Complex coacervation-based loading and tunable release of a cationic protein from monodisperse glycosaminoglycan microgels
Glycosaminoglycans (GAGs) are of interest for biomedical applications because of their ability to retain proteins ( e.g. growth factors) involved in cell-to-cell signaling processes. In this study, the potential of GAG-based microgels for protein delivery and their protein release kinetics upon enca...
Gespeichert in:
| Veröffentlicht in: | Soft matter 2018, Vol.14 (3), p.6327-6341 |
|---|---|
| Hauptverfasser: | , , , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 6341 |
|---|---|
| container_issue | 3 |
| container_start_page | 6327 |
| container_title | Soft matter |
| container_volume | 14 |
| creator | Schuurmans, Carl C. L Abbadessa, Anna Bengtson, Mikkel A Pletikapic, Galja Eral, Huseyin Burak Koenderink, Gijsje Masereeuw, Rosalinde Hennink, Wim E Vermonden, Tina |
| description | Glycosaminoglycans (GAGs) are of interest for biomedical applications because of their ability to retain proteins (
e.g.
growth factors) involved in cell-to-cell signaling processes. In this study, the potential of GAG-based microgels for protein delivery and their protein release kinetics upon encapsulation in hydrogel scaffolds were investigated. Monodisperse hyaluronic acid methacrylate (HAMA) and chondroitin sulfate methacrylate (CSMA) micro-hydrogel spheres (diameters 500-700 μm), were used to study the absorption of a cationic model protein (lysozyme), microgel (de)swelling, intra-gel lysozyme distribution and its diffusion coefficient in the microgels dispersed in buffers (pH 7.4) of varying ionic strengths. Upon incubation in 20 mM buffer, lysozyme was absorbed up to 3 and 4 mg mg
−1
dry microspheres for HAMA and CSMA microgels respectively, with loading efficiencies up to 100%. Binding stoichiometries of disaccharide : lysozyme (10.2 : 1 and 7.5 : 1 for HAMA and CSMA, respectively) were similar to those for GAG-lysozyme complex coacervates based on soluble GAGs found in literature. Complex coacervates inside GAG microgels were also formed in buffers of higher ionic strengths as opposed to GAG-lysozyme systems based on soluble GAGs, likely due to increased local anionic charge density in the GAG networks. Binding of cationic lysozyme to the negatively charged microgel networks resulted in deswelling up to a factor 2 in diameter. Lysozyme release from the microgels was dependent on the ionic strength of the buffer and on the number of anionic groups per disaccharide, (1 for HAMA
versus
2 for CSMA). Lysozyme diffusion coefficients of 0.027 in HAMA and |
| doi_str_mv | 10.1039/c8sm00686e |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_swepu</sourceid><recordid>TN_cdi_proquest_miscellaneous_2072183087</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2072183087</sourcerecordid><originalsourceid>FETCH-LOGICAL-c514t-8a51f9f22a9044ee545283fa55ad7953ac4ad7f2656341bfd995a383e9b698d3</originalsourceid><addsrcrecordid>eNpd0s9rFTEQB_AgFvtDL96VgJcirObnvuyxPKsWKh4s4i3MZmefqbvJmuza1r_evL76BE_5wnwYMswQ8pyzN5zJ5q0zeWSsNjU-Ikd8pVRVG2Ue77P8dkiOc75mTBrF6yfkUDImlDbiiPxex3Ea8Ja6CA7TL5h9DFULGTs6ROh82FAIHZ2XAO2ANOGApUhjT4G6e-0dnVKc0QfapzjSMYbY-TxhKm4z3LmYYfQhbiMEOnqX4gaH_JQc9DBkfPbwnpCr9-dX64_V5ecPF-uzy8pprubKgOZ90wsBDVMKUSstjOxBa-hWjZbgVAm9qHUtFW_7rmk0SCOxaevGdPKEVLu2-QanpbVT8iOkOxvB23f-65mNaWN_zN-tkLXUq-JPd74M9XPBPNvRZ4fDAAHjkq1gK8GNZGZLX_1Hr-OSQhmmKMMarQ0XRb3eqTJ3zgn7_Rc4s9sF2rX58ul-gecFv3xoubQjdnv6d2MFvNiBlN2--u8C5B8n3aHp</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2080955812</pqid></control><display><type>article</type><title>Complex coacervation-based loading and tunable release of a cationic protein from monodisperse glycosaminoglycan microgels</title><source>Royal Society Of Chemistry Journals 2008-</source><source>Alma/SFX Local Collection</source><creator>Schuurmans, Carl C. L ; Abbadessa, Anna ; Bengtson, Mikkel A ; Pletikapic, Galja ; Eral, Huseyin Burak ; Koenderink, Gijsje ; Masereeuw, Rosalinde ; Hennink, Wim E ; Vermonden, Tina</creator><creatorcontrib>Schuurmans, Carl C. L ; Abbadessa, Anna ; Bengtson, Mikkel A ; Pletikapic, Galja ; Eral, Huseyin Burak ; Koenderink, Gijsje ; Masereeuw, Rosalinde ; Hennink, Wim E ; Vermonden, Tina</creatorcontrib><description>Glycosaminoglycans (GAGs) are of interest for biomedical applications because of their ability to retain proteins (
e.g.
