TY  - JOUR
A1  - Erdossy, Julia
A1  - Horvath, Viola
A1  - Yarman, Aysu
A1  - Scheller, Frieder W.
A1  - Gyurcsanyi, Robert E.
T1  - Electrosynthesized molecularly imprinted polymers for protein recognition
JF  - Trends in Analytical Chemistry
N2  - 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.
KW  - Molecularly imprinted polymers
KW  - Proteins
KW  - Surface imprinting
KW  - Electropolymerization
KW  - Nanostructuring
KW  - Hybrid nanofilms
Y1  - 2016
U6  - https://doi.org/10.1016/j.trac.2015.12.018
SN  - 0165-9936
SN  - 1879-3142
VL  - 79
SP  - 179
EP  - 190
PB  - Elsevier
CY  - Oxford
ER  - 
TY  - JOUR
A1  - Yarman, Aysu
A1  - Scheller, Frieder W.
T1  - MIP-esterase/Tyrosinase Combinations for Paracetamol and Phenacetin
JF  - Electroanalysis : an international journal devoted to fundamental and practical aspects of electroanalysis
N2  - 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.
KW  - Paracetamol
KW  - Molecularly imprinted polymers
KW  - Electropolymerization
KW  - Tyrosinase
KW  - Esterase
KW  - Phenacetin
Y1  - 2016
U6  - https://doi.org/10.1002/elan.201600042
SN  - 1040-0397
SN  - 1521-4109
VL  - 28
SP  - 2222
EP  - 2227
PB  - Wiley-VCH
CY  - Weinheim
ER  - 
TY  - GEN
A1  - Scheller, Frieder W.
A1  - Sakar Dasdan, Dolunay
T1  - Selected papers presented on the 2nd International Conference on the New Trends in Chemistry, Zagreb, Croatia, April 19-22, 2016 Preface
T2  - Bulgarian chemical communications : journal of the Chemical Institutes of the Bulgarian Academy of Sciences and of the Bulgarian Chemical Society = Izvestija po chimija
Y1  - 2016
SN  - 0324-1130
VL  - 48
SP  - 4
EP  - 4
PB  - Bulgarian Academy of Sciences
CY  - Sofia
ER  - 
TY  - JOUR
A1  - Loew, Noya
A1  - Bogdanoff, Peter
A1  - Herrmann, Iris
A1  - Wollenberger, Ursula
A1  - Scheller, Frieder W.
A1  - Katterle, Martin
T1  - Influence of modifications on the efficiency of pyrolysed CoTMPP as electrode material for horseradish peroxidase and the reduction of hydrogen peroxide
JF  - Electroanalysis : an international journal devoted to fundamental and practical aspects of electroanalysis
N2  - 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.
KW  - cobalt porphyrin
KW  - electron transfer
KW  - horseradish peroxidase
KW  - hydrogen peroxide
KW  - immobilization
Y1  - 2006
U6  - https://doi.org/10.1002/elan.200603664
SN  - 1040-0397
VL  - 18
IS  - 23
SP  - 2324
EP  - 2330
PB  - Wiley-VCH
CY  - Weinheim
ER  - 
TY  - JOUR
A1  - Yarman, Aysu
A1  - Dechtrirat, Decha
A1  - Bosserdt, Maria
A1  - Jetzschmann, Katharina J.
A1  - Gajovic-Eichelmann, Nenad
A1  - Scheller, Frieder W.
T1  - Cytochrome c-derived hybrid systems based on moleculary imprinted polymers
JF  - Electroanalysis : an international journal devoted to fundamental and practical aspects of electroanalysis
N2  - 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.
KW  - Molecularly imprinted polymers
KW  - Microperoxidase-11
KW  - Cytochrome c
KW  - Catalytically active MIPs
KW  - Epitope imprinting
KW  - Monoclonal MIPs
Y1  - 2015
U6  - https://doi.org/10.1002/elan.201400592
SN  - 1040-0397
SN  - 1521-4109
VL  - 27
IS  - 3
SP  - 573
EP  - 586
PB  - Wiley-VCH
CY  - Weinheim
ER  - 
TY  - JOUR
A1  - Stöllner, Daniela
A1  - Stöcklein, Walter F. M.
A1  - Scheller, Frieder W.
A1  - Warsinke, Axel
T1  - Membrane-immobilized haptoglobin as affinity matrix for a hemoglobin-A1c-immunosensor
Y1  - 2002
ER  - 
TY  - JOUR
A1  - Sigolaeva, L. V.
A1  - Markower, Alexander
A1  - Eremenko, A. V.
A1  - Makhaeva, G. F.
