Please use this identifier to cite or link to this item: https://hdl.handle.net/20.500.11851/12511
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dc.contributor.authorAkyel, Hilal-
dc.contributor.authorZirh, Elham Bahador-
dc.contributor.authorZirh, Selim-
dc.contributor.authorYazgi, Hare-
dc.contributor.authorTel, Banu Cahide-
dc.date.accessioned2025-06-11T20:40:58Z-
dc.date.available2025-06-11T20:40:58Z-
dc.date.issued2025-
dc.identifier.issn0250-4685-
dc.identifier.issn1303-829X-
dc.identifier.urihttps://doi.org/10.1515/tjb-2025-0031-
dc.identifier.urihttps://hdl.handle.net/20.500.11851/12511-
dc.description.abstractObjectives Alpha-synuclein (alpha-syn) fibrils, which are associated with Lewy-like inclusions, are currently utilized in the modeling of Parkinson's disease (PD). The fibrils require a length shorter than 100 nm to uptake intracellularly. Our study aims to determine the optimal probe sonication parameters that can be applied in diverse laboratory settings for the fragmentation of fibrils to lengths of <= 100 nm.Methods In our study, human wild-type alpha-syn fibrils were sonicated with 1, 3, and 5 s-on/off pulse applications at varying ambient temperatures (room temperature, ice, and ice-surrounded by dry ice) for a duration of 1 min, with a total of 40 and 60 cycles, respectively. The length of the fibrils was quantified by transmission electron microscopy imaging. The total alpha-syn in SH-SY5Y cells was detected by immunofluorescence staining following the administration of fragmented fibrils after 2-, 4-, and 6-day incubations.Results Although fragmentation was observed under all conditions, fibrils of <= 100 nm were obtained with a 5 s-on/off pulse in ice and ice-surrounded by dry ice ambientes. The fibril length of <= 100 nm was observed on days 2 and 4; however, the highest level of observed intensity was detected on day 6.Conclusions The application of 5 s-on/off consecutive pulses in ice, and ice-surrounded by dry ice ambientes are more effective methods for fragmenting and internalizing fibrils, thereby forming a reproducible cellular PD-like model. In summary, our study provides a significant contribution to the development of an economical and effective sonication methodology for the fragmentation of fibrils in a diverse of laboratory settings.en_US
dc.description.sponsorshipTOBB Economy and Technology Universityen_US
dc.description.sponsorshipWe express our acknowledgement to Prof. Bulent Elibol and Assoc. Prof. Gul Yalcin-Cakmakli for their contributions to purchase of the fibrils and to Assoc. Prof. Urartu Ozgur Safak Seker for providing the opportunity to work in his laboratory at National Nanotechnology Research Center, Bilkent University in Ankara, Turkiye during the fibril sonication and Ph.D. student Cemile Elif Ozcelik for her assistance in the laboratory. Moreover, we acknowledge the support provided by TOBB Economy and Technology University for transmission electron microscopy imaging.en_US
dc.language.isoenen_US
dc.publisherWalter de Gruyter Gmbhen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectAlpha-Synuclein Fibrilen_US
dc.subjectSonicationen_US
dc.subjectCell Cultureen_US
dc.subjectTransmission Electron Microscopyen_US
dc.subjectParkinson'S Diseaseen_US
dc.titleComparison of Various Fragmentation Methods of Alpha-Synuclein Fibrils for Establishing a Parkinson's Disease-Like Model in Cell Cultureen_US
dc.typeArticleen_US
dc.departmentTOBB University of Economics and Technologyen_US
dc.identifier.wosWOS:001494829200001-
dc.identifier.doi10.1515/tjb-2025-0031-
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.identifier.scopusqualityQ4-
dc.identifier.wosqualityQ4-
dc.description.woscitationindexScience Citation Index Expanded-
item.fulltextNo Fulltext-
item.grantfulltextnone-
item.languageiso639-1en-
item.openairetypeArticle-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.cerifentitytypePublications-
Appears in Collections:WoS İndeksli Yayınlar Koleksiyonu / WoS Indexed Publications Collection
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