@article{Scheller2001, author = {Scheller, Frieder W.}, title = {Biomolek{\"u}le als Reporter in der Analytik : keine Forschung im Elfenbeinturm}, year = {2001}, language = {de} } @article{Scheller2000, author = {Scheller, Frieder W.}, title = {Biomolekulare Erkennungssysteme f{\"u}r die Biochemische Analytik}, year = {2000}, language = {de} } @article{WarsinkeBenkertScheller1996, author = {Warsinke, Axel and Benkert, Alexander and Scheller, Frieder W.}, title = {Biomolecular modules for creatinine determination}, year = {1996}, language = {en} } @article{SchellerLettau2003, author = {Scheller, Frieder W. and Lettau, Kristian}, title = {Biomimetische Rezeptoren und Biochips}, year = {2003}, language = {de} } @article{SchellerBierNeumann1994, author = {Scheller, Frieder W. and Bier, Frank Fabian and Neumann, B.}, title = {Bioindikation in aquatischen {\"O}kosystemen : Bioindikation in limnischen und k{\"u}stennahen {\"O}kosystemen ; Grundlagen, Verfahren und Methoden}, publisher = {Fischer}, address = {Jena}, pages = {S. 380 - 386}, year = {1994}, language = {de} } @article{SigolaevaMarkowerEremenkoetal.2001, author = {Sigolaeva, L. V. and Markower, Alexander and Eremenko, A. V. and Makhaeva, G. F. and Malygin, V. V. and Kurochkin, I. N. and Scheller, Frieder W.}, title = {Bioelectrochemical anaysis of neuropathy targes esterase activity in blood}, year = {2001}, language = {en} } @article{SchellerWollenbergerLeietal.2002, author = {Scheller, Frieder W. and Wollenberger, Ursula and Lei, Chenghong and Jin, Wen and Ge, Bixia and Lehmann, Claudia and Lisdat, Fred and Fridman, Vadim}, title = {Bioelectrocatalysis by redox enzymes at modified electrodes}, year = {2002}, language = {en} } @article{YarmanNagelGajovicEichelmannetal.2011, author = {Yarman, Aysu and Nagel, Thomas and Gajovic-Eichelmann, Nenad and Fischer, Anna and Wollenberger, Ursula and Scheller, Frieder W.}, title = {Bioelectrocatalysis by Microperoxidase-11 in a Multilayer Architecture of Chitosan Embedded Gold Nanoparticles}, series = {Electroanalysis : an international journal devoted to fundamental and practical aspects of electroanalysis}, volume = {23}, journal = {Electroanalysis : an international journal devoted to fundamental and practical aspects of electroanalysis}, number = {3}, publisher = {Wiley-Blackwell}, address = {Malden}, issn = {1040-0397}, doi = {10.1002/elan.201000535}, pages = {611 -- 618}, year = {2011}, abstract = {We report on the redox behaviour of the microperoxidase-11 (MP-11) which has been electrostatically immobilized in a matrix of chitosan-embedded gold nanoparticles on the surface of a glassy carbon electrode. MP-11 contains a covalently bound heme c as the redox active group that exchanges electrons with the electrode via the gold nanoparticles. Electroactive surface concentration of MP-11 at high scan rate is between 350+/-50 pmol cm(-2), which reflects a multilayer process. The formal potential (E degrees') of MP-11 in the gold nanoparticles-chitosan film was estimated to be -(267.7+/-2.9) mV at pH 7.0. The heterogeneous electron transfer rate constant (k(s)) starts at 1.21 s(-1) and levels off at 6.45 s(-1) in the scan rate range from 0.1 to 2.0 V s(-1). Oxidation and reduction of MP-11 by hydrogen peroxide and superoxide, respectively have been coupled to the direct electron transfer of MP-11.}, language = {en} } @article{BogdanovskayaFridmanTarasevichetal.1994, author = {Bogdanovskaya, V. A. and Fridman, Vadim and Tarasevich, M. R. and Scheller, Frieder W.}, title = {Bioelectrocatalysis by immobilized peroxidase : the reaction mechanism and the possibility of electroanalytical detection of both inhibitors and activators of enzyme}, year = {1994}, language = {en} } @article{LehmannWollenbergerBrigeliusFloheetal.1998, author = {Lehmann, Claudia and Wollenberger, Ursula and Brigelius-Floh{\´e}, Regina and Scheller, Frieder W.}, title = {Bioelectrocatalysis by a selenoenzyme}, year = {1998}, language = {en} } @article{JetzschmannTankJagerszkietal.2019, author = {Jetzschmann, Katharina J. and Tank, Steffen and Jagerszki, Gyula and Gyurcsanyi, Robert E. and Wollenberger, Ulla and Scheller, Frieder W.