pH and Thrombin Concentration Are Decisive in Synthesizing Stiff, Stable, and Open‐Porous Fibrin‐Collagen Hydrogel Blends without Chemical Cross‐Linker
Fibrin‐collagen hydrogel blends exhibit high potential for tissue engineering applications. However, it is still unclear whether the underlying cross‐linking mechanisms are of chemical or physical nature. It is here hypothesized that chemical cross‐linkers play a negligible role and that instead pH...
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description | Fibrin‐collagen hydrogel blends exhibit high potential for tissue engineering applications. However, it is still unclear whether the underlying cross‐linking mechanisms are of chemical or physical nature. It is here hypothesized that chemical cross‐linkers play a negligible role and that instead pH and thrombin concentration are decisive for synthetizing blends with high stiffness and hydrolytic stability. Different fibrin‐collagen formulations (pure and with additional transglutaminase) are used and the blends’ compaction rate, hydrolytic stability, compressive strength, and hydrogel microstructure are investigated. The effect of thrombin concentration on gel compaction is examined and the importance of pH control during synthesis observed. It is revealed that transglutaminase impairs gel stability and it is deduced that fibrin‐collagen blends mainly cross‐link by mechanical interactions due to physical fibril entanglement as opposed to covalent bonds from chemical cross‐linking. High thrombin concentrations and basic pH during synthesis reduce gel compaction and enhance stiffness and long‐term stability. Scanning electron microscopy reveals a highly interpenetrating fibrous network with unique, interconnected open‐porous microstructures. Endothelial cells proliferate on the blends and form a confluent monolayer. This study reveals the underlying cross‐linking mechanisms and presents enhanced fibrin‐collagen blends with high stiffness, hydrolytic stability, and large, interconnected pores; findings that offer high potential for advanced tissue engineering applications.
The underlying cross‐linking mechanisms of fibrin‐collagen hydrogel blends are still unclear. It is shown that thrombin concentration and pH control during synthesis are decisive for fabricating stiff, stable, and open‐porous fibrin‐collagen blends. Herein, it is revealed that chemical cross‐linkers are negligible and that the cross‐linking is based on physical fibril entanglement rather than chemical cross‐linking, creating interpenetrating, yet open‐porous fibrous networks. |
doi_str_mv | 10.1002/adhm.202203302 |
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The underlying cross‐linking mechanisms of fibrin‐collagen hydrogel blends are still unclear. It is shown that thrombin concentration and pH control during synthesis are decisive for fabricating stiff, stable, and open‐porous fibrin‐collagen blends. Herein, it is revealed that chemical cross‐linkers are negligible and that the cross‐linking is based on physical fibril entanglement rather than chemical cross‐linking, creating interpenetrating, yet open‐porous fibrous networks.</description><identifier>ISSN: 2192-2640</identifier><identifier>ISSN: 2192-2659</identifier><identifier>EISSN: 2192-2659</identifier><identifier>DOI: 10.1002/adhm.202203302</identifier><identifier>PMID: 36546310</identifier><language>eng</language><publisher>Germany: Wiley Subscription Services, Inc</publisher><subject>Biocompatible Materials - chemistry ; Chemical bonds ; Chemical Sciences ; Chemical synthesis ; Collagen ; Collagen - chemistry ; Compaction ; Compressive strength ; Covalent bonds ; cross‐linking mechanisms ; Endothelial Cells ; Entanglement ; Fibrin ; Fibrin - chemistry ; Hydrogels ; Hydrogels - chemistry ; Hydrogen-Ion Concentration ; interpenetrating networks ; Mechanical stimuli ; Microstructure ; microstructures ; Mixtures ; pH control ; pH effects ; Physics ; Porosity ; Scanning electron microscopy ; Stiffness ; Thrombin ; Tissue Engineering</subject><ispartof>Advanced healthcare materials, 2023-04, Vol.12 (10), p.e2203302-n/a</ispartof><rights>2023 The Authors. Advanced Healthcare Materials published by Wiley‐VCH GmbH</rights><rights>2023 The Authors. Advanced Healthcare Materials published by Wiley-VCH GmbH.