Please use this identifier to cite or link to this item: https://hdl.handle.net/20.500.11851/1023
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dc.contributor.authorKabay, Gözde-
dc.contributor.authorCan, Gizem Kaleli-
dc.contributor.authorMutlu, Mehmet-
dc.date.accessioned2019-05-23T05:48:44Z
dc.date.available2019-05-23T05:48:44Z
dc.date.issued2017-11
dc.identifier.citationKabay, G., Can, G. K., & Mutlu, M. (2017). Amyloid-like protein nanofibrous membranes as a sensing layer infrastructure for the design of mass-sensitive biosensors. Biosensors and Bioelectronics, 97, 285-291.en_US
dc.identifier.issn0956-5663
dc.identifier.othernumber of pages 7
dc.identifier.urihttps://doi.org/10.1016/j.bios.2017.06.016-
dc.identifier.urihttps://hdl.handle.net/20.500.11851/1023-
dc.description.abstractQuartz crystal microbalances (QCMs) have been used in the literature for mass sensitive biosensor applications. However, their performance, reliability and stability have been limited by the chemical treatment steps required for the functionalization and activation of the QCM surface, prior to antibody immobilization. Specifically, these steps cause increased film thickness, which diminishes performance by mass overload, and create a harsh environment, which reduces biological activity. In this work, we eliminated this chemical step by introducing a sensing layer modification using electrospun amyloid like-bovine serum albumin (AL-BSA) nanofibers on QCM surfaces. Owing to the self-functionality of AL-BSA nanofibers, these modified QCM surfaces were directly activated by glutaraldehyde (GA). To assess the performance of these modified electrodes, a model protein, lysozyme (Lys), was selected as the biological agent to be immobilized. Frequency measurements were performed in batch (dip-and-dry) and continuous (flow-cell) processes, and binding performances were compared. AL-BSA modified surfaces were characterized by X-ray photoelectron spectroscopy (XPS), scanning electron microscope (SEM), quartz crystal microbalance (QCM), contact angle (CA) and attenuated total reflectance-Fourier transform infrared spectroscopy (ATR-FTIR). Protein detection was measured based on the frequency shift before and after the covalent bonding of Lys. Under optimized conditions, the proposed immobilization platforms could bind 335 ng/mL and 250 ng/mL of Lys for batch and continuous processes, respectively. Our results demonstrate the potential usage of these self-functional electrospun AL-BSA infrastructure sensing layers on QCM surfaces. This modification enables the direct immobilization of bioactive agents by eliminating any surface functionalization process for further mass-sensitive biosensor applications.en_US
dc.language.isoenen_US
dc.publisherElsevier Advanced Technologyen_US
dc.relation.ispartofBiosensors & Bioelectronicsen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectamyloid-like proteinen_US
dc.subjectquartz crystal microbalanceen_US
dc.subjectelectrospinningen_US
dc.subjectlysozymeen_US
dc.subjectbovine serum albuminen_US
dc.subjectprotein immobilizationen_US
dc.titleAmyloid-like protein nanofibrous membranes as a sensing layer infrastructure for the design of mass-sensitive biosensorsen_US
dc.typeArticleen_US
dc.departmentFaculties, Faculty of Engineering, Department of Biomedical Engineeringen_US
dc.departmentFakülteler, Mühendislik Fakültesi, Biyomedikal Mühendisliği Bölümütr_TR
dc.identifier.volume97
dc.identifier.startpage285
dc.identifier.endpage291
dc.relation.tubitakScientific and Technological Research Council of Turkey [215Z047]en_US
dc.authorid0000-0001-7146-1937-
dc.authorid0000-0002-8594-3459-
dc.identifier.wosWOS:000405153000040en_US
dc.identifier.scopus2-s2.0-85020663125en_US
dc.institutionauthorMutlu, Mehmet-
dc.institutionauthorKabay, Gözde-
dc.identifier.pmid28618364en_US
dc.identifier.doi10.1016/j.bios.2017.06.016-
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.identifier.scopusqualityQ1-
item.fulltextNo Fulltext-
item.languageiso639-1en-
item.openairetypeArticle-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.cerifentitytypePublications-
item.grantfulltextnone-
crisitem.author.dept02.2. Department of Biomedical Engineering-
Appears in Collections:Biyomedikal Mühendisliği Bölümü / Department of Biomedical Engineering
PubMed İndeksli Yayınlar Koleksiyonu / PubMed Indexed Publications Collection
Scopus İndeksli Yayınlar Koleksiyonu / Scopus Indexed Publications Collection
WoS İndeksli Yayınlar Koleksiyonu / WoS Indexed Publications Collection
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