}, title = {Bio-Electrosynthesis of Vectorially Imprinted Polymer Nanofilms for Cytochrome P450cam}, series = {ChemElectroChem}, volume = {6}, journal = {ChemElectroChem}, number = {6}, publisher = {Wiley-VCH}, address = {Weinheim}, issn = {2196-0216}, doi = {10.1002/celc.201801851}, pages = {1818 -- 1823}, year = {2019}, abstract = {A new approach for synthesizing a vectorially imprinted polymer (VIP) is presented for the microbial cytochrome P450cam enzyme. A surface attached binding motif of a natural reaction partner of the target protein, putidaredoxin (Pdx), is the anchor to the underlying transducer. The 15 amino acid peptide anchor, which stems from the largest continuous amino acid chain within the binding site of Pdx was modified: (i) internal cysteines were replaced by serines to prevent disulfide bond formation; (ii) 2 ethylene glycol units were attached to the N-terminus as a spacer region; and (iii) an N-terminal cysteine was added to allow the immobilization on the gold electrode surface. Immobilization on GCE was achieved via an N-(1-pyrenyl)maleimide (NPM) cross-linker. In this way oriented immobilization of P450cam was accomplished by binding it to a peptide-modified gold or glassy carbon electrode (GCE) prior to the electrosynthesis of a polymer nanofilm around the immobilized target. This VIP nanofilm enabled reversible oriented docking of P450cam as it is indicated by the catalytic oxygen reduction via direct electron transfer between the enzyme and the underlying electrode. Catalysis of oxygen reduction by P450cam bound to the VIP-modified GCE was used to measure rebinding to the VIP. The mild coupling of an oxidoreductase with the electrode may be appropriate for realizing electrode-driven substrate conversion by instable P450 enzymes without the need of NADPH co-factor.}, language = {en} } @article{SchellerYarman2015, author = {Scheller, Frieder W. and Yarman, Aysu}, title = {Bio vs. Mimetika in der Bioanalytik}, series = {Biochemie und analytische Biochemie}, volume = {4}, journal = {Biochemie und analytische Biochemie}, number = {2}, issn = {2161-1009}, pages = {2}, year = {2015}, abstract = {Nat{\"u}rliche Evolution hat geschaffenBiopolymereauf der Basis von Aminos{\"a}uren undNukleotidezeigt hohe chemische Selektivit{\"a}t und katalytische Kraft. Die molekulare Erkennung durch Antik{\"o}rper und die katalytische Umwandlung der Substratmolek{\"u}le durch Enzyme findet in sogenannten Paratopen oder katalytischen Zentren des Makromolek{\"u}ls statt, die typischerweise 10-15 Aminos{\"a}uren umfassen. Die konzertierte Wechselwirkung zwischen den Reaktionspartnern f{\"u}hrt zu Affinit{\"a}ten bis zu nanomolaren Konzentrationen f{\"u}r die Antigenbindung und n{\"a}hert sich einer Million Ums{\"a}tze pro Sekunde anEnzym-katalysierte Reaktionen.}, language = {de} } @article{SchellerScheller1996, author = {Scheller, Frieder W. and Scheller, A.}, title = {Bi-Enzymelektrode zur Messung von Sorbitol in pharmazeutischen Produkten}, year = {1996}, language = {de} } @article{BauerEremenkoKuehnetal.1998, author = {Bauer, Christian G. and Eremenko, A. V. and K{\"u}hn, A. and K{\"u}rzinger, K. and Markower, Alexander and Scheller, Frieder W.}, title = {Automated amplifield flow immunoassay for cocaine}, year = {1998}, language = {en} } @article{OzcelikayKurbanogluYarmanetal.2020, author = {Ozcelikay, Goksu and Kurbanoglu, Sevinc and Yarman, Aysu and Scheller, Frieder W. and Ozkan, Sibel A.}, title = {Au-Pt nanoparticles based molecularly imprinted nanosensor for electrochemical detection of the lipopeptide antibiotic drug Daptomycin}, series = {Sensors and actuators : B, Chemical}, volume = {320}, journal = {Sensors and actuators : B, Chemical}, publisher = {Elsevier Science}, address = {Amsterdam}, issn = {0925-4005}, doi = {10.1016/j.snb.2020.128285}, pages = {7}, year = {2020}, abstract = {In this work, a novel electrochemical molecularly imprinted polymer (MIP) sensor for the detection of the lipopeptide antibiotic Daptomycin (DAP) is presented which integrates gold decorated platinum nanoparticles (Au-Pt NPs) into the nanocomposite film. The sensor was prepared by