Bioengineering / Biyomühendislik

Permanent URI for this collectionhttps://hdl.handle.net/11147/4529

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Scopus Q: search.filters.scopusQuartile.Q2Subject: search.filters.subject.Biomaterials

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  • Article
    Citation - WoS: 14
    Citation - Scopus: 16
    Synergistic Effect of Type and Concentration of Surfactant and Diluting Solvent on the Morphology of Emulsion Templated Matrices Developed as Tissue Engineering Scaffolds
    (Elsevier, 2022) Claeyssens, Frederik; Aldemir Dikici, Betül; Dikici, Serkan
    Emulsion templating is an advantageous route for the fabrication of tissue engineering scaffolds. Emulsions are mostly stabilised using surfactants, and the performances of the surfactants depend on various parameters such as emulsification temperature and the presence of the electrolytes. In this study, we suggest that diluting solvent type also has a dramatic impact on the efficiency of the surfactant and morphology of the polymerised emulsions. For this, morphologies of polycaprolactone methacrylate-based polymerised emulsions, which are designed for tissue engineering applications and in vitro biocompatibilities, were shown by our group, prepared using four different surfactants, and three different solvents were investigated. Results showed that the diluting solvent used in the emulsion composition has a strong impact on the performance of the surfactant and consequently on the morphology of polymerised emulsions. Increasing surfactant concentration and diluting solvent volume have an opposite impact on the characteristics of emulsions. Scaffolds with average pore sizes changing from 10 to 78 μm could be fabricated. Establishing these relations enables us to have control over the overall morphology of polymerised emulsions and precisely engineer them for specific tissue engineering applications by tuning solvent and surfactant type and concentration.
  • Article
    Citation - WoS: 2
    Citation - Scopus: 2
    Cloning, Expression, and Characterization of a Novel Sericin-Like Protein
    (Wiley, 2022) Bostan, Fatmanur; Sürmeli, Nur Başak
    Silk consists of two proteins called fibroin and sericin. While fibroin is used in the textile industry and has various biomaterial applications, sericin has been considered as waste material until recently. Sericin is a multicomponent protein and it has important properties such as biocompatibility, biodegradability, cryoprotectivity, and antioxidant. Sericin from silkworm cocoons can be obtained by chemical, enzymatic, and heat treatment methods. However, sericin obtained with these treatment methods is not of consistent and high quality. Moreover, the exposure of sericin to harsh conditions during extraction leads to inconsistencies in the composition and structure of the sericin obtained. The inconsistencies in sericin structure and composition decrease application of sericin as a biomaterial. Here, we produce a sericin-like protein (Ser4mer) with native sequence of sericin encoding four repeats of the conserved 38 amino acid motif recombinantly in Escherichia coli and characterize its structural properties. Ser4mer protein shows similar structure to native sericin and higher solubility than previously obtained recombinant sericin-like proteins. Recombinant production of a soluble sericin-like protein will significantly expand its applications as a biomaterial. In addition, recombinant production of silk proteins will allow us to understand sequence-structure relationships in these proteins.