Hemoglobin and Red Blood Cells Catalyze Atom Transfer Radical Polymerization

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• 作者：Tilana B. Silva ; Mariana Spulber ; Marzena K. Kocik ; Farzad Seidi ; Himanshu Charan ; Martin Rother ; Severin J. Sigg ; Kasper Renggli ; Gergely Kali ; Nico Bruns
• 刊名：Biomacromolecules
• 出版年：2013
• 出版时间：August 12, 2013
• 年：2013
• 卷：14
• 期：8
• 页码：2703-2712
• 全文大小：448K
• 年卷期：v.14,no.8(August 12, 2013)
• ISSN：1526-4602

文摘

Hemoglobin (Hb) is a promiscuous protein that not only transports oxygen, but also catalyzes several biotransformations. A novel in vitro catalytic activity of Hb is described. Bovine Hb and human erythrocytes were found to display ATRPase activity, i.e., they catalyzed the polymerization of vinyl monomers under conditions typical for atom transfer radical polymerization (ATRP). N-isopropylacrylamide (NIPAAm), poly(ethylene glycol) methyl ether acrylate (PEGA), and poly(ethylene glycol) methyl ether methacrylate (PEGMA) were polymerized using organobromine initiators and the reducing agent ascorbic acid in acidic aqueous solution. In order to avoid chain transfer from polymer radicals to Hb鈥檚 cysteine residues, the accessible cysteines were blocked by a reaction with a maleimide. The formation of polymers with bromine chain ends, relatively low polydispersity indices (PDI), first order kinetics and an increase in the molecular weight of poly(PEGA) and poly(PEGMA) upon conversion indicate that control of the polymerization by Hb occurred via reversible atom transfer between the protein and the growing polymer chain. For poly(PEGA) and poly(PEGMA), the reactions proceeded with a good to moderate degree of control. Sodium dodecyl sulfate (SDS) gel electrophoresis, circular dichroism spectroscopy, and time-resolved ultraviolet鈥搗isible (UV鈥搗is) spectroscopy revealed that the protein was stable during polymerization, and only underwent minor conformational changes. As Hb and erythrocytes are readily available, environmentally friendly, and nontoxic, their ATRPase activity is a useful tool for synthetic polymer chemistry. Moreover, this novel activity enhances the understanding of Hb鈥檚 redox chemistry in the presence of organobromine compounds.