electropolymerization of o-phenylenediamine (o-PD) in the presence of DAP using cyclic voltammetry. Cyclic voltammetry and differential pulse voltammetry were applied to follow the changes in the MIP-layer related to rebinding and removal of the target DAP by using the redox marker [Fe(CN)(6)](3-/4-). Under optimized operational conditions, the MIP/Au-Pt NPs/ GCE nanosensor exhibits a linear response in the range of 1-20 pM towards DAP. The limit of detection and limit of quantification were determined to be 0.161pM +/- 0.012 and 0.489pM +/- 0.012, respectively. The sensitivity towards the antibiotics Vancomycin and Erythromycin and the amino acids glycine and tryptophan was below 7 percent as compared with DAP. Moreover, the nanosensor was also successfully used for the detection of DAP in deproteinated human serum samples.}, language = {en} } @article{SchellerLisdatWollenberger2005, author = {Scheller, Frieder W. and Lisdat, Fred and Wollenberger, Ursula}, title = {Application of electrically contacted enzymes for biosensors}, isbn = {3-527- 30690-0}, year = {2005}, language = {en} } @article{StrefferKaatzBaueretal.1998, author = {Streffer, Katrin and Kaatz, Helvi and Bauer, Christian G. and Makower, Alexander and Schulmeister, Thomas and Scheller, Frieder W. and Peter, Martin G. and Wollenberger, Ursula}, title = {Application of a sensitive catechol detector for determination of tyrosinase inhibitors}, year = {1998}, language = {en} } @article{SchellerTiepnerWarsinke2004, author = {Scheller, Frieder W. and Tiepner, K. and Warsinke, Axel}, title = {Anwendung von Biosensoren in der Lebensmittelanalytik}, isbn = {3-89947-120-2}, year = {2004}, language = {de} } @article{Scheller2002, author = {Scheller, Frieder W.}, title = {Analytische Biochemie : Entwicklung von Biosensoren und Biochips}, year = {2002}, language = {de} } @article{SchellerBier2004, author = {Scheller, Frieder W. and Bier, Frank Fabian}, title = {Analytical Biochemistry (Editorial)}, year = {2004}, language = {en} } @article{LisdatUtepbergenovHaseloffetal.2001, author = {Lisdat, Fred and Utepbergenov, D. and Haseloff, R. F. and Blasig, Ingolf E. and St{\"o}cklein, Walter F. M. and Scheller, Frieder W. and Brigelius-Floh{\´e}, Regina}, title = {An optical method for the detection of oxidative stress using protein-RNA interaction}, year = {2001}, language = {en} } @article{LettauWarsinkeLaschewskyetal.2004, author = {Lettau, Kristian and Warsinke, Axel and Laschewsky, Andr{\´e} and Mosbach, K. and Yilmaz, E. and Scheller, Frieder W.}, title = {An esterolytic imprinted polymer prepared via a silica-supported transition state analogue}, year = {2004}, abstract = {In this work we describe a new preparation method for an esterolytic imprinted polymer with catalytic sites on the surface. A template was prepared by immobilizing a transition state analogue (phosphoramidic acid derivative) of an esterolytic reaction within porous silica particles. Polymerization within the pores was carried out using 4- vinylimidazole as a functional monomer and divinylbenzene as a cross-linker. The polymer was released by dissolution of the silica support with hydrofluoric acid and catalytic properties were studied by incubation with three different 4- nitrophenylesters and spectrophotometric determination of the released 4-nitrophenol. For 4-nitrophenyl acetate an activity of 211 nmol min(-1) mg(-1) and a K-m value of 2.2 mmol L-1 was obtained}, language = {en} } @article{BierEhrentreichFoersterMakoweretal.1996, author = {Bier, Frank Fabian and Ehrentreich-F{\"o}rster, Eva and Makower, Alexander and Scheller, Frieder W.}, title = {An enzymatic amplification cycle for high sensitive immunoassay}, year = {1996}, language = {en} } @article{MakWollenbergerSchelleretal.2003, author = {Mak, Karen K. W. and Wollenberger, Ursula and Scheller, Frieder W. and Renneberg, Reinhard}, title = {An amperometric bi-enzyme sensor for determination of formate using cofactor regeneration}, year = {2003}, language = {en} } @article{BierEhrentreichFoersterScheller1996, author = {Bier, Frank Fabian and Ehrentreich-F{\"o}rster, Eva and Scheller, Frieder W.