A1  - Malygin, V. V.
A1  - Kurochkin, I. N.
A1  - Scheller, Frieder W.
T1  - Bioelectrochemical anaysis of neuropathy targes esterase activity in blood
Y1  - 2001
ER  - 
TY  - JOUR
A1  - Rose, Andreas
A1  - Pfeiffer, Dorothea
A1  - Scheller, Frieder W.
A1  - Wollenberger, Ursula
T1  - Quinoprotein glucose dehydrogenasemodified thick-film electrodes for the amperometric detection of phenolic compounds in flow injection analysis
Y1  - 2001
ER  - 
TY  - JOUR
A1  - Scheller, Frieder W.
A1  - Wollenberger, Ursula
A1  - Warsinke, Axel
A1  - Lisdat, Fred
T1  - Research and development in biosensors
Y1  - 2001
ER  - 
TY  - JOUR
A1  - Lisdat, Fred
A1  - Utepbergenov, D.
A1  - Haseloff, R. F.
A1  - Blasig, Ingolf E.
A1  - Stöcklein, Walter F. M.
A1  - Scheller, Frieder W.
A1  - Brigelius-Flohé, Regina
T1  - An optical method for the detection of oxidative stress using protein-RNA interaction
Y1  - 2001
ER  - 
TY  - JOUR
A1  - Hock, Bertold
A1  - Scheller, Frieder W.
T1  - Conclusions and outlook
Y1  - 2001
ER  - 
TY  - JOUR
A1  - Ignatov, S.
A1  - Ge, Bixia
A1  - Scheller, Frieder W.
A1  - Lisdat, Fred
T1  - Detection of the antioxidant activity detection of flavonoids by using superoxide sensor
Y1  - 2001
SN  - 1-58603-164-3
ER  - 
TY  - JOUR
A1  - Lehmann, Claudia
A1  - Wollenberger, Ursula
A1  - Brigelius-Flohé, Regina
A1  - Scheller, Frieder W.
T1  - Modified gold electrodes for electrochemical studies of the reaction phospholipid hydroperoxide glutathione peroxidas with glutathione and glutathione disulfide
Y1  - 2001
ER  - 
TY  - JOUR
A1  - Lisdat, Fred
A1  - Ge, Bixia
A1  - Meyerhoff, M. E.
A1  - Scheller, Frieder W.
T1  - Signal chains with cytochromes at SAM modified gold electrodes
Y1  - 2001
ER  - 
TY  - JOUR
A1  - Lisdat, Fred
A1  - Ge, Bixia
A1  - Krause, B.
A1  - Ehrlich, A.
A1  - Bienert, H.
A1  - Scheller, Frieder W.
T1  - Nucleic acid-promoted electron transfer to cytochrome c
Y1  - 2001
ER  - 
TY  - JOUR
A1  - Scheller, Frieder W.
T1  - Biosensoren auf dem Weg zur Biochip-Technologie
Y1  - 2001
UR  - http://bisc.ch/de/focus_bioelektronik_1_d.pdf
ER  - 
TY  - JOUR
A1  - Scheller, Frieder W.
T1  - Biomoleküle als Reporter in der Analytik : keine Forschung im Elfenbeinturm
Y1  - 2001
ER  - 
TY  - JOUR
A1  - Lisdat, Fred
A1  - Scheller, Frieder W.
T1  - Technical principles. Electrodes
Y1  - 2000
SN  - 90-5702-447-7
ER  - 
TY  - JOUR
A1  - Scheller, Frieder W.
A1  - Pfeiffer, Dorothea
T1  - Biosensor-Technologie in der Medizin und den Biowissenschaften
Y1  - 2000
ER  - 
TY  - JOUR
A1  - Fridman, Vadim
A1  - Wollenberger, Ursula
A1  - Bogdanovskaya, V. A.
A1  - Lisdat, Fred
A1  - Ruzgas, T.
A1  - Lindgren, A.
A1  - Gorton, Lo
A1  - Scheller, Frieder W.
T1  - Electrochemical investigation of cellobiose oxidation by cellobiose dehydrogenase in the presence of cytochrome c as mediator
Y1  - 2000
ER  - 
TY  - JOUR
A1  - Makower, Alexander
A1  - Barmin, Anatoli V.
A1  - Scheller, Frieder W.
T1  - Eine neue Methode zur hochempfindlichen Analyse von Pestiziden
Y1  - 2000
ER  - 
TY  - JOUR
A1  - Warsinke, Axel
A1  - Benkert, Alexander
A1  - Scheller, Frieder W.
