Aggregation of albumin: influence of the protein glycation

Abstract

Free radicals are a normal component of cellular oxygen metabolism in mammals. However, free radical-associated damage is an important factor in many pathological processes. Aggregation, glycation and oxidative damage cause protein modifications, frequently observed in numerous diseases. Albumin represents the most abundant circulating protein. Many epidemiological studies have established an inverse relationship between the level of serum albumin and the risk of death. Albumin is involved in several biological functions, including the regulation of oncotic pressure, and the binding and transport of many molecules. In addition, albumin displays potent antioxidant and free radical scavenging activities through the redox cycling of its free thiol and its ability to bind metal ions. Albumin constitutes a well-known protein capable of self-assembling in aggregates and also sensible to glycative modification especially in cases of diabetes. In this review, we firstly report the different beneficial activities exerted by albumin, a multifunctional protein