Synthesizing a Hybrid Nanocomposite as an Affinity Adsorbent through Surface-Initiated Atom Transfer Radical Polymerization Catalyzed by Myoglobin

Abstract

A hybrid bifunctional core–shell nanostructure was synthesized for the first time via surface-initiated atom transfer radical polymerization (SI-ATRP) using myoglobin as a biocatalyst (ATRPase) in an aqueous solution. N -Isopropyl acrylamide (NIPA) and N -(3-aminopropyl)methacrylamide (APMA) were applied to graft flexible polymer brushes onto initiator-functionalized silica nanoparticles. Two different approaches were implemented to form the core–shell nanocomposite: (a) random copolymerization, Si@p(NIPA- co -APMA) and (b) sequential block copolymerization, Si@pNIPA- b -pAPMA. These nanocomposites can be used as versatile intermediates, thereby leading to different types of materials for targeted applications. In this work, a phenylboronic acid ligand was immobilized on the side chain of the grafted brushes during a series of postmodification reactions to create a boronate affinity adsorbent. The ability to selectively bind glycoproteins (ovalbumin and glycated hemoglobin) via boronic acid was assessed at two different temperatures (20 and 40 °C), where Si@pNIPA- b -APMA BA (163 mg OVA/g of particle) displayed an approximately 1.5-fold higher capacity than Si@p(NIPA- co -APMA) BA (107 mg OVA/g of particle). In addition to selective binding to glycoproteins, the nanocomposites exhibited selective binding for myoglobin due to the molecular imprinting effect during the postmodification process, that is, 72 and 111 mg Mb/g for Si@p(NIPA- co -APMA) BA and Si@pNIPA- b -pAPMA BA , respectively.

In Situ Preparation of Star-Shaped Protein–“Smart” Polymer Conjugates with pH and Thermo-Dual Responsibility for Bacterial Separation

“…The BSA-supported poly­(NIPAm- co -AGE) was synthesized by a copper-free SI-ATRP catalyzed by myoglobin . Briefly, BSA@Br (0.5 g), NIPAm (2.1 g, 18.0 mmol), AGE (2.1 g, 18.0 mmol), and 130 mL of deionized water were charged into a 200 mL flask, and then the sample was deoxygenized by nitrogen bubbling at 25 °C for 20 min.…”

“…The BSA-supported poly(NIPAm-co-AGE) was synthesized by a copper-free SI-ATRP catalyzed by myoglobin. 44 Briefly, BSA@Br (0.5 g), NIPAm (2.1 g, 18.0 mmol), AGE (2.1 g, 18.0 mmol), and 130 mL of deionized water were charged into a 200 mL flask, and then the sample was deoxygenized by nitrogen bubbling at 25 °C for 20 min. Then, myoglobin (482 mg, 0.03 mmol) and sodium ascorbate (640 mg, 3.2 mmol) dissolved in 20 mL of deionized water were added into the mixture and the obtained sample was nitrogen-purged for another 30 min at 25 °C.…”

“…carried negative charges, 61 the betaine with the quaternary ammonium cation was modified on the BSA affinity composite. 44 The obtained products (BSA@poly- (NIPAm-co-AGE)@Bt and BSA@poly(NIPAm-co-AGE)@ DFFPBA@Bt) were further employed in the recognition of S. aureus and Salmonella spp. in PBS (0.01 mol/mL) at pH 6.0−9.0.…”

Synthesis of artificial cells via biocatalytic polymerisation-induced self-assembly

“…46,47 A wide range of biologically derived catalysts have been employed as ATRPase, such as horseradish peroxidase, 44 laccase, 46 catalase, 47 haemoglobin (Hb), 45,48,49 and myoglobin (Mb). 50 This paves the way for a biocatalytic PISA methodology based on enzymemediated ATRP (Fig. 1a).…”

Artificial cell synthesis using biocatalytic polymerization-induced self-assembly

“…Biocatalytic ATRP (bioATRP) uses enzymes or their co-factors to initiate and control radical polymerizations and was introduced simultaneously by our group 40 , 44 , 45 and di Lena and co-workers 46 , 47 . A wide range of biologically derived catalysts have been employed as ATRPase, such as horseradish peroxidase 44 , laccase 46 , catalase 47 , haemoglobin 45 , 48 , 49 and myoglobin (Mb) 50 . This paves the way for a biocatalytic PISA methodology based on enzyme-mediated ATRP (Fig.…”