(638d) Polymeric ligand Affinity Membranes for Protein Separations: Experiments and Simulations

Liu, Z., University of Arkansas
Du, H., University of Arkansas
Wickramasinghe, S. R., University of Arkansas
Qian, X., University of Arkansas

Bisphosphonate drived ligand has a remarkable affinity for arginine (Arg) residues on protein surface. Here, a bisphosphonate derived ligand was successfully synthesized and grafted from the surface of regenerated cellulose membrane for protein separations. Atom transfer radical polymerization (ATRP) was used for surface modification of this polymeric ligand. Two types of monomers were copolymerized with different polymerization time (ATRP 1 h, 3 h and 5 h). Besides the bisphosphonate drived monomer, which was used as the functional monomer, another hydrophilic monomer N-(2-hydroxypropyl)methacrylamide(HPMA) was used for copolymerization to enhance the flexibility of the copolymer ligand and further improve specific protein adsorption. The copolymerization of this type of bisphosphonate copolymer derivatives was successful for the first time using ATRP. Static and dynamic binding capacities were determined for binding and elution of Arg rich lysozyme. The interaction mechanism between the copolymer ligand and lysozyme was elucidated using classical molecular dynamics (MD) simulations.