}, title = {Amplifying bienzyme cycle-linked immunoassays for determination of 2,4- dichlorphenoxyacetic acid}, year = {1996}, language = {en} } @article{KirsteinKirsteinSchelleretal.1998, author = {Kirstein, Dieter and Kirstein, Lincoln and Scheller, Frieder W. and Borcherding, H.}, title = {Amperometric nitrate biosensors on the basis of Pseudomonas stutzeri nitrate reductase}, year = {1998}, language = {en} } @article{IlievKaishevaSchelleretal.1995, author = {Iliev, I. and Kaisheva, A. and Scheller, Frieder W. and Pfeiffer, Dorothea}, title = {Amperometric gas-diffusion / enzyme electrode}, year = {1995}, language = {en} } @article{PfeifferSchellerSchubertetal.1993, author = {Pfeiffer, Dorothea and Scheller, Frieder W. and Schubert, Florian and Setz, K.}, title = {Amperometric enzyme electrodes for lactate and glucose determinations in highly diluted and undiluted media}, year = {1993}, language = {en} } @article{IgnatovShishniashviliGeetal.2002, author = {Ignatov, S. and Shishniashvili, D. and Ge, Bixia and Scheller, Frieder W. and Lisdat, Fred}, title = {Amperometric biosensor based on a functionalized gold electrode for the detection of antioxidants}, year = {2002}, language = {en} } @article{BarminEremenkoOsipovaetal.1999, author = {Barmin, Anatoli V. and Eremenko, Arkadi V. and Osipova, T. and Kurochkin, Iliya and Makower, Alexander and Scheller, Frieder W.}, title = {Affinyi fermentometrischeskii analis ingibitorov cholinestarasi}, year = {1999}, language = {ru} } @article{LiuWollenbergerHalameketal.2005, author = {Liu, Songqin and Wollenberger, Ursula and Halamek, Jan and Leupold, Eik and St{\"o}cklein, Walter F. M. and Warsinke, Axel and Scheller, Frieder W.}, title = {Affinity interaction betwen phenylboronic acid-carrying self-assembled monolayers and FAD or HRP}, year = {2005}, abstract = {A method is provided for the recognition of glycated molecules based on their binding affinities to boronate- carrying monolayers. The affinity interaction of flavin adenine dinucleotide (FAD) and horseradish peroxidase (HRP) with phenylboronic acid monolayers on gold was investigated by using voltammetric and microgravimetric methods. Conjugates of 3-aminopherrylboronic acid and 3,3'-dithiodipropionic acid di(N-hydroxysuccinimide ester) or 11-mercaptoundecanoic acid were prepared and self-assembled on gold surfaces to generate monolayers. FAD is bound to this modified sur-face and recognized by a pair of redox peaks with a formal potential of -0.433 V in a 0.1 m phosphate buffer solution, pH 6.5. Upon addition of a sugar to the buffer, the bound FAD could be replaced, indicating that the binding is reversible. Voltammetric, mass measurements, and photometric activity assays show that the HRP can also be bound to the interface. This binding is reversible, and HRP can be replaced by sorbitol or removed in acidic solution. The effects of pH, incubation time, and concentration of H2O2 were studied by comparing the catalytic reduction of H2O2 in the presence of the electron-donor thionine. The catalytic current of the HRP-loaded electrode was proportional to HRP concentrations in the incubation solution in the range between 5 mu g mL(-1) and 0.4 mg mL(-1) with a linear slope of 3.34 mu A mL mg(-1) and a correlation coefficient of 0.9945}, language = {en} } @article{MakowerBarminMorzunovaetal.1997, author = {Makower, Alexander and Barmin, Anatoli V. and Morzunova, T. and Eremenko, Arkadi V. and Bier, Frank Fabian and Scheller, Frieder W.}, title = {Affinity enzymomoetric assay for detection of organophosphorus compounds}, year = {1997}, language = {en} } @article{StoellnerSchellerWarsinke2002, author = {Stoellner, Daniela and Scheller, Frieder W. and Warsinke, Axel}, title = {Activation of cellulose membranes with 1,1{\"i}-carbonyldiimidazole or 1-cyano-4-4-dimethylaminopyridinium tetrafluoroborate as a basis for the development of immunosensors}, year = {2002}, language = {en} } @article{SchellerSchmid2020, author = {Scheller, Frieder W. and Schmid, Rolf}, title = {A tribute to Isao Karube (1942-2020) and his influence on sensor science}, series = {Analytical and bioanalytical chemistry : a merger of Fresenius' journal