A review on interaction of different preservatives with plasma proteins

Abstract

Blood proteins also termed as plasma proteins present in blood plasma. Plasmacontains90%waterand6- 8% proteins. The proteins in plasma include the antibody proteins, coagulation factors and the proteins ALBUMIN, FIBRINOGEN. Among those Albumin is the abundant one that act as carriers for the transportation of various macromolecules. The food preservatives and the serum albumin, the study of interaction between the two has great significance on human health. The following approaches are main source for the study of binding interactions of food preservatives (Citreoviridin, ascorbyl stearate, cinnamaldehyde, deoxynivalenol, Ascorbyl palmitate, butylated hydroxytoluene) with plasma proteins (albumin, Fibrinogen):UV–Visabsorption, circulardichroism (CD), steady-statefluorescencemethodand in-sillico techniques. Quenching mechanism is investigated through ka of reaction, the number of binding sites present in protein molecule and their thermodynamical aspects. The distance between the protein (serum albumin, fibrinogen) is obtained from FT-IR i.e. fluorescence resonance energy transfer. The approximate calculation of secondary structure makeup of unbounded serum albumin, Fibrinogen and its food preservatives complexes were done by the FT-IR spectra. This study is done to analyze the binding interactions of toxic preservatives and useful preservatives with the serum albumin via conformational changes occurring in the structure of serum albumin.