</rights><rights>2023. This article is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5032-2b25f8cd2517dfec3d3f79a5255acf9f4e39e9b686ef40853086f9f5139c7ef53</citedby><cites>FETCH-LOGICAL-c5032-2b25f8cd2517dfec3d3f79a5255acf9f4e39e9b686ef40853086f9f5139c7ef53</cites><orcidid>0000-0003-0990-5028</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%2Fadhm.202203302$$EPDF$$P50$$Gwiley$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fadhm.202203302$$EHTML$$P50$$Gwiley$$Hfree_for_read</linktohtml><link.rule.ids>230,314,780,784,885,1417,27924,27925,45574,45575</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/36546310$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.inrae.fr/hal-04330441$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Wachendörfer, Mattis</creatorcontrib><creatorcontrib>Buhl, Eva Miriam</creatorcontrib><creatorcontrib>Messaoud, Ghazi Ben</creatorcontrib><creatorcontrib>Richtering, Walter</creatorcontrib><creatorcontrib>Fischer, Horst</creatorcontrib><title>pH and Thrombin Concentration Are Decisive in Synthesizing Stiff, Stable, and Open‐Porous Fibrin‐Collagen Hydrogel Blends without Chemical Cross‐Linker</title><title>Advanced healthcare materials</title><addtitle>Adv Healthc Mater</addtitle><description>Fibrin‐collagen hydrogel blends exhibit high potential for tissue engineering applications. However, it is still unclear whether the underlying cross‐linking mechanisms are of chemical or physical nature. It is here hypothesized that chemical cross‐linkers play a negligible role and that instead pH and thrombin concentration are decisive for synthetizing blends with high stiffness and hydrolytic stability. Different fibrin‐collagen formulations (pure and with additional transglutaminase) are used and the blends’ compaction rate, hydrolytic stability, compressive strength, and hydrogel microstructure are investigated. The effect of thrombin concentration on gel compaction is examined and the importance of pH control during synthesis observed. It is revealed that transglutaminase impairs gel stability and it is deduced that fibrin‐collagen blends mainly cross‐link by mechanical interactions due to physical fibril entanglement as opposed to covalent bonds from chemical cross‐linking. High thrombin concentrations and basic pH during synthesis reduce gel compaction and enhance stiffness and long‐term stability. Scanning electron microscopy reveals a highly interpenetrating fibrous network with unique, interconnected open‐porous microstructures. Endothelial cells proliferate on the blends and form a confluent monolayer. This study reveals the underlying cross‐linking mechanisms and presents enhanced fibrin‐collagen blends with high stiffness, hydrolytic stability, and large, interconnected pores; findings that offer high potential for advanced tissue engineering applications.
The underlying cross‐linking mechanisms of fibrin‐collagen hydrogel blends are still unclear. It is shown that thrombin concentration and pH control during synthesis are decisive for fabricating stiff, stable, and open‐porous fibrin‐collagen blends. Herein, it is revealed that chemical cross‐linkers are negligible and that the cross‐linking is based on physical fibril entanglement rather than chemical cross‐linking, creating interpenetrating, yet open‐porous fibrous networks.</description><subject>Biocompatible Materials - chemistry</subject><subject>Chemical bonds</subject><subject>Chemical Sciences</subject><subject>Chemical synthesis</subject><subject>Collagen</subject><subject>Collagen - chemistry</subject><subject>Compaction</subject><subject>Compressive strength</subject><subject>Covalent bonds</subject><subject>cross‐linking mechanisms</subject><subject>Endothelial Cells</subject><subject>Entanglement</subject><subject>Fibrin</subject><subject>Fibrin - chemistry</subject><subject>Hydrogels</subject><subject>Hydrogels - chemistry</subject><subject>Hydrogen-Ion Concentration</subject><subject>interpenetrating networks</subject><subject>Mechanical stimuli</subject><subject>Microstructure</subject><subject>microstructures</subject><subject>Mixtures</subject><subject>pH control</subject><subject>pH effects</subject><subject>Physics</subject><subject>Porosity</subject><subject>Scanning electron microscopy</subject><subject>Stiffness</subject><subject>Thrombin</subject><subject>Tissue Engineering</subject><issn>2192-2640</issn><issn>2192-2659</issn><issn>2192-2659</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2023</creationdate><recordtype>article</recordtype><sourceid>24P</sourceid><sourceid>WIN</sourceid><sourceid>EIF</sourceid><recordid>eNqFUstu1DAUjRCIVqVblsgSG5A6gx9xHis0pJRBGlSklrXlJNcTl8Se2slUw6qf0B_g5_gSHFIG6AZvrn3vuce-xyeKnhM8JxjTN7JuujnFlGLGMH0UHVKS0xlNeP54v4_xQXTs_RUOK-EkycjT6IAlPE4YwYfR980SSVOjy8bZrtQGFdZUYHone20NWjhAp1Bpr7eAQvViZ_oGvP6mzRpd9FqpkxBk2cLJL5rzDZgft3efrbODR2e6dHo8F7Zt5RoMWu5qZ9fQonctmNqjG903duhR0UCnK9miwlnvQ8dKm6_gnkVPlGw9HN_Ho-jL2fvLYjlbnX_4WCxWs4pjFqYsKVdZVVNO0lpBxWqm0lxyyrmsVK5iYDnkZZIloGKccYazJKQ5YXmVguLsKHo78W6GsoN6EqAVG6c76XbCSi3-rRjdiLXdCkLiwIrzwPB6Ymge9C0XKzHmcBz-KI7JlgTsq_vbnL0ewPei076CIJGBIJugKU8xT_IYB-jLB9ArOzgTtBA0wyTLEpZmATWfUNWongO1fwHBYnSKGJ0i9k4JDS_-nncP_-2LAMgnwI1uYfcfOrE4XX76Q_4Tj5jOgA</recordid><startdate>20230401</startdate><enddate>20230401</enddate><creator>Wachendörfer, Mattis</creator><creator>Buhl, Eva