifications to their structure. Viral inactivation is a key step in downstream processes, and it is achieved by titration of the mAb at low pH, followed by neutralization.