FUNCTIONALIZED MONODISPERSE PARTICLES WITH CHLOROMETHYL GROUPS FOR THE COVALENT COUPLING OF PROTEINS

The functionalized core-shell monodisperse latex particles with surfac e chloromethyl groups were synthesized by means of a two-step emulsion polymerization process in a batch reactor at two reaction temperature s. In a first step, the core was synthesized by means of a batch emuls ion polymerization of styrene (St), and in the second step, the shell was formed bg batch emulsion copolymerization of St and (chloromethyl) styrene (CMS) using the seed obtained previously. The latexes were cha racterized by TEM and conductopotentiometric titrations in order to ob tain the particle size distribution and the amount of the different su rface groups, respectively. Covalent binding of protein to chloromethy l groups was studied using lysozyme at two pHs, 7 and 11. Two differen t methods were used to determine the amount of protein covalently boun d or physically adsorbed: desorption with surfactants, and chloride io ns release upon chemical binding.