title: Electric field induced changes in protein conformation.
abstract: The effect of a low strength oscillating electric field on the conformation of Bovine Serum Albumin (BSA) and Lysozyme in solution has been measured. A purpose built cell has been used to measure the real time autofluorescence and Circular Dichroism of the protein solutions exposed to electric fields of differing strength and frequency. Exposure to the electric fields results in protein unfolding for both Lysozyme and BSA. The applied field strengths are extremely small compared to the protein inter-chain intra-molecular forces. We propose a model whereby the electrophoretic motion of the proteins leads to a frictional force that results in protein unfolding. For BSA and Lysozyme in the electric fields used in this study, the shear rates at the protein surface under electrophoretic motion are of order 10(3) and 10(4) s(-1) respectively. Prolonged electric field exposure results in significant frictional energy dissipation in the proteins. The energy dissipated in the proteins results in protein unfolding, which is a critical initial step for protein aggregation and potentially amyloid fibril formation.
authors.affiliation: CSL Behring, 189-209 Camp Road, Broadmeadows, Victoria, 3047, Australia.
authors.forename: Innocent
authors.initials: I
authors.lastname: Bekard
authors.forename: Dave E
authors.initials: DE
authors.lastname: Dunstan
mesh_terms: D000818:Animals; D002417:Cattle; D002645:Chickens; D004560:Electricity; D006860:Hydrogen Bonding; D006863:Hydrogen-Ion Concentration; D009113:Muramidase / Q000737:chemistry* / Q000378:metabolism; D017434:Protein Structure, Tertiary; D058767:Protein Unfolding; D012710:Serum Albumin, Bovine / Q000737:chemistry* / Q000378:metabolism; D013696:Temperature
chemical_list: D012710:Serum Albumin, Bovine; D009113:Muramidase