@misc{ErdossyHorvathYarmanetal.2016,
  author    = {Erdossy, Julia and Horvath, Viola and Yarman, Aysu and Scheller, Frieder W. and Gyurcsanyi, Robert E.},
  title     = {Electrosynthesized molecularly imprinted polymers for protein recognition},
  series = {Trends in Analytical Chemistry},
  volume    = {79},
  journal   = {Trends in Analytical Chemistry},
  publisher = {Elsevier},
  address   = {Oxford},
  issn      = {0165-9936},
  doi       = {10.1016/j.trac.2015.12.018},
  pages     = {179 -- 190},
  year      = {2016},
  abstract  = {Molecularly imprinted polymers (MIPs) for the recognition of proteins are expected to possess high affinity through the establishment of multiple interactions between the polymer matrix and the large number of functional groups of the target. However, while highly affine recognition sites need building blocks rich in complementary functionalities to their target, such units are likely to generate high levels of nonspecific binding. This paradox, that nature solved by evolution for biological receptors, needs to be addressed by the implementation of new concepts in molecular imprinting of proteins. Additionally, the structural variability, large size and incompatibility with a range of monomers made the development of protein MIPs to take a slow start. While the majority of MIP preparation methods are variants of chemical polymerization, the polymerization of electroactive functional monomers emerged as a particularly advantageous approach for chemical sensing application. Electropolymerization can be performed from aqueous solutions to preserve the natural conformation of the protein templates, with high spatial resolution and electrochemical control of the polymerization process. This review compiles the latest results, identifying major trends and providing an outlook on the perspectives of electrosynthesised protein-imprinted MIPs for chemical sensing. (C) 2016 Elsevier B.V. All rights reserved.},
  language  = {en}
}
@article{YarmanScheller2016,
  author    = {Yarman, Aysu and Scheller, Frieder W.},
  title     = {MIP-esterase/Tyrosinase Combinations for Paracetamol and Phenacetin},
  series = {Electroanalysis : an international journal devoted to fundamental and practical aspects of electroanalysis},
  volume    = {28},
  journal   = {Electroanalysis : an international journal devoted to fundamental and practical aspects of electroanalysis},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {1040-0397},
  doi       = {10.1002/elan.201600042},
  pages     = {2222 -- 2227},
  year      = {2016},
  abstract  = {A new electrochemical MIP sensor for the most frequently used drug paracetamol (PAR) was prepared by electropolymerization of mixtures containing the template molecule and the functional monomers ophenylenediamine, resorcinol and aniline. The imprinting factor of 12 reflects the effective target binding to the MIP as compared with the non-imprinted electropolymer. Combination of the MIP with a nonspecific esterase allows the measurement of phenacetin - another analgesic drug. In the second approach the PAR containing sample solution was pretreated with tyrosinase in order to prevent electrochemical interferences by ascorbic acid and uric acid. Interference-free indication at a very low electrode potential without fouling of the electrode surface was achieved with the o-phenylenediamine: resorcinol-based MIP.},
  language  = {en}
}
@misc{SchellerSakarDasdan2016,
  author    = {Scheller, Frieder W. and Sakar Dasdan, Dolunay},
  title     = {Selected papers presented on the 2nd International Conference on the New Trends in Chemistry, Zagreb, Croatia, April 19-22, 2016 Preface},
  series = {Bulgarian chemical communications : journal of the Chemical Institutes of the Bulgarian Academy of Sciences and of the Bulgarian Chemical Society = Izvestija po chimija},
  volume    = {48},
  journal   = {Bulgarian chemical communications : journal of the Chemical Institutes of the Bulgarian Academy of Sciences and of the Bulgarian Chemical Society = Izvestija po chimija},
  publisher = {Bulgarian Academy of Sciences},
  address   = {Sofia},
  issn      = {0324-1130},
  pages     = {4 -- 4},
  year      = {2016},
  language  = {en}
}
@article{LoewBogdanoffHerrmannetal.2006,
  author    = {Loew, Noya and Bogdanoff, Peter and Herrmann, Iris and Wollenberger, Ursula and Scheller, Frieder W. and Katterle, Martin},
  title     = {Influence of modifications on the efficiency of pyrolysed CoTMPP as electrode material for horseradish peroxidase and the reduction of hydrogen peroxide},
  series = {Electroanalysis : an international journal devoted to fundamental and practical aspects of electroanalysis},
  volume    = {18},
  journal   = {Electroanalysis : an international journal devoted to fundamental and practical aspects of electroanalysis},
