Preparation of Protein A Membranes Using Propargyl Methacrylate-Based Copolymers and Copper-Catalyzed Alkyne–Azide Click Chemistry
The development of convective technologies for antibody purification is of interest to the bioprocessing industries. This study developed a Protein A membrane using a combination of graft polymerization and copper(I)-catalyzed alkyne–azide click chemistry. Regenerated cellulose supports were functio...
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| Format: | Article |
| Language: | English |
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MDPI AG
2024-01-01
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| Series: | Polymers |
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| Online Access: | https://www.mdpi.com/2073-4360/16/2/239 |
| _version_ | 1797342641218650112 |
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| author | Joshua Osuofa Scott M. Husson |
| author_facet | Joshua Osuofa Scott M. Husson |
| author_sort | Joshua Osuofa |
| collection | DOAJ |
| description | The development of convective technologies for antibody purification is of interest to the bioprocessing industries. This study developed a Protein A membrane using a combination of graft polymerization and copper(I)-catalyzed alkyne–azide click chemistry. Regenerated cellulose supports were functionalized via surface-initiated copolymerization of propargyl methacrylate (PgMA) and poly(ethylene glycol) methyl ether methacrylate (PEGMEMA<sub>300</sub>), followed by a reaction with azide-functionalized Protein A ligand. The polymer-modified membranes were characterized using attenuated total reflectance Fourier-transform infrared spectroscopy (ATR-FTIR), gravimetric analysis, and permeability measurements. Copolymer composition was determined using the Mayo–Lewis equation. Membranes clicked with azide-conjugated Protein A were evaluated by measuring static and dynamic binding (DBC<sub>10</sub>) capacities for human immunoglobulin G (hIgG). Copolymer composition and degree of grafting were found to affect maximum static binding capacities, with values ranging from 5 to 16 mg/mL. DBC<sub>10</sub> values did not vary with flow rate, as expected of membrane adsorbers. |
| first_indexed | 2024-03-08T10:37:15Z |
| format | Article |
| id | doaj.art-39118961988245b28a6e14a359d82498 |
| institution | Directory Open Access Journal |
| issn | 2073-4360 |
| language | English |
| last_indexed | 2024-03-08T10:37:15Z |
| publishDate | 2024-01-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Polymers |
| spelling | doaj.art-39118961988245b28a6e14a359d824982024-01-26T18:14:04ZengMDPI AGPolymers2073-43602024-01-0116223910.3390/polym16020239Preparation of Protein A Membranes Using Propargyl Methacrylate-Based Copolymers and Copper-Catalyzed Alkyne–Azide Click ChemistryJoshua Osuofa0Scott M. Husson1Department of Chemical and Biomolecular Engineering, Clemson University, Clemson, SC 29634, USADepartment of Chemical and Biomolecular Engineering, Clemson University, Clemson, SC 29634, USAThe development of convective technologies for antibody purification is of interest to the bioprocessing industries. This study developed a Protein A membrane using a combination of graft polymerization and copper(I)-catalyzed alkyne–azide click chemistry. Regenerated cellulose supports were functionalized via surface-initiated copolymerization of propargyl methacrylate (PgMA) and poly(ethylene glycol) methyl ether methacrylate (PEGMEMA<sub>300</sub>), followed by a reaction with azide-functionalized Protein A ligand. The polymer-modified membranes were characterized using attenuated total reflectance Fourier-transform infrared spectroscopy (ATR-FTIR), gravimetric analysis, and permeability measurements. Copolymer composition was determined using the Mayo–Lewis equation. Membranes clicked with azide-conjugated Protein A were evaluated by measuring static and dynamic binding (DBC<sub>10</sub>) capacities for human immunoglobulin G (hIgG). Copolymer composition and degree of grafting were found to affect maximum static binding capacities, with values ranging from 5 to 16 mg/mL. DBC<sub>10</sub> values did not vary with flow rate, as expected of membrane adsorbers.https://www.mdpi.com/2073-4360/16/2/239AGET ATRPaffinity chromatographyantibody purificationsurface-initiated polymerization |
| spellingShingle | Joshua Osuofa Scott M. Husson Preparation of Protein A Membranes Using Propargyl Methacrylate-Based Copolymers and Copper-Catalyzed Alkyne–Azide Click Chemistry Polymers AGET ATRP affinity chromatography antibody purification surface-initiated polymerization |
| title | Preparation of Protein A Membranes Using Propargyl Methacrylate-Based Copolymers and Copper-Catalyzed Alkyne–Azide Click Chemistry |
| title_full | Preparation of Protein A Membranes Using Propargyl Methacrylate-Based Copolymers and Copper-Catalyzed Alkyne–Azide Click Chemistry |
| title_fullStr | Preparation of Protein A Membranes Using Propargyl Methacrylate-Based Copolymers and Copper-Catalyzed Alkyne–Azide Click Chemistry |
| title_full_unstemmed | Preparation of Protein A Membranes Using Propargyl Methacrylate-Based Copolymers and Copper-Catalyzed Alkyne–Azide Click Chemistry |
| title_short | Preparation of Protein A Membranes Using Propargyl Methacrylate-Based Copolymers and Copper-Catalyzed Alkyne–Azide Click Chemistry |
| title_sort | preparation of protein a membranes using propargyl methacrylate based copolymers and copper catalyzed alkyne azide click chemistry |
| topic | AGET ATRP affinity chromatography antibody purification surface-initiated polymerization |
| url | https://www.mdpi.com/2073-4360/16/2/239 |
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