The Effect of Ficol on α-lactalbumin Aggregation

Abstract

Abstract-During folding pathway surface of amino acids are available which result to abnormal interaction between protein and environment and cause to aggregation. The intra cellular aggregation forms amyloid fibrils which has been seen in Alzheimer disease, type 2 Diabte. Amyloid aggregation is produced from deposition of intermediately folded protein states. In this study we evaluated the effect of molecular crowding agent,ficol, on α-lactalbumin amyloid using light scattering spectroscopy, Tht binding assay, intrinsic fluorescence intensity, ANS binding assay and CD spectroscopy. Our results showed ficol ficol70 decreased the rate of aggregation and increased the lag phase of the reaction. The decrease of α-lactalbumin amyloid aggregation is because of reduction in non specific interaction between ficol and α -lactalbumin and environment in the presence of ficol.