Tuning physical properties of polyurethane hard segments through extender chain length variation and doping of pentaerythritol and their effect on in vitro protein adsorption
This study explores the synthesis and characterization of polyurethanes (PUs) derived from hexamethylene diisocyanate (HDI) and 1,n‐alkane diols with varying chain lengths (n = 4, 6, and 10). Additionally, pentaerythritol (PE) is introduced as a dopant in PU6 at different weight percentages (25%, 50...
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description | This study explores the synthesis and characterization of polyurethanes (PUs) derived from hexamethylene diisocyanate (HDI) and 1,n‐alkane diols with varying chain lengths (n = 4, 6, and 10). Additionally, pentaerythritol (PE) is introduced as a dopant in PU6 at different weight percentages (25%, 50%, 75%, and 1:1%w/w). The research encompasses a comprehensive analysis of PU properties, including morphology, crystallinity, surface area, porosity, thermal behavior, rheological properties, and electrical conductivity. Of particular interest is the evaluation of protein adsorption capabilities employing bovine serum albumin (BSA) and fibrinogen proteins in in vitro tests. The study emphasizes the crucial role played by the chain length between isocyanate and diol groups and the nature and strength of hydrogen bonds among chains in shaping the polymer's properties, especially crystallinity and biocompatibility. Among the synthesized PUs, PU6 emerges as the top performer in terms of crystallinity and biocompatibility. Furthermore, the addition of PE is found to act as a plasticizer, reducing the glass transition temperature (Tg) from 75°C to 31°C. Electrochemical Impedance Spectroscopy shows that doping influences charge transfer processes, rendering the material semi‐conducting, as evidenced by decreased conductance when adding silver nanoparticles to PU6. Notably, protein adsorption studies reveal that undoped PU6 displays superior protein resistance compared to its doped counterpart, with fibrinogen exhibiting a higher adsorption affinity than BSA. The study discusses a plausible mechanism underlying protein adsorption.
Polymer surface for protein adsorption resistance can be tuned! |
doi_str_mv | 10.1002/app.54982 |
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Polymer surface for protein adsorption resistance can be tuned!</description><identifier>ISSN: 0021-8995</identifier><identifier>EISSN: 1097-4628</identifier><identifier>DOI: 10.1002/app.54982</identifier><language>eng</language><publisher>Hoboken, USA: John Wiley & Sons, Inc</publisher><subject>Adsorption ; Alkanes ; Biocompatibility ; Bonding strength ; Charge transfer ; Crystallinity ; Diols ; Doping ; Electrical resistivity ; Electrochemical impedance spectroscopy ; Fibrinogen ; Glass transition temperature ; Hexamethylene diisocyanate ; Hydrogen bonds ; In vitro methods and tests ; Isocyanates ; Physical properties ; Polyethylenes ; Polyurethane ; Polyurethane resins ; polyurethanes ; Protein adsorption ; protein adsorption resistance ; Proteins ; pseudocapacitors ; Rheological properties ; Serum albumin ; Silver ; Thermodynamic properties</subject><ispartof>Journal of applied polymer science, 2024-02, Vol.141 (8), p.n/a</ispartof><rights>2023 Wiley Periodicals LLC.</rights><rights>2024 Wiley Periodicals LLC.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c3112-faa7080fcfc5d500f7128b1c7ae9e08ca19e34cdee0a2a37c8d8c432492915923</cites><orcidid>0000-0002-6017-9706</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fapp.54982$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fapp.54982$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,777,781,1412,27905,27906,45555,45556</link.rule.ids></links><search><creatorcontrib>Wagh, Shrish G.</creatorcontrib><creatorcontrib>Sahani, Mayur H.</creatorcontrib><creatorcontrib>Soni, Hemant P.</creatorcontrib><title>Tuning physical properties of polyurethane hard segments through extender chain length variation and doping of pentaerythritol and their effect on in vitro protein adsorption</title><title>Journal of applied polymer science</title><description>This study explores the synthesis and characterization of polyurethanes (PUs) derived from hexamethylene diisocyanate (HDI) and 1,n‐alkane diols with varying chain lengths (n = 4, 6, and 10). Additionally, pentaerythritol (PE) is introduced as a dopant in PU6 at different weight percentages (25%, 50%, 75%, and 1:1%w/w). The research encompasses a comprehensive analysis of PU properties, including morphology, crystallinity, surface area, porosity, thermal behavior, rheological properties, and electrical conductivity. Of particular interest is the evaluation of protein adsorption capabilities employing bovine serum albumin (BSA) and fibrinogen proteins in in vitro tests. The study emphasizes the crucial role played by the chain length between isocyanate and diol groups and the nature and strength of hydrogen bonds among chains in shaping the polymer's properties, especially crystallinity and biocompatibility. Among the synthesized PUs, PU6 emerges as the top performer in terms of crystallinity and biocompatibility. Furthermore, the addition of PE is found to act as a plasticizer, reducing the glass transition temperature (Tg) from 75°C to 31°C. Electrochemical Impedance Spectroscopy shows that doping influences charge transfer processes, rendering the material semi‐conducting, as evidenced by decreased conductance when adding silver nanoparticles to PU6. Notably, protein adsorption studies reveal that undoped PU6 displays superior protein resistance compared to its doped counterpart, with fibrinogen exhibiting a higher adsorption affinity than BSA. The study discusses a plausible mechanism underlying protein adsorption.