growth factors) involved in cell-to-cell signaling processes. In this study, the potential of GAG-based microgels for protein delivery and their protein release kinetics upon encapsulation in hydrogel scaffolds were investigated. Monodisperse hyaluronic acid methacrylate (HAMA) and chondroitin sulfate methacrylate (CSMA) micro-hydrogel spheres (diameters 500-700 μm), were used to study the absorption of a cationic model protein (lysozyme), microgel (de)swelling, intra-gel lysozyme distribution and its diffusion coefficient in the microgels dispersed in buffers (pH 7.4) of varying ionic strengths. Upon incubation in 20 mM buffer, lysozyme was absorbed up to 3 and 4 mg mg
−1
dry microspheres for HAMA and CSMA microgels respectively, with loading efficiencies up to 100%. Binding stoichiometries of disaccharide : lysozyme (10.2 : 1 and 7.5 : 1 for HAMA and CSMA, respectively) were similar to those for GAG-lysozyme complex coacervates based on soluble GAGs found in literature. Complex coacervates inside GAG microgels were also formed in buffers of higher ionic strengths as opposed to GAG-lysozyme systems based on soluble GAGs, likely due to increased local anionic charge density in the GAG networks. Binding of cationic lysozyme to the negatively charged microgel networks resulted in deswelling up to a factor 2 in diameter. Lysozyme release from the microgels was dependent on the ionic strength of the buffer and on the number of anionic groups per disaccharide, (1 for HAMA
versus
2 for CSMA). Lysozyme diffusion coefficients of 0.027 in HAMA and <0.006 μm
2
s
−1
in CSMA microgels were found in 170 mM buffer (duration of release 14 and 28 days respectively). Fluorescence Recovery After Photobleaching (FRAP) measurements yielded similar trends, although lysozyme diffusion was likely altered due to the negative charges introduced to the protein through the FITC-labeling resulting in weaker protein-matrix interactions. Finally, lysozyme-loaded CSMA microgels were embedded into a thermosensitive hydrogel scaffold. These composite systems showed complete lysozyme release in ∼58 days as opposed to only 3 days for GAG-free scaffolds. In conclusion, covalently crosslinked methacrylated GAG hydrogels have potential as controlled release depots for cationic proteins in tissue engineering applications.
Glycosaminoglycan-based microgels are of interest for biomedical applications because of their ability to retain and gradually release bioactive cationic proteins.</description><identifier>ISSN: 1744-683X</identifier><identifier>ISSN: 1744-6848</identifier><identifier>EISSN: 1744-6848</identifier><identifier>DOI: 10.1039/c8sm00686e</identifier><identifier>PMID: 30024582</identifier><language>eng</language><publisher>England: Royal Society of Chemistry</publisher><subject>Anionic charge densities ; Binding ; Biomedical applications ; Biomedical materials ; Buffers ; Carrier sense multiple access ; Cations ; Cell signaling ; Cell-to-cell signaling ; Charge density ; Chondroitin sulfate ; Coacervation ; Complex networks ; Controlled release ; Covalently cross-linked ; Crosslinking ; Diffusion ; Diffusion coefficient ; Diffusion rate ; Disaccharides ; Embedded systems ; Enzymes ; Fluorescence ; Fluorescence recovery after photobleaching ; Gels ; Glycosaminoglycans ; Growth factors ; Hyaluronic acid ; Hydrogels ; Ionic strength ; Kinetics ; Lysozyme ; Medical applications ; Microgels ; Microspheres ; Photobleaching ; Protein release kinetics ; Proteins ; Scaffolds ; Scaffolds (biology) ; Stoichiometry ; Sulfur compounds ; Thermo-sensitive hydrogel ; Tissue engineering ; Tissue engineering applications</subject><ispartof>Soft matter, 2018, Vol.14 (3), p.6327-6341</ispartof><rights>Copyright Royal