  number    = {23},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {1040-0397},
  doi       = {10.1002/elan.200603664},
  pages     = {2324 -- 2330},
  year      = {2006},
  abstract  = {A tailor-made horseradish peroxidase (HRP) bulk composite electrode was developed on the basis of pyrolyzed cobalt tetramethoxyphenylporphyrin (CoTMPP) by modifying pore size and surface area of the porous carbon material through varying amounts of iron oxalate and sulfur prior to pyrolyzation. The materials were used to immobilize horseradish peroxidase (HRP). These electrodes were characterized in terms of their efficiency to reduce hydrogen peroxide. The heterogeneous electron transfer rate constants of different materials were determined with the rotating disk electrode method and a k(S) (401 +/- 61 s(-1)) exceeding previously reported values for native HRP was found.},
  language  = {en}
}
@misc{YarmanDechtriratBosserdtetal.2015,
  author    = {Yarman, Aysu and Dechtrirat, Decha and Bosserdt, Maria and Jetzschmann, Katharina J. and Gajovic-Eichelmann, Nenad and Scheller, Frieder W.},
  title     = {Cytochrome c-derived hybrid systems based on moleculary imprinted polymers},
  series = {Electroanalysis : an international journal devoted to fundamental and practical aspects of electroanalysis},
  volume    = {27},
  journal   = {Electroanalysis : an international journal devoted to fundamental and practical aspects of electroanalysis},
  number    = {3},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {1040-0397},
  doi       = {10.1002/elan.201400592},
  pages     = {573 -- 586},
  year      = {2015},
  abstract  = {Hybrid architectures which combine a MIP with an immobilized affinity ligand or a biocatalyst sum up the advantages of both components. In this paper, hybrid architectures combining a layer of a molecularly imprinted electropolymer with a mini-enzyme or a self-assembled monolayer will be presented. (i) Microperoxidase-11 (MP-11) catalyzed oxidation of the drug aminopyrine on a product-imprinted sublayer: The peroxide dependent conversion of the analyte aminopyrine takes place in the MP-11 containing layer on top of a product-imprinted electropolymer on the indicator electrode. The hierarchical architecture resulted in the elimination of interfering signals for ascorbic acid and uric acid. An advantage of the new hierarchical structure is the separation of MIP formation by electropolymerization and immobilization of the catalyst. In this way it was for the first time possible to integrate an enzyme with a MIP layer in a sensor configuration. This combination has the potential to be transferred to other enzymes, e.g. P450, opening the way to clinically important analytes. (ii) Epitope-imprinted poly-scopoletin layer for binding of the C-terminal peptide and cytochrome c (Cyt c): The MIP binds both the target peptide and the parent protein almost eight times stronger than the non-imprinted polymer with affinities in the lower micromolar range. Exchange of only one amino acid in the peptide decreases the binding by a factor of five. (iii) MUA-poly-scopoletin MIP for cytochrome c: Cyt c bound to the MIP covered gold electrode exhibits direct electron transfer with a redox potential and rate constant typical for the native protein. The MIP cover layer suppresses the displacement of the target protein by BSA or myoglobin. The combination of protein imprinted polymers with an efficient electron transfer is a new concept for characterizing electroactive proteins such as Cyt c. The competition with other proteins shows that the MIP binds its target Cyt c preferentially and that molecular shape and the charge of protein determine the binding of interfering proteins.},
  language  = {en}
}
@article{StoellnerStoeckleinSchelleretal.2002,
  author    = {St{\"o}llner, Daniela and St{\"o}cklein, Walter F. M. and Scheller, Frieder W. and Warsinke, Axel},
  title     = {Membrane-immobilized haptoglobin as affinity matrix for a hemoglobin-A1c-immunosensor},
  year      = {2002},
  language  = {en}
}
@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{RosePfeifferSchelleretal.2001,
  author    = {Rose, Andreas and Pfeiffer, Dorothea and Scheller, Frieder W. and Wollenberger, Ursula},
  title     = {Quinoprotein glucose dehydrogenasemodified thick-film electrodes for the amperometric detection of phenolic compounds in flow injection analysis},
  year      = {2001},
  language  = {en}
}
@article{SchellerWollenbergerWarsinkeetal.2001,
  author    = {Scheller, Frieder W. and Wollenberger, Ursula and Warsinke, Axel and Lisdat, Fred},
  title     = {Research and development in biosensors},
  year      = {2001},
  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{HockScheller2001,
  author    = {Hock, Bertold and Scheller, Frieder W.},
  title     = {Conclusions and outlook},
  year      = {2001},
  language  = {en}
}