Polymer surface for protein adsorption resistance can be tuned!</description><subject>Adsorption</subject><subject>Alkanes</subject><subject>Biocompatibility</subject><subject>Bonding strength</subject><subject>Charge transfer</subject><subject>Crystallinity</subject><subject>Diols</subject><subject>Doping</subject><subject>Electrical resistivity</subject><subject>Electrochemical impedance spectroscopy</subject><subject>Fibrinogen</subject><subject>Glass transition temperature</subject><subject>Hexamethylene diisocyanate</subject><subject>Hydrogen bonds</subject><subject>In vitro methods and tests</subject><subject>Isocyanates</subject><subject>Physical properties</subject><subject>Polyethylenes</subject><subject>Polyurethane</subject><subject>Polyurethane resins</subject><subject>polyurethanes</subject><subject>Protein adsorption</subject><subject>protein adsorption resistance</subject><subject>Proteins</subject><subject>pseudocapacitors</subject><subject>Rheological properties</subject><subject>Serum albumin</subject><subject>Silver</subject><subject>Thermodynamic properties</subject><issn>0021-8995</issn><issn>1097-4628</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2024</creationdate><recordtype>article</recordtype><recordid>eNp1kcFu2zAMhoWhA5ZmO-wNBOzUg1NJtmPrGARbO6BAe8jOBidTsQpXUiU5m19qz1g52bUnguD3_yT4E_KVsw1nTNyC95u6kq34QFacyaaotqK9Iqs840UrZf2JXMf4zBjnNduuyL_DZI09Uj_M0SgYqQ_OY0gGI3WaejfOU8A0gEU6QOhpxOML2hRpGoKbjgPFvwltj4GqAYylI9pjGugJgoFknKVge9o7vyxZDLMWMMxZbZIbz9M0oAkUtUaVaFZkl5NJwS23JMwd9NEFv7h9Jh81jBG__K9r8uvH98P-vnh4vPu53z0UquRcFBqgYS3TSqu6rxnTDRftb64aQImsVcAllpXqERkIKBvV9q2qSlFJIXktRbkm3y6--YTXCWPqnt0UbF7ZZaJq8lebbaZuLpQKLsaAuvPBvECYO866JY4ux9Gd48js7YX9Y0ac3we73dPTRfEGAgiRvA</recordid><startdate>20240220</startdate><enddate>20240220</enddate><creator>Wagh, Shrish G.</creator><creator>Sahani, Mayur H.</creator><creator>Soni, Hemant P.</creator><general>John Wiley & Sons, Inc</general><general>Wiley Subscription Services, Inc</general><scope>AAYXX</scope><scope>CITATION</scope><scope>7SR</scope><scope>8FD</scope><scope>JG9</scope><orcidid>https://orcid.org/0000-0002-6017-9706</orcidid></search><sort><creationdate>20240220</creationdate><title>Tuning physical properties of polyurethane hard segments through extender chain length variation and doping of pentaerythritol and their effect on in vitro protein adsorption</title><author>Wagh, Shrish G. ; Sahani, Mayur H. ; Soni, Hemant P.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3112-faa7080fcfc5d500f7128b1c7ae9e08ca19e34cdee0a2a37c8d8c432492915923</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2024</creationdate><topic>Adsorption</topic><topic>Alkanes</topic><topic>Biocompatibility</topic><topic>Bonding strength</topic><topic>Charge transfer</topic><topic>Crystallinity</topic><topic>Diols</topic><topic>Doping</topic><topic>Electrical resistivity</topic><topic>Electrochemical impedance spectroscopy</topic><topic>Fibrinogen</topic><topic>Glass transition temperature</topic><topic>Hexamethylene diisocyanate</topic><topic>Hydrogen bonds</topic><topic>In vitro methods and tests</topic><topic>Isocyanates</topic><topic>Physical properties</topic><topic>Polyethylenes</topic><topic>Polyurethane</topic><topic>Polyurethane resins</topic><topic>polyurethanes</topic><topic>Protein adsorption</topic><topic>protein adsorption resistance</topic><topic>Proteins</topic><topic>pseudocapacitors</topic><topic>Rheological properties</topic><topic>Serum albumin</topic><topic>Silver</topic><topic>Thermodynamic properties</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wagh, Shrish G.