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...
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| Veröffentlicht in: | Polymers 2023-12, Vol.16 (1), p.65 |
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| creator | Jahan, Samin Doyle, Catherine Ghimire, Anupama Combita, Diego Rainey, Jan K Wagner, Brian D Ahmed, Marya |
| 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
-(+)- and
-(-)-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. |
| doi_str_mv | 10.3390/polym16010065 |
| format | Article |
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-(+)- and
-(-)-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.</description><identifier>ISSN: 2073-4360</identifier><identifier>EISSN: 2073-4360</identifier><identifier>DOI: 10.3390/polym16010065</identifier><identifier>PMID: 38201730</identifier><language>eng</language><publisher>Switzerland: MDPI AG</publisher><subject>Acids ; Addition polymerization ; Albumin ; Analysis ; Biocompatibility ; Biomolecules ; Chain transfer ; Dichroism ; Drug delivery systems ; Drugs ; Ethylene glycol ; Fluorescence ; Fluorescence spectroscopy ; Health aspects ; High temperature ; Hydration ; Hydrophilicity ; Lysozyme ; Methacrylamide ; Molecular interactions ; Molecular weight ; NMR spectroscopy ; Optical activity ; Polyethylene glycol ; Polymerization ; Polymers ; Proteins ; Serum albumin ; Solvents ; Spectrum analysis ; Stability analysis ; Stereoisomerism ; Stereoisomers ; Surface active agents ; Thermal stability ; Trehalose ; Vehicles</subject><ispartof>Polymers, 2023-12, Vol.16 (1), p.65</ispartof><rights>COPYRIGHT 2023 MDPI AG</rights><rights>2023 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2023 by the authors. 2023</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c439t-8d62c8ee28acd6a7cd7ee9121ef3c907c5fdf05eec47b9202df416a385b14e5e3</cites><orcidid>0000-0003-4693-0724 ; 0000-0001-8227-7895 ; 0000-0003-0793-5573 ; 0000-0003-2449-7405 ; 0000-0002-1951-0209</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC10781056/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC10781056/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,881,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/38201730$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Jahan, Samin</creatorcontrib><creatorcontrib>Doyle, Catherine</creatorcontrib><creatorcontrib>Ghimire, Anupama</creatorcontrib><creatorcontrib>Combita, Diego</creatorcontrib><creatorcontrib>Rainey, Jan K</creatorcontrib><creatorcontrib>Wagner, Brian D</creatorcontrib><creatorcontrib>Ahmed, Marya</creatorcontrib><title>Elucidating the Role of Optical Activity of Polymers in Protein-Polymer Interactions</title><title>Polymers</title><addtitle>Polymers (Basel)</addtitle><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
-(+)- and
-(-)-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.</description><subject>Acids</subject><subject>Addition polymerization</subject><subject>Albumin</subject><subject>Analysis</subject><subject>Biocompatibility</subject><subject>Biomolecules</subject><subject>Chain transfer</subject><subject>Dichroism</subject><subject>Drug delivery systems</subject><subject>Drugs</subject><subject>Ethylene glycol</subject><subject>Fluorescence</subject><subject>Fluorescence spectroscopy</subject><subject>Health aspects</subject><subject>High temperature</subject><subject>Hydration</subject><subject>Hydrophilicity</subject><subject>Lysozyme</subject><subject>Methacrylamide</subject><subject>Molecular interactions</subject><subject>Molecular weight</subject><subject>NMR spectroscopy</subject><subject>Optical activity</subject><subject>Polyethylene glycol</subject><subject>Polymerization</subject><subject>Polymers</subject><subject>Proteins</subject><subject>Serum albumin</subject><subject>Solvents</subject><subject>Spectrum analysis</subject><subject>Stability analysis</subject><subject>Stereoisomerism</subject><subject>Stereoisomers</subject><subject>Surface active agents</subject><subject>Thermal stability</subject><subject>Trehalose</subject><subject>Vehicles</subject><issn>2073-4360</issn><issn>2073-4360</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2023</creationdate><recordtype>article</recordtype><sourceid>BENPR</sourceid><recordid>eNptks9rHCEUx6W0NCHNsdcy0Esvk_pr1DmVJaRtIJBQ0rO4zpuNwdGtOoH97-OQbdgt1YOPr5_3fTx9CH0k-IKxHn_dRr-biMAEY9G9QacUS9ZyJvDbg_gEnef8iOvinRBEvkcnTFFMJMOn6P7Kz9YNpriwacoDNL-ihyaOze22OGt8s7LFPbmyW7S7pRyk3LjQ3KVYwIV2rzXXoUAyFY4hf0DvRuMznO_PM_T7-9X95c_25vbH9eXqprWc9aVVg6BWAVBl7CCMtIME6AklMDLbY2m7cRhxB2C5XPcU02HkRBimujXh0AE7Q99efLfzeoLBQijJeL1NbjJpp6Nx-vgmuAe9iU-aYKkI7kR1-LJ3SPHPDLnoyWUL3psAcc6a9oRxznuFK_r5H_QxzinU_haKKqq6Q2pjPGgXxlgL28VUr6TsGZec8kpd_Ieqe4DJ2RhgdFU_SmhfEmyKOScYX5skWC-joI9GofKfDl_mlf778ewZOpWvWg</recordid><startdate>20231224</startdate><enddate>20231224</enddate><creator>Jahan, Samin</creator><creator>Doyle, Catherine</creator><creator>Ghimire, Anupama</creator><creator>Combita, Diego</creator><creator>Rainey, Jan K</creator><creator>Wagner, Brian D</creator><creator>Ahmed, Marya</creator><general>MDPI AG</general><general>MDPI</general><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7SR</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>HCIFZ</scope><scope>JG9</scope><scope>KB.