Society of Chemistry 2018</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c514t-8a51f9f22a9044ee545283fa55ad7953ac4ad7f2656341bfd995a383e9b698d3</citedby><cites>FETCH-LOGICAL-c514t-8a51f9f22a9044ee545283fa55ad7953ac4ad7f2656341bfd995a383e9b698d3</cites><orcidid>0000-0002-6047-5900 ; 0000-0002-5750-714X ; 0000-0002-7823-8807</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,777,781,882,4010,27904,27905,27906</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/30024582$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-236357$$DView record from Swedish Publication Index$$Hfree_for_read</backlink></links><search><creatorcontrib>Schuurmans, Carl C. L</creatorcontrib><creatorcontrib>Abbadessa, Anna</creatorcontrib><creatorcontrib>Bengtson, Mikkel A</creatorcontrib><creatorcontrib>Pletikapic, Galja</creatorcontrib><creatorcontrib>Eral, Huseyin Burak</creatorcontrib><creatorcontrib>Koenderink, Gijsje</creatorcontrib><creatorcontrib>Masereeuw, Rosalinde</creatorcontrib><creatorcontrib>Hennink, Wim E</creatorcontrib><creatorcontrib>Vermonden, Tina</creatorcontrib><title>Complex coacervation-based loading and tunable release of a cationic protein from monodisperse glycosaminoglycan microgels</title><title>Soft matter</title><addtitle>Soft Matter</addtitle><description>Glycosaminoglycans (GAGs) are of interest for biomedical applications because of their ability to retain proteins (
e.g.
growth factors) involved in cell-to-cell signaling processes. In this study, the potential of GAG-based microgels for protein delivery and their protein release kinetics upon encapsulation in hydrogel scaffolds were investigated. Monodisperse hyaluronic acid methacrylate (HAMA) and chondroitin sulfate methacrylate (CSMA) micro-hydrogel spheres (diameters 500-700 μm), were used to study the absorption of a cationic model protein (lysozyme), microgel (de)swelling, intra-gel lysozyme distribution and its diffusion coefficient in the microgels dispersed in buffers (pH 7.4) of varying ionic strengths. Upon incubation in 20 mM buffer, lysozyme was absorbed up to 3 and 4 mg mg
−1
dry microspheres for HAMA and CSMA microgels respectively, with loading efficiencies up to 100%. Binding stoichiometries of disaccharide : lysozyme (10.2 : 1 and 7.5 : 1 for HAMA and CSMA, respectively) were similar to those for GAG-lysozyme complex coacervates based on soluble GAGs found in literature. Complex coacervates inside GAG microgels were also formed in buffers of higher ionic strengths as opposed to GAG-lysozyme systems based on soluble GAGs, likely due to increased local anionic charge density in the GAG networks. Binding of cationic lysozyme to the negatively charged microgel networks resulted in deswelling up to a factor 2 in diameter. Lysozyme release from the microgels was dependent on the ionic strength of the buffer and on the number of anionic groups per disaccharide, (1 for HAMA
versus
2 for CSMA). Lysozyme diffusion coefficients of 0.027 in HAMA and <0.006 μm
2
s
−1
in CSMA microgels were found in 170 mM buffer (duration of release 14 and 28 days respectively). Fluorescence Recovery After Photobleaching (FRAP) measurements yielded similar trends, although lysozyme diffusion was likely altered due to the negative charges introduced to the protein through the FITC-labeling resulting in weaker protein-matrix interactions. Finally, lysozyme-loaded CSMA microgels were embedded into a thermosensitive hydrogel scaffold. These composite systems showed complete lysozyme release in ∼58 days as opposed to only 3 days for GAG-free scaffolds. In conclusion, covalently crosslinked methacrylated GAG hydrogels have potential as controlled release depots for cationic proteins in tissue engineering applications.