@article{IgnatovGeSchelleretal.2001,
  author    = {Ignatov, S. and Ge, Bixia and Scheller, Frieder W. and Lisdat, Fred},
  title     = {Detection of the antioxidant activity detection of flavonoids by using superoxide sensor},
  isbn      = {1-58603-164-3},
  year      = {2001},
  language  = {en}
}
@article{LehmannWollenbergerBrigeliusFloheetal.2001,
  author    = {Lehmann, Claudia and Wollenberger, Ursula and Brigelius-Floh{\´e}, Regina and Scheller, Frieder W.},
  title     = {Modified gold electrodes for electrochemical studies of the reaction phospholipid hydroperoxide glutathione peroxidas with glutathione and glutathione disulfide},
  year      = {2001},
  language  = {en}
}
@article{LisdatGeMeyerhoffetal.2001,
  author    = {Lisdat, Fred and Ge, Bixia and Meyerhoff, M. E. and Scheller, Frieder W.},
  title     = {Signal chains with cytochromes at SAM modified gold electrodes},
  year      = {2001},
  language  = {en}
}
@article{LisdatGeKrauseetal.2001,
  author    = {Lisdat, Fred and Ge, Bixia and Krause, B. and Ehrlich, A. and Bienert, H. and Scheller, Frieder W.},
  title     = {Nucleic acid-promoted electron transfer to cytochrome c},
  year      = {2001},
  language  = {en}
}
@article{Scheller2001,
  author    = {Scheller, Frieder W.},
  title     = {Biosensoren auf dem Weg zur Biochip-Technologie},
  year      = {2001},
  language  = {de}
}
@article{Scheller2001,
  author    = {Scheller, Frieder W.},
  title     = {Biomolek{\"u}le als Reporter in der Analytik : keine Forschung im Elfenbeinturm},
  year      = {2001},
  language  = {de}
}
@article{LisdatScheller2000,
  author    = {Lisdat, Fred and Scheller, Frieder W.},
  title     = {Technical principles. Electrodes},
  isbn      = {90-5702-447-7},
  year      = {2000},
  language  = {en}
}
@article{SchellerPfeiffer2000,
  author    = {Scheller, Frieder W. and Pfeiffer, Dorothea},
  title     = {Biosensor-Technologie in der Medizin und den Biowissenschaften},
  year      = {2000},
  language  = {de}
}
@article{FridmanWollenbergerBogdanovskayaetal.2000,
  author    = {Fridman, Vadim and Wollenberger, Ursula and Bogdanovskaya, V. A. and Lisdat, Fred and Ruzgas, T. and Lindgren, A. and Gorton, Lo and Scheller, Frieder W.},
  title     = {Electrochemical investigation of cellobiose oxidation by cellobiose dehydrogenase in the presence of cytochrome c as mediator},
  year      = {2000},
  language  = {en}
}
@article{MakowerBarminScheller2000,
  author    = {Makower, Alexander and Barmin, Anatoli V. and Scheller, Frieder W.},
  title     = {Eine neue Methode zur hochempfindlichen Analyse von Pestiziden},
  year      = {2000},
  language  = {de}
}
@article{WarsinkeBenkertScheller2000,
  author    = {Warsinke, Axel and Benkert, Alexander and Scheller, Frieder W.},
  title     = {Electrochemical immunoassays},
  year      = {2000},
  language  = {en}
}
@article{GajovicBinyaminWarsinkeetal.2000,
  author    = {Gajovic, Nenad and Binyamin, Gary and Warsinke, Axel and Scheller, Frieder W. and Heller, A.},
  title     = {Operation of a miniature redox hydrogel-based pyruvate sensor in undiluted deoxygenated calf serum},
  year      = {2000},
  language  = {en}
}
@article{LeiWollenbergerScheller2000,
  author    = {Lei, Chenghong and Wollenberger, Ursula and Scheller, Frieder W.},
  title     = {Clay based direct electrochemistry of myoglobin},
  year      = {2000},
  language  = {en}
}
@article{LeiWollenbergerJungetal.2000,
  author    = {Lei, Chenghong and Wollenberger, Ursula and Jung, Christiane and Scheller, Frieder W.},
  title     = {Clay-bridged electron transfer between cytochrome P450(cam) and electrode},
  year      = {2000},
  language  = {en}
}
@article{LisdatScheller2000,
  author    = {Lisdat, Fred and Scheller, Frieder W.},
  title     = {Principles of sensorial radical detection - a minireview},
  year      = {2000},
  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{Scheller2000,
  author    = {Scheller, Frieder W.},
  title     = {Biomolekulare Erkennungssysteme f{\"u}r die Biochemische Analytik},
  year      = {2000},
  language  = {de}
}
@article{Scheller2000,
  author    = {Scheller, Frieder W.},
  title     = {Biosensor-Stabilit{\"a}t},
  year      = {2000},
  language  = {de}
}
@article{LisdatGeStoeckleinetal.2000,
  author    = {Lisdat, Fred and Ge, Bixia and St{\"o}cklein, Walter F. M. and Scheller, Frieder W. and Meyer, T.},
  title     = {Electrochemical behaviour and nitric oxides interaction of immobilised cytochrome c from Rhodocyclus gelatinosus},
  year      = {2000},
  language  = {en}
}
@article{ChenWollenbergerLisdatetal.2000,
  author    = {Chen, Jian and Wollenberger, Ursula and Lisdat, Fred and Ge, Bixia and Scheller, Frieder W.},
  title     = {Superoxide sensor based on hemin modified electrode},
  year      = {2000},
  language  = {en}
}
@article{JuLiuGeetal.2000,