of analytical chemistry, Analusis and Quimica analitica}, volume = {412}, journal = {Analytical and bioanalytical chemistry : a merger of Fresenius' journal of analytical chemistry, Analusis and Quimica analitica}, number = {28}, publisher = {Springer}, address = {Berlin}, issn = {1618-2642}, doi = {10.1007/s00216-020-02946-5}, pages = {7709 -- 7711}, year = {2020}, language = {en} } @article{BeissenhirtzSchellerLisdat2004, author = {Beissenhirtz, Moritz Karl and Scheller, Frieder W. and Lisdat, Fred}, title = {A superoxide sensor based on a multilayer cytochrome c electrode}, issn = {0003-2700}, year = {2004}, abstract = {A novel multilayer cytochrome c electrode for the quantification of superoxide radical concentrations is introduced. The electrode consists of alternating layers of cytochrome c and poly(aniline(sulfonic acid)) on a gold wire electrode. The formation of multilayer structures was proven by SPR experiments. Assemblies with 2-15 protein layers showed electrochemical communication with the gold electrode. For every additional layer, a substantial increase in electrochemically active cytochrome c (cyt. c) was found. For electrodes of more than 10 layers, the increase was more than 1 order of magnitude as compared to monolayer electrode systems. Thermodynamic and kinetic parameters of the electrodes were characterized. The mechanism of electron transfer within the multilayer assembly was studied, with results suggesting a protein-protein electron-transfer model. Electrodes of 2-15 layers were applied to the in vitro quantification of enzymatically generated superoxide, showing superior sensitivity as compared to a monolayer-based sensor. An electrode with 6 cyt. c/PASA layers showed the highest sensitivity of the systems studied, giving an increase in sensitivity of half an order of magnitude versus the that of the monolayer electrode. The stability of the system was optimized using thermal treatment, resulting in no loss in sensor signal or protein loading after 10 successive measurements or 2 days of storage}, language = {en} } @article{BierEhrentreichFoersterDoellingetal.1997, author = {Bier, Frank Fabian and Ehrentreich-F{\"o}rster, Eva and D{\"o}lling, R. and Eremenko, A. V. and Scheller, Frieder W.}, title = {A redox-label immunosensor on basis of a bi-enzyme electrode}, year = {1997}, language = {en} } @article{GajovicHabermuellerWarsinkeetal.1999, author = {Gajovic, Nenad and Haberm{\"u}ller, K. and Warsinke, Axel and Schuhmann, W. and Scheller, Frieder W.}, title = {A pyruvate oxidase electrode based on an electrochemically deposited redox polymer}, year = {1999}, language = {en} } @article{TellerHalamekMakoweretal.2006, author = {Teller, C. and Halamek, Jan and Makower, Alexander and Fournier, Didier and Schulze, H. and Scheller, Frieder W.}, title = {A piezoelectric sensor with propidium as a recognition element for cholinesterases}, doi = {10.1016/j.snb.2005.02.053}, year = {2006}, abstract = {A piezoelectric biosensor has been developed on the basis of the reversible acetylcholinesterase (AChE) inhibitor propidium. The propidium cation was bound to a 11-mercaptoundecanoic acid monolayer on gold-coated quartz crystals. The immobilization was done via activation of carboxyl groups by 1,3-dicyclohexylcarbodiimide (DCC). Different types of cholinesterases (acetyl- and butyryl-ChE) from different origins were tested for their binding ability towards the immobilized propidium. Binding Studies were performed in a flow system, Furthermore, catalytically active and organophosphate-inhibited enzyme were compared re-aiding their binding capability. The binding constants were derived by using an one to one binding model and a refined model also including rebinding effects. It was shown that organophosphorylation of the active site hardly influences the affinity of AChE towards propidium. Furthermore the propidium-based biosensor provides equal sensitivity as compared with piezolelectric sensors with immobilized paraoxon- an active site ligand of AChE. (c) 2005 Elsevier B.V. All rights reserved}, language = {en} } @article{GajovicWarsinkeScheller1995, author = {Gajovic, Nenad and Warsinke, Axel and Scheller, Frieder W.