Scopus İndeksli Yayınlar Koleksiyonu / Scopus Indexed Publications Collection
Permanent URI for this collectionhttps://hdl.handle.net/11147/7148
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Article Citation - WoS: 17Citation - Scopus: 16Development of Cissus Quadrangularis-Loaded Poss-Reinforced Chitosan-Based Bilayer Sponges for Wound Healing Applications: Drug Release and in Vitro Bioactivity(American Chemical Society, 2023) Tıhmınlıoğlu, Funda; Tamburacı, Sedef; Tıhmınlıoğlu, Funda; 03.02. Department of Chemical Engineering; 03. Faculty of Engineering; 01. Izmir Institute of TechnologyNowadays, antibiotic-loaded biomaterials have been widelyusedin wound healing applications. However, the use of natural extractshas come into prominence as an alternative to these antimicrobialagents in the recent period. Among natural sources, Cissus quadrangularis (CQ) herbal extract is usedfor treatment of bone and skin diseases in ayurvedic medicine dueto its antibacterial and anti-inflammatory effects. In this study,chitosan-based bilayer wound dressings were fabricated with electrospinningand freeze-drying techniques. CQ extract-loaded chitosan nanofiberswere coated on chitosan/POSS nanocomposite sponges using an electrospinningmethod. The bilayer sponge is designed to treat exudate wounds whilemimicking the layered structure of skin tissue. Bilayer wound dressingswere investigated with regard to the morphology and physical and mechanicalproperties. In addition, CQ release from bilayer wound dressings and in vitro bioactivity studies were performed to determinethe effect of POSS nanoparticles and CQ extract loading on NIH/3T3and HS2 cells. The morphology of nanofibers was investigated withSEM analysis. Physical characteristics of bilayer wound dressingswere determined with FT-IR analysis, swelling study, open porositydetermination, and mechanical test. The antimicrobial activity ofCQ extract released from bilayer sponges was investigated with a discdiffusion method. Bilayer wound dressings' in vitro bioactivity was examined using cytotoxicity determination, woundhealing assay, proliferation, and the secretion of biomarkers forskin tissue regeneration. The nanofiber layer diameter was obtainedin the range of 77.9-97.4 nm. The water vapor permeabilityof the bilayer dressing was obtained as 4021 to 4609 g/m(2)day, as it is in the ideal range for wound repair. The release ofthe CQ extract over 4 days reached 78-80% cumulative release.The release media were found to be antibacterial against Gram-negativeand Gram-positive bacteria. In vitro studies showedthat both CQ extract and POSS incorporation induced cell proliferationas well as wound healing activity and collagen deposition. As a result,CQ-loaded bilayer CHI-POSS nanocomposites were found as a potentialcandidate for wound healing applications.Article Citation - WoS: 13Citation - Scopus: 13Solid-Binding Peptide-Guided Spatially Directed Immobilization of Kinetically Matched Enzyme Cascades in Membrane Nanoreactors(American Chemical Society, 2021) Yücesoy, Deniz Tanıl; Yücesoy, Deniz Tanıl; Akkineni, Susrut; Tamerler, Candan; Hinds, Bruce J.; Sarıkaya, Mehmet; 03.01. Department of Bioengineering; 03. Faculty of Engineering; 01. Izmir Institute of TechnologyBiocatalysis is a useful strategy for sustainable green synthesis of fine chemicals due to its high catalytic rate, reaction specificity, and operation under ambient conditions. Addressable immobilization of enzymes onto solid supports for one-pot multistep biocatalysis, however, remains a major challenge. In natural pathways, enzymes are spatially coupled to prevent side reactions, eradicate inhibitory products, and channel metabolites sequentially from one enzyme to another. Construction of a modular immobilization platform enabling spatially directed assembly of multiple biocatalysts would, therefore, not only allow the development of high-efficiency bioreactors but also provide novel synthetic routes for chemical synthesis. In this study, we developed a modular cascade flow reactor using a generalizable solid-binding peptide-directed immobilization strategy that allows selective immobilization of fusion enzymes on anodic aluminum oxide (AAO) monoliths with high positional precision. Here, the lactate dehydrogenase and formate dehydrogenase enzymes were fused with substrate-specific peptides to facilitate their self-immobilization through the membrane channels in cascade geometry. Using this cascade model, two-step biocatalytic production of l-lactate is demonstrated with concomitant regeneration of soluble nicotinamide adenine dinucleotide (NADH). Both fusion enzymes retained their catalytic activity upon immobilization, suggesting their optimal display on the support surface. The 85% cascading reaction efficiency was achieved at a flow rate that kinetically matches the residence time of the slowest enzyme. In addition, 84% of initial catalytic activity was preserved after 10 days of continuous operation at room temperature. The peptide-directed modular approach described herein is a highly effective strategy to control surface orientation, spatial localization, and loading of multiple enzymes on solid supports. The implications of this work provide insight for the single-step construction of high-power cascadic devices by enabling co-expression, purification, and immobilization of a variety of engineered fusion enzymes on patterned surfaces. © 2021 The Authors. Published by American Chemical Society.