  author    = {Ju, Huangxian and Liu, Songqin and Ge, Bixia and Lisdat, Fred and Scheller, Frieder W.},
  title     = {Electrochemistry of cytochrome c immobilized on colloidal gold modified carbon paste electrodes and its electrocatalytic activity},
  year      = {2000},
  language  = {en}
}
@article{StoeckleinRohdeScharteetal.2000,
  author    = {St{\"o}cklein, Walter F. M. and Rohde, M. and Scharte, Gudrun and Behrsing, Olaf and Warsinke, Axel and Micheel, Burkhard and Scheller, Frieder W.},
  title     = {Sensitive detection of triazine and phenylurea pesticides in pure organic solvent by enzyme linked immunsorbent assay (ELISA): stabilities, solubilities and sensitives},
  year      = {2000},
  language  = {en}
}
@article{Scheller1999,
  author    = {Scheller, Frieder W.},
  title     = {Deutliche Signale setzen [Leitartikel]},
  year      = {1999},
  language  = {de}
}
@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{LisdatGeScheller1999,
  author    = {Lisdat, Fred and Ge, Bixia and Scheller, Frieder W.},
  title     = {Oligonucleotide-modified electrodes for fast electron transfer to cytochrome c},
  year      = {1999},
  language  = {en}
}
@article{LisdatGeEhrentreichFoersteretal.1999,
  author    = {Lisdat, Fred and Ge, Bixia and Ehrentreich-F{\"o}rster, Eva and Reszka, R. and Scheller, Frieder W.},
  title     = {SOD activity measurement using cytochrome c modified electrode},
  year      = {1999},
  language  = {en}
}
@article{GajovicWarsinkeHuangetal.1999,
  author    = {Gajovic, Nenad and Warsinke, Axel and Huang, T. and Schulmeister, Thomas and Scheller, Frieder W.},
  title     = {Characterization and mathematical modelling of a novel bienzyme electrode for L-malate with cofactor recycling},
  year      = {1999},
  language  = {en}
}
@article{BauerKuehnGajovicetal.1999,
  author    = {Bauer, Christian G. and K{\"u}hn, A. and Gajovic, Nenad and Skorobogatko, O. V. and Holt, P. J. and Bruce, N. C. and Makower, Alexander and Lowe, Ch. R. and Scheller, Frieder W.},
  title     = {New enzymen sensors for morphine and codeine based on morphine dehydrogenase and laccase},
  year      = {1999},
  language  = {en}
}
@article{KleinjungEhrentreichFoersterScheller1999,
  author    = {Kleinjung, Frank and Ehrentreich-F{\"o}rster, Eva and Scheller, Frieder W.},
  title     = {Changing functionality of surfaces by directed self-assembly using oligonucleotides - the oligo-tag},
  year      = {1999},
  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{SchellerJinEhrentreichFoersteretal.1999,
  author    = {Scheller, Frieder W. and Jin, Wen and Ehrentreich-F{\"o}rster, Eva and Ge, Bixia and Lisdat, Fred and B{\"u}ttemeyer, R. and Wollenberger, Ursula},
  title     = {Cytochrome c based superoxide sensor for in vivo application},
  year      = {1999},
  language  = {en}
}
@article{LeiLisdatWollenbergeretal.1999,
  author    = {Lei, Chenghong and Lisdat, Fred and Wollenberger, Ursula and Scheller, Frieder W.},
  title     = {Cytochrome c : Clay-modified electrode},
  year      = {1999},
  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{StojanovicErdossyKeltaietal.2017,
  author    = {Stojanovic, Zorica and Erdossy, Julia and Keltai, Katalin and Scheller, Frieder W. and Gyurcsanyi, Robert E.},
  title     = {Electrosynthesized molecularly imprinted polyscopoletin nanofilms for human serum albumin detection},
  series = {Analytica chimica acta : an international journal devoted to all branches of analytical chemistry},
  volume    = {977},
  journal   = {Analytica chimica acta : an international journal devoted to all branches of analytical chemistry},
  publisher = {Elsevier},
  address   = {Amsterdam},
  issn      = {0003-2670},
  doi       = {10.1016/j.aca.2017.04.043},
  pages     = {1 -- 9},
  year      = {2017},
  abstract  = {Molecularly imprinted polymers (MIPs) rendered selective solely by the imprinting with protein templates lacking of distinctive properties to facilitate strong target-MIP interaction are likely to exhibit medium to low template binding affinities. While this prohibits the use of such MIPs for applications requiring the assessment of very low template concentrations, their implementation for the quantification of high-abundance proteins seems to have a clear niche in the analytical practice. We investigated this opportunity by developing a polyscopoletin-based MIP nanofilm for the electrochemical determination of elevated human serum albumin (HSA) in urine. As reference for a low abundance protein ferritin-MIPs were also prepared by the same procedure. Under optimal conditions, the imprinted sensors gave a linear response to HSA in the concentration range of 20-100 mg/dm(3), and to ferritin in the range of 120-360 mg/dm(3). While as expected the obtained limit of detection was not sufficient to determine endogenous ferritin in plasma, the HSA-sensor was successfully employed to analyse urine samples of patients with albuminuria. The results suggest that MIP-based sensors may be applicable for quantifying high abundance proteins in a clinical setting. (c) 2017 Elsevier B.V. All rights reserved.},
