Elucidating the Role of Optical Activity of Polymers in Protein–Polymer Interactions
Proteins are biomolecules with potential applications in agriculture, food sciences, pharmaceutics, biotechnology, and drug delivery. Interactions of hydrophilic and biocompatible polymers with proteins may impart proteolytic stability, improving the therapeutic effects of biomolecules and also acti...
| Main Authors: | , , , , , , |
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| Format: | Article |
| Language: | English |
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MDPI AG
2023-12-01
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| Series: | Polymers |
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| Online Access: | https://www.mdpi.com/2073-4360/16/1/65 |
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| author | Samin Jahan Catherine Doyle Anupama Ghimire Diego Combita Jan K. Rainey Brian D. Wagner Marya Ahmed |
| author_facet | Samin Jahan Catherine Doyle Anupama Ghimire Diego Combita Jan K. Rainey Brian D. Wagner Marya Ahmed |
| author_sort | Samin Jahan |
| collection | DOAJ |
| description | Proteins are biomolecules with potential applications in agriculture, food sciences, pharmaceutics, biotechnology, and drug delivery. Interactions of hydrophilic and biocompatible polymers with proteins may impart proteolytic stability, improving the therapeutic effects of biomolecules and also acting as excipients for the prolonged storage of proteins under harsh conditions. The interactions of hydrophilic and stealth polymers such as poly(ethylene glycol), poly(trehalose), and zwitterionic polymers with various proteins are well studied. This study evaluates the molecular interactions of hydrophilic and optically active poly(vitamin B5 analogous methacrylamide) (poly(B5AMA)) with model proteins by fluorescence spectroscopy, nuclear magnetic resonance (NMR) spectroscopy, and circular dichroism (CD) spectroscopy analysis. The optically active hydrophilic polymers prepared using chiral monomers of <i>R</i>-(+)- and <i>S</i>-(−)-B5AMA by the photo-iniferter reversible addition fragmentation chain transfer (RAFT) polymerization showed concentration-dependent weak interactions of the polymers with bovine serum albumin and lysozyme proteins. Poly(B5AMA) also exhibited a concentration-dependent protein stabilizing effect at elevated temperatures, and no effect of the stereoisomers of polymers on protein thermal stability was observed. NMR analysis, however, showed poly(B5AMA) stereoisomer-dependent changes in the secondary structure of proteins. |
| first_indexed | 2024-03-08T14:58:56Z |
| format | Article |
| id | doaj.art-043e32eb558248b0bc8490688f9164ec |
| institution | Directory Open Access Journal |
| issn | 2073-4360 |
| language | English |
| last_indexed | 2024-03-08T14:58:56Z |
| publishDate | 2023-12-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Polymers |
| spelling | doaj.art-043e32eb558248b0bc8490688f9164ec2024-01-10T15:06:42ZengMDPI AGPolymers2073-43602023-12-011616510.3390/polym16010065Elucidating the Role of Optical Activity of Polymers in Protein–Polymer InteractionsSamin Jahan0Catherine Doyle1Anupama Ghimire2Diego Combita3Jan K. Rainey4Brian D. Wagner5Marya Ahmed6Department of Chemistry, University of Prince Edward Island, Charlottetown, PE C1A 4P3, CanadaDepartment of Chemistry, University of Prince Edward Island, Charlottetown, PE C1A 4P3, CanadaDepartment of Biochemistry & Molecular Biology, Dalhousie University, Halifax, NS B3H 4R2, CanadaDepartment of Chemistry, University of Prince Edward Island, Charlottetown, PE C1A 4P3, CanadaDepartment of Biochemistry & Molecular Biology, Dalhousie University, Halifax, NS B3H 4R2, CanadaDepartment of Chemistry, University of Prince Edward Island, Charlottetown, PE C1A 4P3, CanadaDepartment of Chemistry, University of Prince Edward Island, Charlottetown, PE C1A 4P3, CanadaProteins are biomolecules with potential applications in agriculture, food sciences, pharmaceutics, biotechnology, and drug delivery. Interactions of hydrophilic and biocompatible polymers with proteins may impart proteolytic stability, improving the therapeutic effects of biomolecules and also acting as excipients for the prolonged storage of proteins under harsh conditions. The interactions of hydrophilic and stealth polymers such as poly(ethylene glycol), poly(trehalose), and zwitterionic polymers with various proteins are well studied. This study evaluates the molecular interactions of hydrophilic and optically active poly(vitamin B5 analogous methacrylamide) (poly(B5AMA)) with model proteins by fluorescence spectroscopy, nuclear magnetic resonance (NMR) spectroscopy, and circular dichroism (CD) spectroscopy analysis. The optically active hydrophilic polymers prepared using chiral monomers of <i>R</i>-(+)- and <i>S</i>-(−)-B5AMA by the photo-iniferter reversible addition fragmentation chain transfer (RAFT) polymerization showed concentration-dependent weak interactions of the polymers with bovine serum albumin and lysozyme proteins. Poly(B5AMA) also exhibited a concentration-dependent protein stabilizing effect at elevated temperatures, and no effect of the stereoisomers of polymers on protein thermal stability was observed. NMR analysis, however, showed poly(B5AMA) stereoisomer-dependent changes in the secondary structure of proteins.https://www.mdpi.com/2073-4360/16/1/65chiral materialsprotein–polymer interactionsantifoulingprotein stabilizing |
| spellingShingle | Samin Jahan Catherine Doyle Anupama Ghimire Diego Combita Jan K. Rainey Brian D. Wagner Marya Ahmed Elucidating the Role of Optical Activity of Polymers in Protein–Polymer Interactions Polymers chiral materials protein–polymer interactions antifouling protein stabilizing |
| title | Elucidating the Role of Optical Activity of Polymers in Protein–Polymer Interactions |
| title_full | Elucidating the Role of Optical Activity of Polymers in Protein–Polymer Interactions |
| title_fullStr | Elucidating the Role of Optical Activity of Polymers in Protein–Polymer Interactions |
| title_full_unstemmed | Elucidating the Role of Optical Activity of Polymers in Protein–Polymer Interactions |
| title_short | Elucidating the Role of Optical Activity of Polymers in Protein–Polymer Interactions |
| title_sort | elucidating the role of optical activity of polymers in protein polymer interactions |
| topic | chiral materials protein–polymer interactions antifouling protein stabilizing |
| url | https://www.mdpi.com/2073-4360/16/1/65 |
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