Glycosaminoglycan-based microgels are of interest for biomedical applications because of their ability to retain and gradually release bioactive cationic proteins.</description><subject>Anionic charge densities</subject><subject>Binding</subject><subject>Biomedical applications</subject><subject>Biomedical materials</subject><subject>Buffers</subject><subject>Carrier sense multiple access</subject><subject>Cations</subject><subject>Cell signaling</subject><subject>Cell-to-cell signaling</subject><subject>Charge density</subject><subject>Chondroitin sulfate</subject><subject>Coacervation</subject><subject>Complex networks</subject><subject>Controlled release</subject><subject>Covalently cross-linked</subject><subject>Crosslinking</subject><subject>Diffusion</subject><subject>Diffusion coefficient</subject><subject>Diffusion rate</subject><subject>Disaccharides</subject><subject>Embedded systems</subject><subject>Enzymes</subject><subject>Fluorescence</subject><subject>Fluorescence recovery after photobleaching</subject><subject>Gels</subject><subject>Glycosaminoglycans</subject><subject>Growth factors</subject><subject>Hyaluronic acid</subject><subject>Hydrogels</subject><subject>Ionic strength</subject><subject>Kinetics</subject><subject>Lysozyme</subject><subject>Medical applications</subject><subject>Microgels</subject><subject>Microspheres</subject><subject>Photobleaching</subject><subject>Protein release kinetics</subject><subject>Proteins</subject><subject>Scaffolds</subject><subject>Scaffolds (biology)</subject><subject>Stoichiometry</subject><subject>Sulfur compounds</subject><subject>Thermo-sensitive hydrogel</subject><subject>Tissue engineering</subject><subject>Tissue engineering applications</subject><issn>1744-683X</issn><issn>1744-6848</issn><issn>1744-6848</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><recordid>eNpd0s9rFTEQB_AgFvtDL96VgJcirObnvuyxPKsWKh4s4i3MZmefqbvJmuza1r_evL76BE_5wnwYMswQ8pyzN5zJ5q0zeWSsNjU-Ikd8pVRVG2Ue77P8dkiOc75mTBrF6yfkUDImlDbiiPxex3Ea8Ja6CA7TL5h9DFULGTs6ROh82FAIHZ2XAO2ANOGApUhjT4G6e-0dnVKc0QfapzjSMYbY-TxhKm4z3LmYYfQhbiMEOnqX4gaH_JQc9DBkfPbwnpCr9-dX64_V5ecPF-uzy8pprubKgOZ90wsBDVMKUSstjOxBa-hWjZbgVAm9qHUtFW_7rmk0SCOxaevGdPKEVLu2-QanpbVT8iOkOxvB23f-65mNaWN_zN-tkLXUq-JPd74M9XPBPNvRZ4fDAAHjkq1gK8GNZGZLX_1Hr-OSQhmmKMMarQ0XRb3eqTJ3zgn7_Rc4s9sF2rX58ul-gecFv3xoubQjdnv6d2MFvNiBlN2--u8C5B8n3aHp</recordid><startdate>2018</startdate><enddate>2018</enddate><creator>Schuurmans, Carl C. L</creator><creator>Abbadessa, Anna</creator><creator>Bengtson, Mikkel A</creator><creator>Pletikapic, Galja</creator><creator>Eral, Huseyin Burak</creator><creator>Koenderink, Gijsje</creator><creator>Masereeuw, Rosalinde</creator><creator>Hennink, Wim E</creator><creator>Vermonden, Tina</creator><general>Royal Society of Chemistry</general><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QF</scope><scope>7QO</scope><scope>7QQ</scope><scope>7SC</scope><scope>7SE</scope><scope>7SP</scope><scope>7SR</scope><scope>7TA</scope><scope>7TB</scope><scope>7U5</scope><scope>8BQ</scope><scope>8FD</scope><scope>F28</scope><scope>FR3</scope><scope>H8D</scope><scope>H8G</scope><scope>JG9</scope><scope>JQ2</scope><scope>KR7</scope><scope>L7M</scope><scope>L~C</scope><scope>L~D</scope><scope>P64</scope><scope>7X8</scope><scope>ADTPV</scope><scope>AOWAS</scope><scope>D8V</scope><orcidid>https://orcid.org/0000-0002-6047-5900</orcidid><orcidid>https://orcid.org/0000-0002-5750-714X</orcidid><orcidid>https://orcid.org/0000-0002-7823-8807</orcidid></search><sort><creationdate>2018</creationdate><title>Complex coacervation-based loading and tunable release of a cationic protein from monodisperse glycosaminoglycan microgels</title><author>Schuurmans, Carl C. L ; Abbadessa, Anna ; Bengtson, Mikkel A ; Pletikapic, Galja ; Eral, Huseyin Burak ; Koenderink, Gijsje ; Masereeuw, Rosalinde ; Hennink, Wim E ; Vermonden, Tina</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c514t-8a51f9f22a9044ee545283fa55ad7953ac4ad7f2656341bfd995a383e9b698d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2018</creationdate><topic>Anionic charge