  language  = {en}
}
@article{BognarSupalaYarmanetal.2022,
  author    = {Bogn{\´a}r, Zs{\´o}fia and Supala, Eszter and Yarman, Aysu and Zhang, Xiaorong and Bier, Frank Fabian and Scheller, Frieder W. and Gyurcsanyi, R{\´o}bert E.},
  title     = {Peptide epitope-imprinted polymer microarrays for selective protein recognition},
  series = {Chemical science / RSC, Royal Society of Chemistry},
  volume    = {13},
  journal   = {Chemical science / RSC, Royal Society of Chemistry},
  number    = {5},
  publisher = {Royal Society of Chemistry},
  address   = {Cambridge},
  issn      = {2041-6539},
  doi       = {10.1039/d1sc04502d},
  pages     = {1263 -- 1269},
  year      = {2022},
  abstract  = {We introduce a practically generic approach for the generation of epitope-imprinted polymer-based microarrays for protein recognition on surface plasmon resonance imaging (SPRi) chips. The SPRi platform allows the subsequent rapid screening of target binding kinetics in a multiplexed and label-free manner. The versatility of such microarrays, both as synthetic and screening platform, is demonstrated through developing highly affine molecularly imprinted polymers (MIPs) for the recognition of the receptor binding domain (RBD) of SARS-CoV-2 spike protein. A characteristic nonapeptide GFNCYFPLQ from the RBD and other control peptides were microspotted onto gold SPRi chips followed by the electrosynthesis of a polyscopoletin nanofilm to generate in one step MIP arrays. A single chip screening of essential synthesis parameters, including the surface density of the template peptide and its sequence led to MIPs with dissociation constants (K-D) in the lower nanomolar range for RBD, which exceeds the affinity of RBD for its natural target, angiotensin-convertase 2 enzyme. Remarkably, the same MIPs bound SARS-CoV-2 virus like particles with even higher affinity along with excellent discrimination of influenza A (H3N2) virus. While MIPs prepared with a truncated heptapeptide template GFNCYFP showed only a slightly decreased affinity for RBD, a single mismatch in the amino acid sequence of the template, i.e. the substitution of the central cysteine with a serine, fully suppressed the RBD binding.},
  language  = {en}
}
@article{TanneJeoungPengetal.2015,
  author    = {Tanne, Johannes and Jeoung, Jae-Hun and Peng, Lei and Yarman, Aysu and Dietzel, Birgit and Schulz, Burkhard and Schad, Daniel and Dobbek, Holger and Wollenberger, Ursula and Bier, Frank Fabian and Scheller, Frieder W.},
  title     = {Direct Electron Transfer and Bioelectrocatalysis by a Hexameric, Heme Protein at Nanostructured Electrodes},
  series = {Electroanalysis : an international journal devoted to fundamental and practical aspects of electroanalysis},
  volume    = {27},
  journal   = {Electroanalysis : an international journal devoted to fundamental and practical aspects of electroanalysis},
  number    = {10},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {1040-0397},
  doi       = {10.1002/elan.201500231},
  pages     = {2262 -- 2267},
  year      = {2015},
  abstract  = {A nanohybrid consisting of poly(3-aminobenzenesulfonic acid-co-aniline) and multiwalled carbon nanotubes [MWCNT-P(ABS-A)]) on a gold electrode was used to immobilize the hexameric tyrosine-coordinated heme protein (HTHP). The enzyme showed direct electron transfer between the heme group of the protein and the nanostructured surface. Desorption of the noncovalently bound heme from the protein could be excluded by control measurements with adsorbed hemin on aminohexanthiol-modified electrodes. The nanostructuring and the optimised charge characteristics resulted in a higher protein coverage as compared with MUA/MU modified electrodes. The adsorbed enzyme shows catalytic activity for the cathodic H2O2 reduction and oxidation of NADH.},
  language  = {en}
}
@article{SchellerKleinjungBieretal.1998,
  author    = {Scheller, Frieder W. and Kleinjung, Frank and Bier, Frank Fabian and Markower, Alexander and Neumann, Barbara and Wollenberger, Ursula and Kurochkin, Iliya N. and Eremenko, Arkadi V. and Barmin, Anatoli V. and Klußmann, Sven and F{\"u}rste, Jens-Peter and Erdmann, Volker A. and Mansuy, D.},
  title     = {New recognition elements in biosensing},
  year      = {1998},
  language  = {en}
}
@article{YarmanKurbanoğluZebgeretal.2021,
  author    = {Yarman, Aysu and Kurbanoğlu, Sevin{\c{c}} and Zebger, Ingo and Scheller, Frieder W.},
  title     = {Simple and robust},
  series = {Sensors and actuators : B, Chemical : an international journal devoted to research and development of chemical transducers},
  volume    = {330},
