WoS İndeksli Yayınlar Koleksiyonu / WoS Indexed Publications Collection

Permanent URI for this collectionhttps://hdl.handle.net/11147/7150

Browse

Filters

20222

Settings

Publisher: search.filters.publisher.WileySubject: search.filters.subject.Biomaterials

Search Results

Now showing 1 - 2 of 2
  • Article
    Citation - WoS: 3
    Citation - Scopus: 4
    Microfluidic-Assisted Preparation of Nano and Microscale Chitosan Based 3d Composite Materials: Comparison With Conventional Methods
    (Wiley, 2022) Kimna, Ceren; Değer, Sibel; Tamburacı, Sedef; Tıhmınlıoğlu, Funda
    Although nanofillers contribute to improved physical characteristics and biological functionalities of polymer-based biomaterials, their dispersion in polymer matrices is still a challenging issue in terms of obtaining consistency for the inherent properties. To tackle this problem, homogenization techniques are applied to disperse the nanofillers in such polymers, however, these methods can cause undesired changes especially in the rheological properties and the physical structure of the biopolymer matrices. Recently, as a novel homogenization technique, microfluidization has been used to homogenize polymer nanocomposites to minimize these limitations. In this study, two different nanocomposite structures as chitosan/montmorillonite (CS/MMT) and chitosan/polyhedral oligomeric silsesquioxane nanocages (CS/POSS) were homogenized with microfluidization and investigated in terms of physical alterations. Furthermore, the effect of microfluidizer technique on material characteristics was compared with conventional homogenization techniques, i.e., ultrasonic bath and sonication in terms of solution, nano – (e.g., hydrodynamic size, drug encapsulation) and macroscopic material characteristics (e.g., porosity, mechanical properties, swelling and thermal degradation). It was found that the microfluidizer homogenization improves the physical characteristics in both nano and macroscale materials: Nanospheres obtained from CS/MMT composites showed enhanced stability, uniform size distribution (<100 nm, PDI: [removed]50%) whereas 3D porous CS/POSS scaffolds showed improved structural uniformity (i.e., homogeneous and interconnected microstructure) and enhanced thermal and mechanical properties. The obtained results indicate that the microfluidizer homogenization ensures a successful nanofiller dispersion in polymer matrices, thereby improving the biomaterial characteristics impressively compared to the sonication methods.
  • 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.