T1  - Electrochemical immunoassays
Y1  - 2000
ER  - 
TY  - JOUR
A1  - Gajovic, Nenad
A1  - Binyamin, Gary
A1  - Warsinke, Axel
A1  - Scheller, Frieder W.
A1  - Heller, A.
T1  - Operation of a miniature redox hydrogel-based pyruvate sensor in undiluted deoxygenated calf serum
Y1  - 2000
ER  - 
TY  - JOUR
A1  - Lei, Chenghong
A1  - Wollenberger, Ursula
A1  - Scheller, Frieder W.
T1  - Clay based direct electrochemistry of myoglobin
Y1  - 2000
ER  - 
TY  - JOUR
A1  - Lei, Chenghong
A1  - Wollenberger, Ursula
A1  - Jung, Christiane
A1  - Scheller, Frieder W.
T1  - Clay-bridged electron transfer between cytochrome P450(cam) and electrode
Y1  - 2000
ER  - 
TY  - JOUR
A1  - Lisdat, Fred
A1  - Scheller, Frieder W.
T1  - Principles of sensorial radical detection - a minireview
Y1  - 2000
ER  - 
TY  - JOUR
A1  - Chen, Ziping
A1  - Warsinke, Axel
A1  - Gajovic, Nenad
A1  - Große, St.
A1  - Hu, J.
A1  - Kleber, H.-P.
A1  - Scheller, Frieder W.
T1  - A D-carnitine dehydrogenase electrode for the assessment of enantiomeric purity of L-carnitine preparations
Y1  - 2000
ER  - 
TY  - JOUR
A1  - Scheller, Frieder W.
T1  - Biomolekulare Erkennungssysteme für die Biochemische Analytik
Y1  - 2000
ER  - 
TY  - JOUR
A1  - Scheller, Frieder W.
T1  - Biosensor-Stabilität
Y1  - 2000
ER  - 
TY  - JOUR
A1  - Lisdat, Fred
A1  - Ge, Bixia
A1  - Stöcklein, Walter F. M.
A1  - Scheller, Frieder W.
A1  - Meyer, T.
T1  - Electrochemical behaviour and nitric oxides interaction of immobilised cytochrome c from Rhodocyclus gelatinosus
Y1  - 2000
ER  - 
TY  - JOUR
A1  - Chen, Jian
A1  - Wollenberger, Ursula
A1  - Lisdat, Fred
A1  - Ge, Bixia
A1  - Scheller, Frieder W.
T1  - Superoxide sensor based on hemin modified electrode
Y1  - 2000
ER  - 
TY  - JOUR
A1  - Ju, Huangxian
A1  - Liu, Songqin
A1  - Ge, Bixia
A1  - Lisdat, Fred
A1  - Scheller, Frieder W.
T1  - Electrochemistry of cytochrome c immobilized on colloidal gold modified carbon paste electrodes and its electrocatalytic activity
Y1  - 2000
ER  - 
TY  - JOUR
A1  - Stöcklein, Walter F. M.
A1  - Rohde, M.
A1  - Scharte, Gudrun
A1  - Behrsing, Olaf
A1  - Warsinke, Axel
A1  - Micheel, Burkhard
A1  - Scheller, Frieder W.
T1  - Sensitive detection of triazine and phenylurea pesticides in pure organic solvent by enzyme linked immunsorbent assay (ELISA): stabilities, solubilities and sensitives
Y1  - 2000
ER  - 
TY  - JOUR
A1  - Scheller, Frieder W.
T1  - Deutliche Signale setzen [Leitartikel]
Y1  - 1999
ER  - 
TY  - JOUR
A1  - Huang, T.
A1  - Warsinke, Axel
A1  - Koroljova-Skorobogatko, O. V.
A1  - Makower, Alexander
A1  - Kuwana, T.
A1  - Scheller, Frieder W.
T1  - A bienzyme carbon paste electrode for the sensitive detection of NADPH and the measurement of glucose-6- phosphate dehydrogenase
Y1  - 1999
ER  - 
TY  - JOUR
A1  - Lisdat, Fred
A1  - Ge, Bixia
A1  - Scheller, Frieder W.
T1  - Oligonucleotide-modified electrodes for fast electron transfer to cytochrome c
Y1  - 1999
ER  - 
TY  - JOUR
A1  - Lisdat, Fred
A1  - Ge, Bixia
A1  - Ehrentreich-Förster, Eva
A1  - Reszka, R.
A1  - Scheller, Frieder W.
T1  - SOD activity measurement using cytochrome c modified electrode
Y1  - 1999
ER  - 
TY  - JOUR
A1  - Gajovic, Nenad
A1  - Warsinke, Axel
A1  - Huang, T.
