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dc.contributor.authorYue, Kan
dc.contributor.authorLi, Xiuyu
dc.contributor.authorSchrobback, Karsten
dc.contributor.authorSheikhi, Amir
dc.contributor.authorAnnabi, Nasim
dc.contributor.authorLeijten, Jeroen
dc.contributor.authorZhang, Weijia
dc.contributor.authorZhang, Yu Shrike
dc.contributor.authorHutmacher, Dietmar W
dc.contributor.authorKlein, Travis J
dc.contributor.authorKhademhosseini, Ali
dc.date.accessioned2022-03-28T00:19:52Z
dc.date.available2022-03-28T00:19:52Z
dc.date.issued2017
dc.identifier.issn0142-9612en_US
dc.identifier.doi10.1016/j.biomaterials.2017.04.050en_US
dc.identifier.urihttp://hdl.handle.net/10072/413550
dc.description.abstractBiochemically modified proteins have attracted significant attention due to their widespread applications as biomaterials. For instance, chemically modified gelatin derivatives have been widely explored to develop hydrogels for tissue engineering and regenerative medicine applications. Among the reported methods, modification of gelatin with methacrylic anhydride (MA) stands out as a convenient and efficient strategy to introduce functional groups and form hydrogels via photopolymerization. Combining light-activation of modified gelatin with soft lithography has enabled the materialization of microfabricated hydrogels. So far, this gelatin derivative has been referred to in the literature as gelatin methacrylate, gelatin methacrylamide, or gelatin methacryloyl, with the same abbreviation of GelMA. Considering the complex composition of gelatin and the presence of different functional groups on the amino acid residues, both hydroxyl groups and amine groups can possibly react with methacrylic anhydride during functionalization of the protein. This can also apply to the modification of other proteins, such as recombinant human tropoelastin to form MA-modified tropoelastin (MeTro). Here, we employed analytical methods to quantitatively determine the amounts of methacrylate and methacrylamide groups in MA-modified gelatin and tropoelastin to better understand the reaction mechanism. By combining two chemical assays with instrumental techniques, such as proton nuclear magnetic resonance (1H NMR) and liquid chromatography tandem-mass spectrometry (LC-MS/MS), our results indicated that while amine groups had higher reactivity than hydroxyl groups and resulted in a majority of methacrylamide groups, modification of proteins by MA could lead to the formation of both methacrylamide and methacrylate groups. It is therefore suggested that the standard terms for GelMA and MeTro should be defined as gelatin methacryloyl and methacryloyl-substituted tropoelastin, respectively, to remain consistent with the widespread abbreviations used in literature.en_US
dc.description.peerreviewedYesen_US
dc.languageEnglishen_US
dc.publisherElsevieren_US
dc.relation.ispartofpagefrom163en_US
dc.relation.ispartofpageto171en_US
dc.relation.ispartofjournalBiomaterialsen_US
dc.relation.ispartofvolume139en_US
dc.subject.fieldofresearchAnalytical biochemistryen_US
dc.subject.fieldofresearchcode310101en_US
dc.subject.keywordsScience & Technologyen_US
dc.subject.keywordsEngineering, Biomedicalen_US
dc.subject.keywordsMaterials Science, Biomaterialsen_US
dc.titleStructural analysis of photocrosslinkable methacryloyl-modified protein derivativesen_US
dc.typeJournal articleen_US
dc.type.descriptionC1 - Articlesen_US
dcterms.bibliographicCitationYue, K; Li, X; Schrobback, K; Sheikhi, A; Annabi, N; Leijten, J; Zhang, W; Zhang, YS; Hutmacher, DW; Klein, TJ; Khademhosseini, A, Structural analysis of photocrosslinkable methacryloyl-modified protein derivatives, Biomaterials, 2017, 139, pp. 163-171en_US
dcterms.dateAccepted2017-04-03
dc.date.updated2022-03-25T03:23:32Z
gro.hasfulltextNo Full Text
gro.griffith.authorHutmacher, Dietmar W.


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