Acrylamide-encapsulated glucose oxidase inhibits breast cancer cell viability
dc.authorid | Öykü Gönül Geyik / 0000-0003-3014-1253 | en_US |
dc.authorscopusid | Öykü Gönül Geyik / 56695248800 | |
dc.authorwosid | Öykü Gönül Geyik / AHB-4716-2022 | |
dc.contributor.author | Rrustemi, Trendelina | |
dc.contributor.author | Gönül Geyik, Öykü | |
dc.contributor.author | Özkaya, Ali Burak | |
dc.contributor.author | Öztürk, Taylan Kurtuluş | |
dc.contributor.author | Yüce, Zeynep | |
dc.contributor.author | Kılınç, Ali | |
dc.date.accessioned | 2021-01-22T08:34:15Z | |
dc.date.available | 2021-01-22T08:34:15Z | |
dc.date.issued | 2020 | en_US |
dc.department | İstinye Üniversitesi, Sağlık Bilimleri Fakültesi, Beslenme ve Diyetetik Bölümü | en_US |
dc.description.abstract | Objectives: Cancer cells modulate metabolic pathways to ensure continuity of energy, macromolecules and redoxhomeostasis. Although these vulnerabilities are often targeted individually, targeting all with an enzyme may prove a novel approach. However, therapeutic enzymes are prone to proteolytic degradation and neutralizing antibodies leading to a reduced half-life and effectiveness. We hypothesized that glucose oxidase (GOX) enzyme that catalyzes oxidation of glucose and production of hydrogen peroxide, may hit all these targets by depleting glucose; crippling anabolic pathways and producing reactive oxygen species (ROS); unbalancing redox homeostasis. Methods: We encapsulated GOX in an acrylamide layer and then performed activity assays in denaturizing settings to determine protection provided by encapsulation. Afterwards, we tested the effects of encapsulated (enGOX) and free (fGOX) enzyme on MCF-7 breast cancer cells. Results: GOX preserved 70% of its activity following encapsulation. When fGOX and enGOX treated with guanidinium chloride, fGOX lost approximately 72% of its activity, while enGOX only lost 30%. Both forms demonstrated remarkable resilience against degradation by proteinase K and inhibited viability of MCF-7 cells in an activity-dependent manner. Conclusions: Encapsulation provided protection to GOX against denaturation without reducing its activity, which would prolong half-life of the enzyme when administered intravenously. | en_US |
dc.identifier.citation | Rrustemi, T., Geyik, Ö. G., Özkaya, A. B., Öztürk, T. K., Yüce, Z., & Kılınç, A. (2020). Acrylamide-encapsulated glucose oxidase inhibits breast cancer cell viability. Turkish Journal of Biochemistry, 1(ahead-of-print). | en_US |
dc.identifier.doi | 10.1515/tjb-2020-0247 | en_US |
dc.identifier.endpage | 816 | en_US |
dc.identifier.issn | 0250-4685 | en_US |
dc.identifier.issn | 1303-829X | en_US |
dc.identifier.issue | 6 | en_US |
dc.identifier.scopus | 2-s2.0-85098995566 | en_US |
dc.identifier.scopusquality | Q4 | en_US |
dc.identifier.startpage | 811 | en_US |
dc.identifier.uri | https://doi.org/10.1515/tjb-2020-0247 | |
dc.identifier.uri | https://hdl.handle.net/20.500.12713/1358 | |
dc.identifier.volume | 45 | en_US |
dc.identifier.wos | WOS:000603517600022 | en_US |
dc.identifier.wosquality | Q4 | en_US |
dc.indekslendigikaynak | Web of Science | en_US |
dc.indekslendigikaynak | Scopus | en_US |
dc.institutionauthor | Gönül Geyik, Öykü | |
dc.language.iso | en | en_US |
dc.publisher | WALTER DE GRUYTER GMBH | en_US |
dc.relation.ispartof | TURKISH JOURNAL OF BIOCHEMISTRY-TURK BIYOKIMYA DERGISI | en_US |
dc.relation.publicationcategory | Makale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı | en_US |
dc.rights | info:eu-repo/semantics/closedAccess | en_US |
dc.subject | Biocompatibility | en_US |
dc.subject | Cancer Therapy | en_US |
dc.subject | Glucose Oxidase | en_US |
dc.subject | MCF-7 | en_US |
dc.subject | Single Enzyme Nanoparticle | en_US |
dc.subject | Starving-Like Therapy | en_US |
dc.subject | Therapeutic Enzyme | en_US |
dc.title | Acrylamide-encapsulated glucose oxidase inhibits breast cancer cell viability | en_US |
dc.type | Article | en_US |
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