}, title = {A novel multienzyme electrode for the determination of citrate}, year = {1995}, language = {en} } @article{SongBierScheller1995, author = {Song, Min Ik and Bier, Frank Fabian and Scheller, Frieder W.}, title = {A method to detect superoxide radicals using teflon membrane and superoxide dismutase}, year = {1995}, language = {en} } @article{ChenWarsinkeGajovicetal.2000, author = {Chen, Ziping and Warsinke, Axel and Gajovic, Nenad and Große, St. and Hu, J. and Kleber, H.-P. and Scheller, Frieder W.}, title = {A D-carnitine dehydrogenase electrode for the assessment of enantiomeric purity of L-carnitine preparations}, year = {2000}, language = {en} } @article{LettauWarsinkeKatterleetal.2006, author = {Lettau, Kristian and Warsinke, Axel and Katterle, Martin and Danielsson, Bengt and Scheller, Frieder W.}, title = {A bifunctional molecularly imprinted polymer (MIP): analysis of binding and catalysis by a thermistor}, doi = {10.1002/anie.200601796}, year = {2006}, abstract = {Binding or catalysis? Both can be distinguished with a molecularly imprinted polymer (MIP) by the different patterns of heat generation. The catalytically active sites, like in the corresponding enzyme, generate a steady-state temperature increase. Thus, enzyme-like catalysis and antibody-analogue binding are analyzed simultaneously in a bifunctional MIP for the first time (see scheme).}, language = {en} } @article{EremenkoMakowerBaueretal.1997, author = {Eremenko, A. V. and Makower, Alexander and Bauer, Christian G. and Kurochkin, I. N. and Scheller, Frieder W.}, title = {A bienzyme electrode for tyrosine containing peptides determination}, year = {1997}, language = {en} } @article{GajovicWarsinkeScheller1998, author = {Gajovic, Nenad and Warsinke, Axel and Scheller, Frieder W.}, title = {A bienzyme electrode for L-malate based on a novel and general design}, year = {1998}, language = {en} } @article{HuangWarsinkeKoroljovaSkorobogatkoetal.1999, author = {Huang, T. and Warsinke, Axel and Koroljova-Skorobogatko, O. V. and Makower, Alexander and Kuwana, T. and Scheller, Frieder W.}, title = {A bienzyme carbon paste electrode for the sensitive detection of NADPH and the measurement of glucose-6- phosphate dehydrogenase}, year = {1999}, language = {en} } @article{ZhangCasertaYarmanetal.2021, author = {Zhang, Xiaorong and Caserta, Giorgio and Yarman, Aysu and Supala, Eszter and Tadjoung Waffo, Armel Franklin and Wollenberger, Ulla and Gyurcsanyi, Robert E. and Zebger, Ingo and Scheller, Frieder W.}, title = {"Out of Pocket" protein binding}, series = {Chemosensors}, volume = {9}, journal = {Chemosensors}, number = {6}, publisher = {MDPI}, address = {Basel}, issn = {2227-9040}, doi = {10.3390/chemosensors9060128}, pages = {13}, year = {2021}, abstract = {The epitope imprinting approach applies exposed peptides as templates to synthesize Molecularly Imprinted Polymers (MIPs) for the recognition of the parent protein. While generally the template protein binding to such MIPs is considered to occur via the epitope-shaped cavities, unspecific interactions of the analyte with non-imprinted polymer as well as the detection method used may add to the complexity and interpretation of the target rebinding. To get new insights on the effects governing the rebinding of analytes, we electrosynthesized two epitope-imprinted polymers using the N-terminal pentapeptide VHLTP-amide of human hemoglobin (HbA) as the template. MIPs were prepared either by single-step electrosynthesis of scopoletin/pentapeptide mixtures or electropolymerization was performed after chemisorption of the cysteine extended VHLTP peptide. Rebinding of the target peptide and the parent HbA protein to the MIP nanofilms was quantified by square wave voltammetry using a redox probe gating, surface enhanced infrared absorption spectroscopy, and atomic force microscopy. While binding of the pentapeptide shows large influence of the amino acid sequence, all three methods revealed strong non-specific binding of HbA to both polyscopoletin-based MIPs with even higher affinities than the target peptides.}, language = {en} }