Blood proteins in aqueous solutions
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The conformation of proteins in solution and on surfaces, as well as changes in the protein conformation caused by other molecules present in solution or external stimuli (e.g., temperature), are central to the biological activity and function of the respective proteins. Our research addresses conformation, association and interactions in aqueous solution of the blood protein fibrinogen which is involved in haemostasis and thrombosis. We are particularly interested in interactions of fibrinogen with poly (ethylene glycol) (PEG) and PEG-containing block copolymers that are known to prevent non-specific protein adsorption on surfaces. These interactions (changes in conformation of fibrinogen in aqueous solutions of synthetic water soluble polymers (PEG6000, PEO100000, Pluronic127)), we probe via a combination of Fluorescence and scattering techniques like DLS (Dynamic light scattering), SAXS (Small angle X-ray scattering) as the main experimental tools. The objective of the project was to find out the type of changes and the conditions under which these conformational changes were induced on fibrinogen. Knowledge of these interactions is very essential for pharmaceutical formulations, biocompatibility of implant materials, blood storage and transfusion, and protein separations.