A1  - Schulmeister, Thomas
A1  - Scheller, Frieder W.
T1  - Characterization and mathematical modelling of a novel bienzyme electrode for L-malate with cofactor recycling
Y1  - 1999
ER  - 
TY  - JOUR
A1  - Bauer, Christian G.
A1  - Kühn, A.
A1  - Gajovic, Nenad
A1  - Skorobogatko, O. V.
A1  - Holt, P. J.
A1  - Bruce, N. C.
A1  - Makower, Alexander
A1  - Lowe, Ch. R.
A1  - Scheller, Frieder W.
T1  - New enzymen sensors for morphine and codeine based on morphine dehydrogenase and laccase
Y1  - 1999
ER  - 
TY  - JOUR
A1  - Kleinjung, Frank
A1  - Ehrentreich-Förster, Eva
A1  - Scheller, Frieder W.
T1  - Changing functionality of surfaces by directed self-assembly using oligonucleotides - the oligo-tag
Y1  - 1999
ER  - 
TY  - JOUR
A1  - Barmin, Anatoli V.
A1  - Eremenko, Arkadi V.
A1  - Osipova, T.
A1  - Kurochkin, Iliya
A1  - Makower, Alexander
A1  - Scheller, Frieder W.
T1  - Affinyi fermentometrischeskii analis ingibitorov cholinestarasi
Y1  - 1999
ER  - 
TY  - JOUR
A1  - Scheller, Frieder W.
A1  - Jin, Wen
A1  - Ehrentreich-Förster, Eva
A1  - Ge, Bixia
A1  - Lisdat, Fred
A1  - Büttemeyer, R.
A1  - Wollenberger, Ursula
T1  - Cytochrome c based superoxide sensor for in vivo application
Y1  - 1999
ER  - 
TY  - JOUR
A1  - Lei, Chenghong
A1  - Lisdat, Fred
A1  - Wollenberger, Ursula
A1  - Scheller, Frieder W.
T1  - Cytochrome c : Clay-modified electrode
Y1  - 1999
ER  - 
TY  - JOUR
A1  - Scheller, Frieder W.
A1  - Yarman, Aysu
T1  - Bio vs. Mimetika in der Bioanalytik
T1  - Bio vs. Mimetics in Bioanalysis: An Editorial
BT  - ein Editorial
JF  - Biochemie und analytische Biochemie
N2  - Natürliche Evolution hat geschaffenBiopolymereauf der Basis von Aminosäuren undNukleotidezeigt hohe chemische Selektivität und katalytische Kraft. Die molekulare Erkennung durch Antikörper und die katalytische Umwandlung der Substratmoleküle durch Enzyme findet in sogenannten Paratopen oder katalytischen Zentren des Makromoleküls statt, die typischerweise 10-15 Aminosäuren umfassen. Die konzertierte Wechselwirkung zwischen den Reaktionspartnern führt zu Affinitäten bis zu nanomolaren Konzentrationen für die Antigenbindung und nähert sich einer Million Umsätze pro Sekunde anEnzym-katalysierte Reaktionen.
N2  - Natural evolution has created biopolymers on the basis of amino
acids and nucleotides showing high chemical selectivity and catalytic
power. Molecular recognition by antibodies and catalytic conversion
of the substrate molecules by enzymes take place in so called paratopes or catalytic centres of the macromolecule which comprise typically 10-15 amino acids. The concerted interaction between the reaction partners result in affinities down to nanomolar concentrations for the antigen binding and approaches one million turnovers per second in enzyme-catalyzed reactions.
Nucleic acids bind complimentary single stranded nucleic acids by
base pairing (hybridisation) with nanomolar affinities but also interact highly specific with proteins, e.g. transcription factors, and lowmolecular weight molecules and even with ions.
Biomimetic binders and catalysts have been generated using
“evolution in the test tube” of non-natural nucleotides or total
chemical synthesis of (molecularly imprinted) polymers in order to
substitute the biological pendants in bioanalysis.
Y1  - 2015
SN  - 2161-1009
VL  - 4
IS  - 2
ER  - 
TY  - JOUR
A1  - Stojanovic, Zorica
A1  - Erdossy, Julia
A1  - Keltai, Katalin
A1  - Scheller, Frieder W.
A1  - Gyurcsanyi, Robert E.
T1  - Electrosynthesized molecularly imprinted polyscopoletin nanofilms for human serum albumin detection
JF  - Analytica chimica acta : an international journal devoted to all branches of analytical chemistry
N2  - 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.
