Biophysical insights into the aggregation mechanism of ovalbumin
Manjumol Mathew, Charuvila T. Aravindakumar, Usha K. Aravind
This work illustrates the possible share of environmental toxins in inducing protein misfolding and hence protein aggregation. This is brought out by the interaction studies of ovalbumin (OVA) with mercuric chloride (denaturant) using time resolved, steady state, atomic force microscopy spectroscopy (AFM). The steady state quenching experiments showed a three state sigmoidal transition pattern indicates a concentration dependent quenching. More insight about the fibrillation pathway at molten globule state is brought out using AFM studies. Various oligomeric structures of OVA are encountered during the study with the addition of different concentrations of HgCl2.Time dependent atomic force microscopy study exposed the formation of fibrils in the end state.
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