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- Title
Conformational Transitions Provoked by Organic Solvents in Chicken Egg Ovalbumin: Mimicking the Local Environment.
- Authors
Iram, Afshin; Naeem, Aabgeena
- Abstract
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.
- Subjects
ORGANIC solvents; OVALBUMINS; GLYCOPROTEINS; ETHYLENE glycol; EGGS; FLUORESCENCE spectroscopy; NAPHTHALENESULFONIC acids; PROTEIN folding
- Publication
Protein Journal, 2013, Vol 32, Issue 1, p7
- ISSN
1572-3887
- Publication type
Article
- DOI
10.1007/s10930-012-9453-2