</scope><scope>PDBOC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0003-4693-0724</orcidid><orcidid>https://orcid.org/0000-0001-8227-7895</orcidid><orcidid>https://orcid.org/0000-0003-0793-5573</orcidid><orcidid>https://orcid.org/0000-0003-2449-7405</orcidid><orcidid>https://orcid.org/0000-0002-1951-0209</orcidid></search><sort><creationdate>20231224</creationdate><title>Elucidating the Role of Optical Activity of Polymers in Protein-Polymer Interactions</title><author>Jahan, Samin ; Doyle, Catherine ; Ghimire, Anupama ; Combita, Diego ; Rainey, Jan K ; Wagner, Brian D ; Ahmed, Marya</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c439t-8d62c8ee28acd6a7cd7ee9121ef3c907c5fdf05eec47b9202df416a385b14e5e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2023</creationdate><topic>Acids</topic><topic>Addition polymerization</topic><topic>Albumin</topic><topic>Analysis</topic><topic>Biocompatibility</topic><topic>Biomolecules</topic><topic>Chain transfer</topic><topic>Dichroism</topic><topic>Drug delivery systems</topic><topic>Drugs</topic><topic>Ethylene glycol</topic><topic>Fluorescence</topic><topic>Fluorescence spectroscopy</topic><topic>Health aspects</topic><topic>High temperature</topic><topic>Hydration</topic><topic>Hydrophilicity</topic><topic>Lysozyme</topic><topic>Methacrylamide</topic><topic>Molecular interactions</topic><topic>Molecular weight</topic><topic>NMR spectroscopy</topic><topic>Optical activity</topic><topic>Polyethylene glycol</topic><topic>Polymerization</topic><topic>Polymers</topic><topic>Proteins</topic><topic>Serum albumin</topic><topic>Solvents</topic><topic>Spectrum analysis</topic><topic>Stability analysis</topic><topic>Stereoisomerism</topic><topic>Stereoisomers</topic><topic>Surface active agents</topic><topic>Thermal stability</topic><topic>Trehalose</topic><topic>Vehicles</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Jahan, Samin</creatorcontrib><creatorcontrib>Doyle, Catherine</creatorcontrib><creatorcontrib>Ghimire, Anupama</creatorcontrib><creatorcontrib>Combita, Diego</creatorcontrib><creatorcontrib>Rainey, Jan K</creatorcontrib><creatorcontrib>Wagner, Brian D</creatorcontrib><creatorcontrib>Ahmed, Marya</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><collection>Engineered Materials Abstracts</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>Materials Science & Engineering Collection</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Materials Science Collection</collection><collection>ProQuest Central Korea</collection><collection>SciTech Premium Collection</collection><collection>Materials Research Database</collection><collection>Materials Science Database</collection><collection>Materials Science Collection</collection><collection>Publicly Available Content Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Polymers</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Jahan, Samin</au><au>Doyle, Catherine</au><au>Ghimire, Anupama</au><au>Combita, Diego</au><au>Rainey, Jan K</au><au>Wagner, Brian D</au><au>Ahmed, Marya</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Elucidating the Role of Optical Activity of Polymers in Protein-Polymer Interactions</atitle><jtitle>Polymers</jtitle><addtitle>Polymers (Basel)</addtitle><date>2023-12-24</date><risdate>2023</risdate><volume>16</volume><issue>1</issue><spage>65</spage><pages>65-</pages><issn>2073-4360</issn><eissn>2073-4360</eissn><abstract>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
-(+)- and
-(-)-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.</abstract><cop>Switzerland</cop><pub>MDPI AG</pub><pmid>38201730</pmid><doi>10.3390/polym16010065</doi><orcidid>https://orcid.org/0000-0003-4693-0724</orcidid><orcidid>https://orcid.org/0000-0001-8227-7895</orcidid><orcidid>https://orcid.org/0000-0003-0793-5573</orcidid><orcidid>https://orcid.org/0000-0003-2449-7405</orcidid><orcidid>https://orcid.org/0000-0002-1951-0209</orcidid><oa>free_for_read</oa></addata></record> |
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| source | MDPI - Multidisciplinary Digital Publishing Institute; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central; PubMed Central Open Access |
| subjects | Acids Addition polymerization Albumin Analysis Biocompatibility Biomolecules Chain transfer Dichroism Drug delivery systems Drugs Ethylene glycol Fluorescence Fluorescence spectroscopy Health aspects High temperature Hydration Hydrophilicity Lysozyme Methacrylamide Molecular interactions Molecular weight NMR spectroscopy Optical activity Polyethylene glycol Polymerization Polymers Proteins Serum albumin Solvents Spectrum analysis Stability analysis Stereoisomerism Stereoisomers Surface active agents Thermal stability Trehalose Vehicles |
| title | Elucidating the Role of Optical Activity of Polymers in Protein-Polymer Interactions |
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