Conformational transitions provoked by organic solvents in chicken egg ovalbumin: mimicking the local environment.

Glycoprotein ovalbumin is an important protein to study helix/sheet transitions as it possess almost equal amount of α-helix and β-sheet. Conformational changes on ovalbumin at various concentrations of glyoxal, ethylene glycol (EG) and polyethylene glycol-400 (PEG-400) were investigated by fluorescence spectroscopy, circular dichroism, attenuated total reflection Fourier transform infra red spectroscopy, 8-anilino-1-naphthalenesulfonic acid and thioflavin T assay. A partially folded state of ovalbumin at 50 % v/v glyoxal was detected that preceded the onset of the aggregation process at the maximum concentration (90 % v/v) of this aldehyde. Aggregates of ovalbumin in the presence EG and PEG-400 were deduced at 70 and 80 % v/v respectively. Maximum aggregation of ovalbumin was observed at 80 % v/v PEG-400, followed by 70 % v/v EG and 90 % v/v glyoxal. Our study confirms that protein aggregation is influenced by the chemistry of organic solvent used thus follows an order of solvent effectiveness (PEG > EG > glyoxal) in inducing the transition. These results provide valuable information on the mechanisms involved in the pathogenesis of some conformational diseases. The α-helix to β-sheet conversion is a diagnostic feature of protein aggregation and has been considered as a general characteristic of amyloid fibrillogenesis in vitro.