Interactions between protein and stereoregular polyelectrolyte

Investigations of protein-polyelectrolyte complexes are important in the design of many biomedical applications that include enzyme immobilization, drug delivery, biosensor design, and in bioprocessing where complexation with polyelectrolytes is used to prevent protein aggregation and for protein purification. In this work, we choose to study the effect of polyelectrolyte stereochemistry on the interactions between sulfonated polystyrene (PSS) and myoglobin. We have sulfonated polystyrene with a unique stereochemical structure or tacticity, i.e (a) atactic polystyrene (aPS), and (b) isotactic polystyrene (iPS). aPS is a typical amorphous polymer and the stereochemistry of atactic polystyrene shows some long range syndiotacticity. iPS is a crystalline polymer and in solid state, it has a conformation of 3-1 helix while in gel state it is more stretched and has a helix of 12-1 conformation. The sulfonated states of aPS and iPS, ie, aPSS and iPSS are soluble in water with special local conformation. In this paper, we will report the different binding strength of PSS with myoglobin.