densities</topic><topic>Binding</topic><topic>Biomedical applications</topic><topic>Biomedical materials</topic><topic>Buffers</topic><topic>Carrier sense multiple access</topic><topic>Cations</topic><topic>Cell signaling</topic><topic>Cell-to-cell signaling</topic><topic>Charge density</topic><topic>Chondroitin sulfate</topic><topic>Coacervation</topic><topic>Complex networks</topic><topic>Controlled release</topic><topic>Covalently cross-linked</topic><topic>Crosslinking</topic><topic>Diffusion</topic><topic>Diffusion coefficient</topic><topic>Diffusion rate</topic><topic>Disaccharides</topic><topic>Embedded systems</topic><topic>Enzymes</topic><topic>Fluorescence</topic><topic>Fluorescence recovery after photobleaching</topic><topic>Gels</topic><topic>Glycosaminoglycans</topic><topic>Growth factors</topic><topic>Hyaluronic acid</topic><topic>Hydrogels</topic><topic>Ionic strength</topic><topic>Kinetics</topic><topic>Lysozyme</topic><topic>Medical applications</topic><topic>Microgels</topic><topic>Microspheres</topic><topic>Photobleaching</topic><topic>Protein release kinetics</topic><topic>Proteins</topic><topic>Scaffolds</topic><topic>Scaffolds (biology)</topic><topic>Stoichiometry</topic><topic>Sulfur compounds</topic><topic>Thermo-sensitive hydrogel</topic><topic>Tissue engineering</topic><topic>Tissue engineering applications</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Schuurmans, Carl C. L</creatorcontrib><creatorcontrib>Abbadessa, Anna</creatorcontrib><creatorcontrib>Bengtson, Mikkel A</creatorcontrib><creatorcontrib>Pletikapic, Galja</creatorcontrib><creatorcontrib>Eral, Huseyin Burak</creatorcontrib><creatorcontrib>Koenderink, Gijsje</creatorcontrib><creatorcontrib>Masereeuw, Rosalinde</creatorcontrib><creatorcontrib>Hennink, Wim E</creatorcontrib><creatorcontrib>Vermonden, Tina</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><collection>Aluminium Industry Abstracts</collection><collection>Biotechnology Research Abstracts</collection><collection>Ceramic Abstracts</collection><collection>Computer and Information Systems Abstracts</collection><collection>Corrosion Abstracts</collection><collection>Electronics & Communications Abstracts</collection><collection>Engineered Materials Abstracts</collection><collection>Materials Business File</collection><collection>Mechanical & Transportation Engineering Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>METADEX</collection><collection>Technology Research Database</collection><collection>ANTE: Abstracts in New Technology & Engineering</collection><collection>Engineering Research Database</collection><collection>Aerospace Database</collection><collection>Copper Technical Reference Library</collection><collection>Materials Research Database</collection><collection>ProQuest Computer Science Collection</collection><collection>Civil Engineering Abstracts</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>Computer and Information Systems Abstracts Academic</collection><collection>Computer and Information Systems Abstracts Professional</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><collection>SwePub</collection><collection>SwePub Articles</collection><collection>SWEPUB Kungliga Tekniska Högskolan</collection><jtitle>Soft matter</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Schuurmans, Carl C. L</au><au>Abbadessa, Anna</au><au>Bengtson, Mikkel A</au><au>Pletikapic, Galja</au><au>Eral, Huseyin Burak</au><au>Koenderink, Gijsje</au><au>Masereeuw, Rosalinde</au><au>Hennink, Wim E</au><au>Vermonden, Tina</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Complex coacervation-based loading and tunable release of a cationic protein from monodisperse glycosaminoglycan microgels</atitle><jtitle>Soft matter</jtitle><addtitle>Soft Matter</addtitle><date>2018</date><risdate>2018</risdate><volume>14</volume><issue>3</issue><spage>6327</spage><epage>6341</epage><pages>6327-6341</pages><issn>1744-683X</issn><issn>1744-6848</issn><eissn>1744-6848</eissn><abstract>Glycosaminoglycans (GAGs) are of interest for biomedical applications because of their ability to retain proteins (
e.g.
