Poster Presenter

Inhibition of structural instability and nanofibrillar aggregation of normal and glycated albumin by Alginate
Esmaeel Sharifi, Naghmeh Sattarahmady and Ali Akbar Moosavi-Movahedi
Iran

Protein aggregation processes have critical roles in biotechnological, pharmaceutical and medical industry. In these subjects, proteins may be necessary to handle and store at high concentrations and temperatures for long times. Different processes such as sterilization, pasteurization and blanching in the food and pharmaceutical industries induced thermal aggregation in proteins. Also, glycation is one of the modification reaction process, can spontaneously occur during a number of technological processes applied in industrial food processing and also in hyperglycemia condition in human body via Millard reactions. Many proteins such as albumin involved in glycation process. So, inhibition of these process is important subject to study. Here, we report characterization of aggregate and unfolding state of human serum albumin (HSA) and glycated HSA (GHSA) under temperature at the presence of dithiothreitol (DTT) that appears to play a role in the initiation of aggregation by reduction of disulfide bonds of HSA and this leads to aggregate of protein. Aggregation study and the effect of alginate (Alg) on stability of HSA and GHSA studied using absorbance, circular dichroism, fluorescence, transmission electron microscopy (TEM) and surface tension techniques. Nanofibril formation is induced by aggregation of HSA and GHSA. The results showed that the presence of Alg inhibits the pathway of nanofibril and aggregation in HSA and GHSA. In this way, Alg inhibits the aggregation process by entrapping HSA and GHSA via shell around of the protein.