Biocatalytic atom transfer radical polymerization in a protein cage nanoreactor

Abstract

Incorporation of the ATRP-catalyzing enzyme horseradish peroxidase (HRP) into the cavities of the group II chaperonin thermosome is demonstrated. The resulting nanoreactor was used to polymerize an acrylate under ARGET ATRP conditions. The confined space within the protein cage results in poly(ethylene glycol) methyl ether acrylate (PEGA) with lower molecular weights (poly(styrene)-apparent M_n = 4400 g mol⁻¹) as well as narrower molecular weight distributions (Đ = 1.08) compared to polymerizations with the free ATRPase (M_n = 43 700 g mol⁻¹ and a Đ of 1.23).