  journal   = {Sensors and actuators : B, Chemical : an international journal devoted to research and development of chemical transducers},
  publisher = {Elsevier Science},
  address   = {Amsterdam [u.a.]},
  issn      = {0925-4005},
  doi       = {10.1016/j.snb.2020.129369},
  pages     = {12},
  year      = {2021},
  abstract  = {A spectrum of 7562 publications on Molecularly Imprinted Polymers (MIPs) has been presented in literature within the last ten years (Scopus, September 7, 2020). Around 10 \% of the papers published on MIPs describe the recognition of proteins. The straightforward synthesis of MIPs is a significant advantage as compared with the preparation of enzymes or antibodies. MIPs have been synthesized from only one up to six functional monomers while proteins are made up of 20 natural amino acids. Furthermore, they can be synthesized against structures of low immunogenicity and allow multi-analyte measurements via multi-target synthesis. Electrochemical methods allow simple polymer synthesis, removal of the template and readout. Among the different sensor configurations electrochemical MIP-sensors provide the broadest spectrum of protein analytes. The sensitivity of MIP-sensors is sufficiently high for biomarkers in the sub-nanomolar region, nevertheless the cross-reactivity of highly abundant proteins in human serum is still a challenge. MIPs for proteins offer innovative tools not only for clinical and environmental analysis, but also for bioimaging, therapy and protein engineering.},
  language  = {en}
}
@article{CasertaZhangYarmanetal.2021,
  author    = {Caserta, Giorgio and Zhang, Xiaorong and Yarman, Aysu and Supala, Eszter and Wollenberger, Ulla and Gyurcs{\´a}nyi, R{\´o}bert E. and Zebger, Ingo and Scheller, Frieder W.},
  title     = {Insights in electrosynthesis, target binding, and stability of peptide-imprinted polymer nanofilms},
  series = {Electrochimica acta : the journal of the International Society of Electrochemistry (ISE)},
  volume    = {381},
  journal   = {Electrochimica acta : the journal of the International Society of Electrochemistry (ISE)},
  publisher = {Elsevier},
  address   = {New York, NY [u.a.]},
  issn      = {0013-4686},
  doi       = {10.1016/j.electacta.2021.138236},
  pages     = {8},
  year      = {2021},
  abstract  = {Molecularly imprinted polymer (MIP) nanofilms have been successfully implemented for the recognition of different target molecules: however, the underlying mechanistic details remained vague. This paper provides new insights in the preparation and binding mechanism of electrosynthesized peptide-imprinted polymer nanofilms for selective recognition of the terminal pentapeptides of the beta-chains of human adult hemoglobin, HbA, and its glycated form HbA1c. To differentiate between peptides differing solely in a glucose adduct MIP nanofilms were prepared by a two-step hierarchical electrosynthesis that involves first the chemisorption of a cysteinyl derivative of the pentapeptide followed by electropolymerization of scopoletin. This approach was compared with a random single-step electrosynthesis using scopo-letin/pentapeptide mixtures. Electrochemical monitoring of the peptide binding to the MIP nanofilms by means of redox probe gating revealed a superior affinity of the hierarchical approach with a Kd value of 64.6 nM towards the related target. Changes in the electrosynthesized non-imprinted polymer and MIP nanofilms during chemical, electrochemical template removal and rebinding were substantiated in situ by monitoring the characteristic bands of both target peptides and polymer with surface enhanced infrared absorption spectroscopy. This rational approach led to MIPs with excellent selectivity and provided key mechanistic insights with respect to electrosynthesis, rebinding and stability of the formed MIPs.},
  language  = {en}
}
@article{WollenbergerSchubertPfeifferetal.1996,
  author    = {Wollenberger, Ursula and Schubert, Florian and Pfeiffer, Dorothea and Scheller, Frieder W.},
  title     = {Recycling sensors based on kinases : proceedings of Mosbach Symposion on Biochemical Technology},
  year      = {1996},
  language  = {en}
}
@article{SchellerWollenbergerPfeifferetal.1996,
  author    = {Scheller, Frieder W. and Wollenberger, Ursula and Pfeiffer, Dorothea and Schubert, Florian},
  title     = {Overview of biosensor technology : proceedings of Mosbach Symposion on Biochemical Technology},
  year      = {1996},
  language  = {en}
}
@article{SchellerSchubertBier1995,
  author    = {Scheller, Frieder W. and Schubert, Florian and Bier, Frank Fabian},
  title     = {Vom Biosensor zur Nanobiotechnologie},
  year      = {1995},
  language  = {de}
}
@article{SchellerWollenbergerSchubertetal.1993,
  author    = {Scheller, Frieder W. and Wollenberger, Ursula and Schubert, Florian and Pfeiffer, Dorothea and Markower, Alexander and McNeil, C. J.},
