Study of interfacial rheology and fibrillization kinetics of insulin in the deep-channel surface viscometer

Abstract

The transformation of proteins from its native to aggregated form has been a major subject of research in recent years because of its increasing relevance in pathology. Large number of cases have been reported where amyloid plaque deposits have been found in people diagnosed with diseases like Alzheimer’s, Parkinson’s, Prion’s and Type II diabetes, to name a few. Fibrillization is a process by which monomeric protein transforms to crystalline fibrillar aggregates under the action of some external perturbation. While the protein’s inherent structure and sequence plays a major role in determining its propensity to undergo the fibrillization process, there are several environmental factors that can also affect the transformation. Extreme pH, temperature and pressure are all been found to facilitate fibrillization. While the effect of such factors are thoroughly studied under laboratory conditions, they fail to enhance our understanding of fibrillization process inside the human body where these conditions stay relatively constant. Protein interactions at interface and fluid flow are tipped as driving factors for fibrillization in-vivo.