Miriam</creator><creator>Messaoud, Ghazi Ben</creator><creator>Richtering, Walter</creator><creator>Fischer, Horst</creator><general>Wiley Subscription Services, Inc</general><general>Wiley</general><general>John Wiley and Sons Inc</general><scope>24P</scope><scope>WIN</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QF</scope><scope>7QP</scope><scope>7QQ</scope><scope>7SC</scope><scope>7SE</scope><scope>7SP</scope><scope>7SR</scope><scope>7T5</scope><scope>7TA</scope><scope>7TB</scope><scope>7TM</scope><scope>7TO</scope><scope>7U5</scope><scope>8BQ</scope><scope>8FD</scope><scope>F28</scope><scope>FR3</scope><scope>H8D</scope><scope>H8G</scope><scope>H94</scope><scope>JG9</scope><scope>JQ2</scope><scope>K9.</scope><scope>KR7</scope><scope>L7M</scope><scope>L~C</scope><scope>L~D</scope><scope>7X8</scope><scope>1XC</scope><scope>VOOES</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0003-0990-5028</orcidid></search><sort><creationdate>20230401</creationdate><title>pH and Thrombin Concentration Are Decisive in Synthesizing Stiff, Stable, and Open‐Porous Fibrin‐Collagen Hydrogel Blends without Chemical Cross‐Linker</title><author>Wachendörfer, Mattis ; 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However, it is still unclear whether the underlying cross‐linking mechanisms are of chemical or physical nature. It is here hypothesized that chemical cross‐linkers play a negligible role and that instead pH and thrombin concentration are decisive for synthetizing blends with high stiffness and hydrolytic stability. Different fibrin‐collagen formulations (pure and with additional transglutaminase) are used and the blends’ compaction rate, hydrolytic stability, compressive strength, and hydrogel microstructure are investigated. The effect of thrombin concentration on gel compaction is examined and the importance of pH control during synthesis observed. It is revealed that transglutaminase impairs gel stability and it is deduced that fibrin‐collagen blends mainly cross‐link by mechanical interactions due to physical fibril entanglement as opposed to covalent bonds from chemical cross‐linking. High thrombin concentrations and basic pH during synthesis reduce gel compaction and enhance stiffness and long‐term stability. Scanning electron microscopy reveals a highly interpenetrating fibrous network with unique, interconnected open‐porous microstructures. Endothelial cells proliferate on the blends and form a confluent monolayer. This study reveals the underlying cross‐linking mechanisms and presents enhanced fibrin‐collagen blends with high stiffness, hydrolytic stability, and large, interconnected pores; findings that offer high potential for advanced tissue engineering applications.
The underlying cross‐linking mechanisms of fibrin‐collagen hydrogel blends are still unclear. It is shown that thrombin concentration and pH control during synthesis are decisive for fabricating stiff, stable, and open‐porous fibrin‐collagen blends. Herein, it is revealed that chemical cross‐linkers are negligible and that the cross‐linking is based on physical fibril entanglement rather than chemical cross‐linking, creating interpenetrating, yet open‐porous fibrous networks.</abstract><cop>Germany</cop><pub>Wiley Subscription Services, Inc</pub><pmid>36546310</pmid><doi>10.1002/adhm.202203302</doi><tpages>13</tpages><orcidid>https://orcid.org/0000-0003-0990-5028</orcidid><oa>free_for_read</oa></addata></record> |
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subjects | Biocompatible Materials - chemistry Chemical bonds Chemical Sciences Chemical synthesis Collagen Collagen - chemistry Compaction Compressive strength Covalent bonds cross‐linking mechanisms Endothelial Cells Entanglement Fibrin Fibrin - chemistry Hydrogels Hydrogels - chemistry Hydrogen-Ion Concentration interpenetrating networks Mechanical stimuli Microstructure microstructures Mixtures pH control pH effects Physics Porosity Scanning electron microscopy Stiffness Thrombin Tissue Engineering |
title | pH and Thrombin Concentration Are Decisive in Synthesizing Stiff, Stable, and Open‐Porous Fibrin‐Collagen Hydrogel Blends without Chemical Cross‐Linker |
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