  title     = {Multienzyme biosensors : coupled enzyme reactions and enzyme activation},
  year      = {1993},
  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{SchellerKirsteinSchubertetal.1993,
  author    = {Scheller, Frieder W. and Kirstein, Dieter and Schubert, Florian and Pfeiffer, Dorothea and McNeil, C. J.},
  title     = {Enzymes in electrochemical biosensors},
  year      = {1993},
  language  = {en}
}
@article{SchellerPfeifferSchubertetal.1995,
  author    = {Scheller, Frieder W. and Pfeiffer, Dorothea and Schubert, Florian and Wollenberger, Ursula},
  title     = {Enzyme - based electrodes},
  year      = {1995},
  language  = {en}
}
@article{WollenbergerSchubertPfeifferetal.1993,
  author    = {Wollenberger, Ursula and Schubert, Florian and Pfeiffer, Dorothea and Scheller, Frieder W.},
  title     = {Enhancing biosensor performance using multienzyme systems},
  year      = {1993},
  language  = {en}
}
@misc{PengYarmanJetzschmannetal.2017,
  author    = {Peng, Lei and Yarman, Aysu and Jetzschmann, Katharina J. and Jeoung, Jae-Hun and Schad, Daniel and Dobbek, Holger and Wollenberger, Ursula and Scheller, Frieder W.},
  title     = {Molecularly imprinted electropolymer for a hexameric heme protein with direct electron transfer and peroxide electrocatalysis},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus4-400627},
  pages     = {11},
  year      = {2017},
  abstract  = {For the first time a molecularly imprinted polymer (MIP) with direct electron transfer (DET) and bioelectrocatalytic activity of the target protein is presented. Thin films of MIPs for the recognition of a hexameric tyrosine-coordinated heme protein (HTHP) have been prepared by electropolymerization of scopoletin after oriented assembly of HTHP on a self-assembled monolayer (SAM) of mercaptoundecanoic acid (MUA) on gold electrodes. Cavities which should resemble the shape and size of HTHP were formed by template removal. Rebinding of the target protein sums up the recognition by non-covalent interactions between the protein and the MIP with the electrostatic attraction of the protein by the SAM. HTHP bound to the MIP exhibits quasi-reversible DET which is reflected by a pair of well pronounced redox peaks in the cyclic voltammograms (CVs) with a formal potential of -184.4 ± 13.7 mV vs. Ag/AgCl (1 M KCl) at pH 8.0 and it was able to catalyze the cathodic reduction of peroxide. At saturation the MIP films show a 12-fold higher electroactive surface concentration of HTHP than the non-imprinted polymer (NIP).},
  language  = {en}
}
@article{PengYarmanJetzschmannetal.2016,
  author    = {Peng, Lei and Yarman, Aysu and Jetzschmann, Katharina J. and Jeoung, Jae-Hun and Schad, Daniel and Dobbek, Holger and Wollenberger, Ursula and Scheller, Frieder W.},
  title     = {Molecularly Imprinted Electropolymer for a Hexameric Heme Protein with Direct Electron Transfer and Peroxide Electrocatalysis},
  series = {SENSORS},
  volume    = {16},
  journal   = {SENSORS},
  publisher = {MDPI},
  address   = {Basel},
  issn      = {1424-8220},
  doi       = {10.3390/s16030272},
  pages     = {1343 -- 1364},
  year      = {2016},
  abstract  = {For the first time a molecularly imprinted polymer (MIP) with direct electron transfer (DET) and bioelectrocatalytic activity of the target protein is presented. Thin films of MIPs for the recognition of a hexameric tyrosine-coordinated heme protein (HTHP) have been prepared by electropolymerization of scopoletin after oriented assembly of HTHP on a self-assembled monolayer (SAM) of mercaptoundecanoic acid (MUA) on gold electrodes. Cavities which should resemble the shape and size of HTHP were formed by template removal. Rebinding of the target protein sums up the recognition by non-covalent interactions between the protein and the MIP with the electrostatic attraction of the protein by the SAM. HTHP bound to the MIP exhibits quasi-reversible DET which is reflected by a pair of well pronounced redox peaks in the cyclic voltammograms (CVs) with a formal potential of -184.4 +/- 13.7 mV vs. Ag/AgCl (1 M KCl) at pH 8.0 and it was able to catalyze the cathodic reduction of peroxide. At saturation the MIP films show a 12-fold higher electroactive surface concentration of HTHP than the non-imprinted polymer (NIP).},
  language  = {en}
}
@article{TadjoungWaffoYesildagCasertaetal.2018,
  author    = {Tadjoung Waffo, Armel Franklin and Yesildag, Cigdem and Caserta, Giorgio and Katz, Sagie and Zebger, Ingo and Lensen, Marga C. and Wollenberger, Ulla and Scheller, Frieder W. and Altintas, Zeynep},
  title     = {Fully electrochemical MIP sensor for artemisinin},
  series = {Sensors and actuators : B, Chemical},
  volume    = {275},
  journal   = {Sensors and actuators : B, Chemical},
  publisher = {Elsevier},
  address   = {Lausanne},
  issn      = {0925-4005},
  doi       = {10.1016/j.snb.2018.08.018},
