Electrosynthesized MIPs for transferrin: Plastibodies or nano-filters?

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dc.contributor.authorZhang, Xiaorong
dc.contributor.authorYarman, Aysu
dc.contributor.authorErdossy, Julia
dc.contributor.authorKatz, Sagie
dc.contributor.authorZebger, Ingo
dc.contributor.authorJetzschmann, Katharina J.
dc.contributor.authorScheller, Frieder W.
dc.date.accessioned2021-01-08T21:51:24Z
dc.date.available2021-01-08T21:51:24Z
dc.date.issued2018
dc.departmentTAÜ, Fen Fakültesi, Moleküler Biyoteknoloji Bölümüen_US
dc.descriptionGyurcsanyi, Robert E./0000-0002-9929-7865en_US
dc.descriptionWOS:000426024200005en_US
dc.descriptionPubMed: 29351867en_US
dc.description.abstractMolecularly imprinted polymer (MP) nanofilrns for transferrin (Trf) have been synthesized on gold surfaces by electro-polymerizing the functional monomer scopoletin in the presence of the protein target or around pre-adsorbed Trf. As determined by atomic force microscopy (AFM) the film thickness was comparable with the molecular dimension of the target. The target (re)binding properties of the electro-synthesized MIP films was evaluated by cyclic voltammetry (CV) and square wave voltammetry (SWV) through the target-binding induced permeability changes of the MIP nanofilms to the ferricyanide redox marker, as well as by surface plasmon resonance (SPR) and surface enhanced infrared absorption spectroscopy (SEIRAS) of the immobilized protein molecules. For Trf a linear concentration dependence in the lower micromolar range and an imprinting factor of similar to 5 was obtained by SWV and SPR. Furthermore, non-target proteins including the iron-free apo-Trf were discriminated by pronounced size and shape specificity. Whilst it is generally assumed that the rebinding of the target or of cross-reacting proteins exclusively takes place at the polymer here we considered also the interaction of the protein molecules with the underlying gold transducers. We demonstrate by SWV that adsorption of proteins suppresses the signal of the redox marker even at the bare gold surface and by SEIRAS that the treatment of the MIP with proteinase K or NaOH only partially removes the target protein. Therefore, we conclude that when interpreting binding of proteins to directly MIP-covered gold electrodes the interactions between the protein and the gold surface should also be considered.
dc.description.sponsorshipERA-Chemistry [61133, OTKANN117637]; Cluster of Excellence [EXC 314]; Lendulet program of the Hungarian Academy of Sciences [LP 2013 - 63]
dc.description.sponsorshipThe authors would like to thank ERA-Chemistry (2014, 61133; OTKANN117637) for the financial support. This work is a part of UniCat, the Cluster of Excellence (EXC 314) coordinated by the Technical University of Berlin within the framework of the German Excellence Initiative. RGy acknowledges additionally the support of the Lendulet program of the Hungarian Academy of Sciences (LP 2013 - 63).
dc.identifier.doi10.1016/j.bios.2018.01.011
dc.identifier.endpage35en_US
dc.identifier.issn0956-5663
dc.identifier.issn1873-4235
dc.identifier.scopus2-s2.0-85041335276
dc.identifier.scopusqualityQ1
dc.identifier.startpage29en_US
dc.identifier.urihttp://doi.org/10.1016/j.bios.2018.01.011
dc.identifier.urihttps://hdl.handle.net/20.500.12846/223
dc.identifier.volume105en_US
dc.identifier.wosWOS:000426024200005
dc.identifier.wosqualityQ1
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.indekslendigikaynakPubMed
dc.institutionauthorYarman, Aysu
dc.language.isoen
dc.publisherElsevier Advanced Technology
dc.relation.ispartofBiosensors & Bioelectronics
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı
dc.rightsinfo:eu-repo/semantics/openAccess
dc.subjectMolecularly Imprinted Polymeren_US
dc.subjectScopoletinen_US
dc.subjectTransferrinen_US
dc.subjectProtein Adsorptionen_US
dc.subjectRedox Markeren_US
dc.titleElectrosynthesized MIPs for transferrin: Plastibodies or nano-filters?
dc.typeArticle

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