Abstract
AbstractThis work presents the real time surface plasmon resonance (SPR) and fluorescence spectroscopy observation of cooperative interactions between aggregate‐forming bovine serum albumin (BSA) and oppositely charged linear macromolecule poly(acrylic) acid (PAA). Interactions between protein and polymer result in formation of polyelectrolyte‐protein polycomplexes, which exhibit expressed conformational transformations, especially at low pH. The rate constants of observed kinetic transformations were calculated and found to vary in the range from 0.8 × 10−3 to 6.7 × 10−3 for different pH values. The processes of aggregation, sedimentation and conformation of BSA‐PAA complex are discussed.
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