Protein amyloid aggregates – polyphenol  interaction for food and pharmaceutics application

 The misfolding of proteins and their subsequent assembly into amyloid fibrils are pathological hallmarks of different types of amyloidosis. Therefore, decoding of the aggregation processes represents a crucial step towards diagnosis and therapy of the disease. On the other hand, amyloid fibrils are considered as promising building blocks for novel biomaterials with potential applications for targeted drug delivery or improved food products. We propose a physical-chemical approach intended to characterize the interaction of polyphenols with several model protein aggregates, with emphasis on amyloid-like fibrils obtained in diverse experimental conditions (temperature, salt, pH). We will study the protein denaturation and aggregation kinetics to estimate the molecular mechanisms that govern these processes. The calorimetric and spectroscopic methods will provide new information concerning polyphenol influence on protein aggregates. The main objective of the project is the development of a young, independent research team focused on a deeper insight into the action of polyphenols on the protein aggregation process, a way to understand the features of aggregates and amyloid-like structures with applications in pharmaceutical and food industry.