growth factors) involved in cell-to-cell signaling processes. In this study, the potential of GAG-based microgels for protein delivery and their protein release kinetics upon encapsulation in hydrogel scaffolds were investigated. Monodisperse hyaluronic acid methacrylate (HAMA) and chondroitin sulfate methacrylate (CSMA) micro-hydrogel spheres (diameters 500-700 μm), were used to study the absorption of a cationic model protein (lysozyme), microgel (de)swelling, intra-gel lysozyme distribution and its diffusion coefficient in the microgels dispersed in buffers (pH 7.4) of varying ionic strengths. Upon incubation in 20 mM buffer, lysozyme was absorbed up to 3 and 4 mg mg
−1
dry microspheres for HAMA and CSMA microgels respectively, with loading efficiencies up to 100%. Binding stoichiometries of disaccharide : lysozyme (10.2 : 1 and 7.5 : 1 for HAMA and CSMA, respectively) were similar to those for GAG-lysozyme complex coacervates based on soluble GAGs found in literature. Complex coacervates inside GAG microgels were also formed in buffers of higher ionic strengths as opposed to GAG-lysozyme systems based on soluble GAGs, likely due to increased local anionic charge density in the GAG networks. Binding of cationic lysozyme to the negatively charged microgel networks resulted in deswelling up to a factor 2 in diameter. Lysozyme release from the microgels was dependent on the ionic strength of the buffer and on the number of anionic groups per disaccharide, (1 for HAMA
versus
2 for CSMA). Lysozyme diffusion coefficients of 0.027 in HAMA and <0.006 μm
2
s
−1
in CSMA microgels were found in 170 mM buffer (duration of release 14 and 28 days respectively). Fluorescence Recovery After Photobleaching (FRAP) measurements yielded similar trends, although lysozyme diffusion was likely altered due to the negative charges introduced to the protein through the FITC-labeling resulting in weaker protein-matrix interactions. Finally, lysozyme-loaded CSMA microgels were embedded into a thermosensitive hydrogel scaffold. These composite systems showed complete lysozyme release in ∼58 days as opposed to only 3 days for GAG-free scaffolds. In conclusion, covalently crosslinked methacrylated GAG hydrogels have potential as controlled release depots for cationic proteins in tissue engineering applications.
Glycosaminoglycan-based microgels are of interest for biomedical applications because of their ability to retain and gradually release bioactive cationic proteins.</abstract><cop>England</cop><pub>Royal Society of Chemistry</pub><pmid>30024582</pmid><doi>10.1039/c8sm00686e</doi><tpages>15</tpages><orcidid>https://orcid.org/0000-0002-6047-5900</orcidid><orcidid>https://orcid.org/0000-0002-5750-714X</orcidid><orcidid>https://orcid.org/0000-0002-7823-8807</orcidid><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1744-683X |
| ispartof | Soft matter, 2018, Vol.14 (3), p.6327-6341 |
| issn | 1744-683X 1744-6848 1744-6848 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_2072183087 |
| source | Royal Society Of Chemistry Journals 2008-; Alma/SFX Local Collection |
| subjects | Anionic charge densities Binding Biomedical applications Biomedical materials Buffers Carrier sense multiple access Cations Cell signaling Cell-to-cell signaling Charge density Chondroitin sulfate Coacervation Complex networks Controlled release Covalently cross-linked Crosslinking Diffusion Diffusion coefficient Diffusion rate Disaccharides Embedded systems Enzymes Fluorescence Fluorescence recovery after photobleaching Gels Glycosaminoglycans Growth factors Hyaluronic acid Hydrogels Ionic strength Kinetics Lysozyme Medical applications Microgels Microspheres Photobleaching Protein release kinetics Proteins Scaffolds Scaffolds (biology) Stoichiometry Sulfur compounds Thermo-sensitive hydrogel Tissue engineering Tissue engineering applications |
| title | Complex coacervation-based loading and tunable release of a cationic protein from monodisperse glycosaminoglycan microgels |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-21T05%3A42%3A18IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_swepu&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Complex%20coacervation-based%20loading%20and%20tunable%20release%20of%20a%20cationic%20protein%20from%20monodisperse%20glycosaminoglycan%20microgels&rft.jtitle=Soft%20matter&rft.au=Schuurmans,%20Carl%20C.%20L&rft.date=2018&rft.volume=14&rft.issue=3&rft.spage=6327&rft.epage=6341&rft.pages=6327-6341&rft.issn=1744-683X&rft.eissn=1744-6848&rft_id=info:doi/10.1039/c8sm00686e&rft_dat=%3Cproquest_swepu%3E2072183087%3C/proquest_swepu%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=2080955812&rft_id=info:pmid/30024582&rfr_iscdi=true |