Lag phase alteration in the modified bovine serum albumin under the inducing and inhibitory effect of vitamin C

Abstract

Lag phase as the initial stage of protein aggregation has an important role in fibril formation and contributes to pathogenesis of many human diseases. Harsh environments provided by some additives can change the rate and the amounts of protein abnormalities. Here we studied the lag phase as the first stage of fibrillation process of bovine serum albumin (BSA) and determined the effects of potassium sorbate (PS) a widespread industrial preservative and vitamin C as an important antioxidant on these changes. Thioflavin T binding assay, circular dichroism, intrinsic and extrinsic fluorescence spectroscopy, and atomic force microscopy techniques were used for these assessments. Our results indicated that the lag phase of BSA fibrillation was affected under different conditions. The length of lag phase in BSA protein aggregation process was short due to the generation of the advanced glycation end products (AGEs) by PS. In contrast, vitamin C by its antioxidant properties and chaperone ability dramatically prolonged BSA lag phase, preserved BSA structural changes that lead to aggregation, and dramatically decreased formation of AGEs and the amount of fibrillation.