Surface plasmon resonance sensors for real-time detection of cyclic citrullinated peptide antibodies

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dc.authorid0000-0001-5173-1522en_US
dc.authorid0000-0003-3260-1639
dc.authorid0000-0001-7548-5741
dc.contributor.authorDibekkaya, Hüseyin
dc.contributor.authorSaylan, Yeşeren
dc.contributor.authorYılmaz, Fatma
dc.contributor.authorDerazshamshir, Ali
dc.contributor.authorDenizli, Adil
dc.date.accessioned2021-06-23T19:44:23Z
dc.date.available2021-06-23T19:44:23Z
dc.date.issued2016
dc.departmentBAİBÜ, Gerede Meslek Yüksekokulu, Kimya Ve Kimyasal İşleme Teknolojileri Bölümüen_US
dc.description.abstractSurface plasmon resonance (SPR) sensors have been used for detection of various biomolecules because of their simplicity, high specificity and sensitivity, real-time detection, low cost, and no requirement of labeling. Recently, molecularly imprinted polymers that are easy to prepare, less expensive, stable, have talent for molecular recognition and also are used for creation selective binding sites for target molecule on the SPR sensors. Here, we show that preparation of cyclic citrullinated peptide antibody (anti-CCP) imprinted SPR sensor to detect CCP antibodies. For this purpose, anti-CCP/AAm pre-complex was synthesized by interacting acrylamide (AAm) monomer with anti-CCP. Then, anti-CCP imprinted (anti-CCP/PAAm) SPR sensor was obtained by reacting with anti-CCP/AAm pre-complex in the presence of the crosslinker, and initiator/activator pair. Besides this, non-imprinted (PAAm) SPR sensor was also prepared without using anti-CCP template. The SPR sensors were characterized and then adsorption-desorption studies were performed with pH 7.0 phosphate buffer (10mM) and acetic acid (10%) with Tween 20 (1%) in pH 7.0 phosphate buffer. Selectivitiy of sensors was investigated by using immunoglobulin M (IgM) and bovine serum albumin (BSA). To determine the adsorption model of interactions between anti-CCP solutions and anti-CCP/PAAm SPR sensor, different adsorption models were performed. The calculated maximum reflection, detection limit, association and dissociation constants were 1.079RU/mL, 0.177RU/mL, 0.589RU/mL and 1.697mL/RU, respectively. Repeatability experiments of anti-CCP/PAAm SPR sensor was performed four times with adsorption-desorption-regeneration cycles without any performance losing. Results showed that anti-CCP/PAAm SPR sensor had high selectivity and sensitivity for detection of CCP antibodies.en_US
dc.identifier.doi10.1080/10601325.2016.1201756
dc.identifier.endpage594en_US
dc.identifier.issn1060-1325
dc.identifier.issn1520-5738
dc.identifier.issue9en_US
dc.identifier.scopus2-s2.0-84978704756en_US
dc.identifier.scopusqualityQ2en_US
dc.identifier.startpage585en_US
dc.identifier.urihttps://doi.org/10.1080/10601325.2016.1201756
dc.identifier.urihttps://hdl.handle.net/20.500.12491/8974
dc.identifier.volume53en_US
dc.identifier.wosWOS:000381060600008en_US
dc.identifier.wosqualityQ3en_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakScopusen_US
dc.institutionauthorYılmaz, Fatma
dc.language.isoenen_US
dc.publisherTaylor & Francis Incen_US
dc.relation.ispartofJournal Of Macromolecular Science Part A-Pure And Applied Chemistryen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectAnti-CCPen_US
dc.subjectMolecular Imprintingen_US
dc.subjectSPR Sensoren_US
dc.subjectSurface Plasmon Resonanceen_US
dc.titleSurface plasmon resonance sensors for real-time detection of cyclic citrullinated peptide antibodiesen_US
dc.typeArticleen_US

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