</creatorcontrib><creatorcontrib>Sahani, Mayur H.</creatorcontrib><creatorcontrib>Soni, Hemant P.</creatorcontrib><collection>CrossRef</collection><collection>Engineered Materials Abstracts</collection><collection>Technology Research Database</collection><collection>Materials Research Database</collection><jtitle>Journal of applied polymer science</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wagh, Shrish G.</au><au>Sahani, Mayur H.</au><au>Soni, Hemant P.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Tuning physical properties of polyurethane hard segments through extender chain length variation and doping of pentaerythritol and their effect on in vitro protein adsorption</atitle><jtitle>Journal of applied polymer science</jtitle><date>2024-02-20</date><risdate>2024</risdate><volume>141</volume><issue>8</issue><epage>n/a</epage><issn>0021-8995</issn><eissn>1097-4628</eissn><abstract>This study explores the synthesis and characterization of polyurethanes (PUs) derived from hexamethylene diisocyanate (HDI) and 1,n‐alkane diols with varying chain lengths (n = 4, 6, and 10). Additionally, pentaerythritol (PE) is introduced as a dopant in PU6 at different weight percentages (25%, 50%, 75%, and 1:1%w/w). The research encompasses a comprehensive analysis of PU properties, including morphology, crystallinity, surface area, porosity, thermal behavior, rheological properties, and electrical conductivity. Of particular interest is the evaluation of protein adsorption capabilities employing bovine serum albumin (BSA) and fibrinogen proteins in in vitro tests. The study emphasizes the crucial role played by the chain length between isocyanate and diol groups and the nature and strength of hydrogen bonds among chains in shaping the polymer's properties, especially crystallinity and biocompatibility. Among the synthesized PUs, PU6 emerges as the top performer in terms of crystallinity and biocompatibility. Furthermore, the addition of PE is found to act as a plasticizer, reducing the glass transition temperature (Tg) from 75°C to 31°C. Electrochemical Impedance Spectroscopy shows that doping influences charge transfer processes, rendering the material semi‐conducting, as evidenced by decreased conductance when adding silver nanoparticles to PU6. Notably, protein adsorption studies reveal that undoped PU6 displays superior protein resistance compared to its doped counterpart, with fibrinogen exhibiting a higher adsorption affinity than BSA. The study discusses a plausible mechanism underlying protein adsorption.
Polymer surface for protein adsorption resistance can be tuned!</abstract><cop>Hoboken, USA</cop><pub>John Wiley & Sons, Inc</pub><doi>10.1002/app.54982</doi><tpages>21</tpages><orcidid>https://orcid.org/0000-0002-6017-9706</orcidid></addata></record> |
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subjects | Adsorption Alkanes Biocompatibility Bonding strength Charge transfer Crystallinity Diols Doping Electrical resistivity Electrochemical impedance spectroscopy Fibrinogen Glass transition temperature Hexamethylene diisocyanate Hydrogen bonds In vitro methods and tests Isocyanates Physical properties Polyethylenes Polyurethane Polyurethane resins polyurethanes Protein adsorption protein adsorption resistance Proteins pseudocapacitors Rheological properties Serum albumin Silver Thermodynamic properties |
title | Tuning physical properties of polyurethane hard segments through extender chain length variation and doping of pentaerythritol and their effect on in vitro protein adsorption |
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