Understanding the Molecular Conformation and Viscoelasticity of Low Sol-Gel Transition Temperature Gelatin Methacryloyl Suspensions

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dc.coverageDOI: 10.3390/ijms24087489
dc.creatorPadilla, Cristina
dc.creatorQuero, Franck
dc.creatorPępczyńska, Marzena
dc.creatorDíaz-Calderon, Paulo
dc.creatorAcevedo, Juan Pablo
dc.creatorByres, Nicholas
dc.creatorBlaker, Jonny J.
dc.creatorMacNaughtan, William
dc.creatorWilliams, Huw E.L.
dc.creatorEnrione, Javier
dc.date2023
dc.date.accessioned2025-11-18T19:49:12Z
dc.date.available2025-11-18T19:49:12Z
dc.description<p>For biomedical applications, gelatin is usually modified with methacryloyl groups to obtain gelatin methacryloyl (GelMA), which can be crosslinked by a radical reaction induced by low wavelength light to form mechanically stable hydrogels. The potential of GelMA hydrogels for tissue engineering has been well established, however, one of the main disadvantages of mammalian-origin gelatins is that their sol-gel transitions are close to room temperature, resulting in significant variations in viscosity that can be a problem for biofabrication applications. For these applications, cold-water fish-derived gelatins, such as salmon gelatin, are a good alternative due to their lower viscosity, viscoelastic and mechanical properties, as well as lower sol-gel transition temperatures, when compared with mammalian gelatins. However, information regarding GelMA (with special focus on salmon GelMA as a model for cold-water species) molecular conformation and the effect of pH prior to crosslinking, which is key for fabrication purposes since it will determine final hydrogel’s structure, remains scarce. The aim of this work is to characterize salmon gelatin (SGel) and salmon methacryloyl gelatin (SGelMA) molecular configuration at two different acidic pHs (3.6 and 4.8) and to compare them to commercial porcine gelatin (PGel) and methacryloyl porcine gelatin (PGelMA), usually used for biomedical applications. Specifically, we evaluated gelatin and GelMA samples’ molecular weight, isoelectric point (IEP), their molecular configuration by circular dichroism (CD), and determined their rheological and thermophysical properties. Results showed that functionalization affected gelatin molecular weight and IEP. Additionally, functionalization and pH affected gelatin molecular structure and rheological and thermal properties. Interestingly, the SGel and SGelMA molecular structure was more sensitive to pH changes, showing differences in gelation temperatures and triple helix formation than PGelMA. This work suggests that SGelMA presents high tunability as a biomaterial for biofabrication, highlighting the importance of a proper GelMA molecular configuration characterization prior to hydrogel fabrication.</p>eng
dc.identifierhttps://investigadores.uandes.cl/en/publications/3e55569c-f0f8-4c29-8f1f-684e8a296807
dc.identifier.urihttps://repositorio.uandes.cl/handle/uandes/55963
dc.languageeng
dc.rightsinfo:eu-repo/semantics/openAccess
dc.sourcevol.24 (2023) nr.8 p.1-19
dc.subjectGelMA
dc.subjectgelatin
dc.subjectmolecular configuration
dc.subjectsol-gel transition temperature
dc.titleUnderstanding the Molecular Conformation and Viscoelasticity of Low Sol-Gel Transition Temperature Gelatin Methacryloyl Suspensionseng
dc.typeArticleeng
dc.typeArtículospa
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