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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… Click to show full 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 Mn = 4400 g mol−1) as well as narrower molecular weight distributions (Đ = 1.08) compared to polymerizations with the free ATRPase (Mn = 43 700 g mol−1 and a Đ of 1.23).
Journal Title: Polymer Chemistry
Year Published: 2017
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