  pages     = {163 -- 173},
  year      = {2018},
  abstract  = {This study aims to develop a rapid, sensitive and cost-effective biomimetic electrochemical sensor for artemisinin determination in plant extracts and for pharmacokinetic studies. A novel molecularly imprinted polymer (MIP)based electrochemical sensor was developed by electropolymerization of o-phenylenediamine (o-PD) in the presence of artemisinin on gold wire surface for sensitive detection of artemisinin. The experimental parameters, including selection of functional monomer, polymerization conditions, template extraction after polymerization, influence of pH and buffer were all optimized. Every step of imprinted film synthesis were evaluated by employing voltammetry techniques, surface-enhanced infrared absorption spectroscopy (SEIRAS) and atomic force microscopy (AFM). The specificity was further evaluated by investigating non-specific artemisinin binding on non-imprinted polymer (NIP) surfaces and an imprinting factor of 6.8 was achieved. The artemisinin imprinted polymers using o-PD as functional monomer have provided highly stable and effective binding cavities for artemisinin. Cross-reactivity studies with drug molecules showed that the MIPs are highly specific for artemisinin. The influence of matrix effect was further investigated both in artificial plant matrix and diluted human serum. The results revealed a high affinity of artemisinin-MIP with dissociation constant of 7.3 x 10(-9) M and with a detection limit of 0.01 mu M and 0.02 mu M in buffer and plant matrix, respectively.},
  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}
}
@misc{MengerYarmanErdoessyetal.2016,
  author    = {Menger, Marcus and Yarman, Aysu and Erd{\"o}ssy, J{\´u}lia and Yildiz, Huseyin Bekir and Gyurcs{\´a}nyi, R{\´o}bert E. and Scheller, Frieder W.},
  title     = {MIPs and Aptamers for Recognition of Proteins in Biomimetic Sensing},
  series = {Biosensors : open access journal},
  volume    = {6},
  journal   = {Biosensors : open access journal},
  publisher = {MDPI},
  address   = {Basel},
  issn      = {2079-6374},
  doi       = {10.3390/bios6030035},
  pages     = {4399 -- 4413},
  year      = {2016},
  abstract  = {Biomimetic binders and catalysts have been generated in order to substitute the biological pendants in separation techniques and bioanalysis. The two major approaches use either "evolution in the test tube" of nucleotides for the preparation of aptamers or total chemical synthesis for molecularly imprinted polymers (MIPs). The reproducible production of aptamers is a clear advantage, whilst the preparation of MIPs typically leads to a population of polymers with different binding sites. The realization of binding sites in the total bulk of the MIPs results in a higher binding capacity, however, on the expense of the accessibility and exchange rate. Furthermore, the readout of the bound analyte is easier for aptamers since the integration of signal generating labels is well established. On the other hand, the overall negative charge of the nucleotides makes aptamers prone to non-specific adsorption of positively charged constituents of the sample and the "biological" degradation of non-modified aptamers and ionic strength-dependent changes of conformation may be challenging in some application.},
  language  = {en}
}
@misc{MengerYarmanErdőssyetal.2017,
  author    = {Menger, Marcus and Yarman, Aysu and Erdőssy, J{\´u}lia and Yildiz, Huseyin Bekir and Gyurcs{\´a}nyi, R{\´o}bert E. and Scheller, Frieder W.},
  title     = {MIPs and aptamers for recognition of proteins in biomimetic sensing},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus4-400496},
  pages     = {19},
  year      = {2017},
  abstract  = {Biomimetic binders and catalysts have been generated in order to substitute the biological pendants in separation techniques and bioanalysis. The two major approaches use either "evolution in the test tube" of nucleotides for the preparation of aptamers or total chemical synthesis for molecularly imprinted polymers (MIPs). The reproducible production of aptamers is a clear advantage, whilst the preparation of MIPs typically leads to a population of polymers with different binding sites. The realization of binding sites in the total bulk of the MIPs results in a higher binding capacity, however, on the expense of the accessibility and exchange rate. Furthermore, the readout of the bound analyte is easier for aptamers since the integration of signal generating labels is well established. On the other hand, the overall negative charge of the nucleotides makes aptamers prone to non-specific adsorption of positively charged constituents of the sample and the "biological" degradation of non-modified aptamers and ionic strength-dependent changes of conformation may be challenging in some application.},
  language  = {en}
}