Influence of Polymer Structure on Protein Partitioning in Two-Phase Aqueous Systems
Copolymers of acrylamide and styrene with two distinct structures were synthesized to study the effect of polymer structure on protein partitioning in two‐phase aqueous systems. Micellar copolymerization was used to prepare a multiblock copolymer, while homogeneous copolymerization was used to prepa...
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| Veröffentlicht in: | Biotechnology progress 1996, Vol.12 (2), p.173-177 |
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| container_title | Biotechnology progress |
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| creator | Hamad, Esam Z. Ijaz, Waseem Ali, Shaik A. Hastaoglu, Mehmet A. |
| description | Copolymers of acrylamide and styrene with two distinct structures were synthesized to study the effect of polymer structure on protein partitioning in two‐phase aqueous systems. Micellar copolymerization was used to prepare a multiblock copolymer, while homogeneous copolymerization was used to prepare a random copolymer, both with the same composition and molecular weight. Phase behavior studies of the copolymers with poly(ethylene glycol) in water showed little difference in the phase boundaries. However, the partitioning of bovine serum albumin between the two aqueous phases was sensitive to the polymer structure. A molecular picture is proposed for the interactions between the protein and block copolymers. The effect of pH on the protein partition is analyzed in terms of the hydrophobic interactions, and the polymer and protein partitioning was correlated using a model based on the Flory−Huggins theory. |
| doi_str_mv | 10.1021/bp950086d |
| format | Article |
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Micellar copolymerization was used to prepare a multiblock copolymer, while homogeneous copolymerization was used to prepare a random copolymer, both with the same composition and molecular weight. Phase behavior studies of the copolymers with poly(ethylene glycol) in water showed little difference in the phase boundaries. However, the partitioning of bovine serum albumin between the two aqueous phases was sensitive to the polymer structure. A molecular picture is proposed for the interactions between the protein and block copolymers. 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Micellar copolymerization was used to prepare a multiblock copolymer, while homogeneous copolymerization was used to prepare a random copolymer, both with the same composition and molecular weight. Phase behavior studies of the copolymers with poly(ethylene glycol) in water showed little difference in the phase boundaries. However, the partitioning of bovine serum albumin between the two aqueous phases was sensitive to the polymer structure. A molecular picture is proposed for the interactions between the protein and block copolymers. The effect of pH on the protein partition is analyzed in terms of the hydrophobic interactions, and the polymer and protein partitioning was correlated using a model based on the Flory−Huggins theory.</description><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Hydrogen-Ion Concentration</subject><subject>Interactions. 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Psychology</topic><topic>Hydrogen-Ion Concentration</topic><topic>Interactions. Associations</topic><topic>Intermolecular phenomena</topic><topic>Methods. Procedures. Technologies</topic><topic>Molecular biophysics</topic><topic>Molecular Weight</topic><topic>Others</topic><topic>Polymers - chemistry</topic><topic>Proteins - chemistry</topic><topic>Solubility</topic><topic>Solutions</topic><topic>Various methods and equipments</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hamad, Esam Z.</creatorcontrib><creatorcontrib>Ijaz, Waseem</creatorcontrib><creatorcontrib>Ali, Shaik A.</creatorcontrib><creatorcontrib>Hastaoglu, Mehmet A.</creatorcontrib><collection>Istex</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Biotechnology Research Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Biotechnology progress</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hamad, Esam Z.</au><au>Ijaz, Waseem</au><au>Ali, Shaik A.</au><au>Hastaoglu, Mehmet A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Influence of Polymer Structure on Protein Partitioning in Two-Phase Aqueous Systems</atitle><jtitle>Biotechnology progress</jtitle><addtitle>Biotechnol Progress</addtitle><date>1996</date><risdate>1996</risdate><volume>12</volume><issue>2</issue><spage>173</spage><epage>177</epage><pages>173-177</pages><issn>8756-7938</issn><eissn>1520-6033</eissn><coden>BIPRET</coden><abstract>Copolymers of acrylamide and styrene with two distinct structures were synthesized to study the effect of polymer structure on protein partitioning in two‐phase aqueous systems. 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| ispartof | Biotechnology progress, 1996, Vol.12 (2), p.173-177 |
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| language | eng |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete |
| subjects | Biological and medical sciences Biotechnology Fundamental and applied biological sciences. Psychology Hydrogen-Ion Concentration Interactions. Associations Intermolecular phenomena Methods. Procedures. Technologies Molecular biophysics Molecular Weight Others Polymers - chemistry Proteins - chemistry Solubility Solutions Various methods and equipments |
| title | Influence of Polymer Structure on Protein Partitioning in Two-Phase Aqueous Systems |
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