KW  - Human serum albumin
KW  - Ferritin
KW  - Molecularly imprinted polymer
KW  - Scopoletin
KW  - Urine
Y1  - 2017
U6  - https://doi.org/10.1016/j.aca.2017.04.043
SN  - 0003-2670
SN  - 1873-4324
VL  - 977
SP  - 1
EP  - 9
PB  - Elsevier
CY  - Amsterdam
ER  - 
TY  - JOUR
A1  - Bognár, Zsófia
A1  - Supala, Eszter
A1  - Yarman, Aysu
A1  - Zhang, Xiaorong
A1  - Bier, Frank Fabian
A1  - Scheller, Frieder W.
A1  - Gyurcsanyi, Róbert E.
T1  - Peptide epitope-imprinted polymer microarrays for selective protein recognition
BT  - application for SARS-CoV-2 RBD protein
JF  - Chemical science / RSC, Royal Society of Chemistry
N2  - 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.
Y1  - 2021
U6  - https://doi.org/10.1039/d1sc04502d
SN  - 2041-6539
VL  - 13
IS  - 5
SP  - 1263
EP  - 1269
PB  - Royal Society of Chemistry
CY  - Cambridge
ER  - 
TY  - JOUR
A1  - Tanne, Johannes
A1  - Jeoung, Jae-Hun
A1  - Peng, Lei
A1  - Yarman, Aysu
A1  - Dietzel, Birgit
A1  - Schulz, Burkhard
A1  - Schad, Daniel
A1  - Dobbek, Holger
A1  - Wollenberger, Ursula
A1  - Bier, Frank Fabian
A1  - Scheller, Frieder W.
T1  - Direct Electron Transfer and Bioelectrocatalysis by a Hexameric, Heme Protein at Nanostructured Electrodes
JF  - Electroanalysis : an international journal devoted to fundamental and practical aspects of electroanalysis
N2  - 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.
KW  - HTHP
KW  - Nanohybrid
KW  - Poylaniline
KW  - Multiwalled carbon nanotube
Y1  - 2015
U6  - https://doi.org/10.1002/elan.201500231
SN  - 1040-0397
SN  - 1521-4109
VL  - 27
IS  - 10
SP  - 2262
EP  - 2267
PB  - Wiley-VCH
CY  - Weinheim
ER  - 
TY  - JOUR
A1  - Scheller, Frieder W.
A1  - Kleinjung, Frank
A1  - Bier, Frank Fabian
A1  - Markower, Alexander
A1  - Neumann, Barbara
A1  - Wollenberger, Ursula
A1  - Kurochkin, Iliya N.
A1  - Eremenko, Arkadi V.
A1  - Barmin, Anatoli V.
A1  - Klußmann, Sven
A1  - Fürste, Jens-Peter
A1  - Erdmann, Volker A.
A1  - Mansuy, D.
T1  - New recognition elements in biosensing
Y1  - 1998
ER  - 
TY  - JOUR
A1  - Yarman, Aysu
A1  - Kurbanoğlu, Sevinç
A1  - Zebger, Ingo
A1  - Scheller, Frieder W.
T1  - Simple and robust
BT  - the claims of protein sensing by molecularly imprinted polymers
JF  - Sensors and actuators : B, Chemical : an international journal devoted to research and development of chemical transducers
N2  - 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.
KW  - Molecularly imprinted polymer
KW  - Plastibodies
KW  - Functional scaffolds
KW  - Biomimetic sensors
KW  - Proteins
Y1  - 2021
U6  - https://doi.org/10.1016/j.snb.2020.129369
SN  - 0925-4005
SN  - 1873-3077
VL  - 330
PB  - Elsevier Science
CY  - Amsterdam [u.a.]
ER  - 
TY  - JOUR
A1  - Caserta, Giorgio
A1  - Zhang, Xiaorong
A1  - Yarman, Aysu
A1  - Supala, Eszter
A1  - Wollenberger, Ulla
A1  - Gyurcsányi, Róbert  E.
A1  - Zebger, Ingo
A1  - Scheller, Frieder W.
T1  - Insights in electrosynthesis, target binding, and stability of peptide-imprinted polymer nanofilms
JF  - Electrochimica acta : the journal of the International Society of Electrochemistry (ISE)
N2  - 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.
KW  - SEIRA spectroelectrochemistry
KW  - peptide imprinting
KW  - electrosynthesis
KW  - MIP
KW  - glycated peptide
Y1  - 2021
U6  - https://doi.org/10.1016/j.electacta.2021.138236
SN  - 0013-4686
SN  - 1873-3859
VL  - 381
PB  - Elsevier
CY  - New York, NY [u.a.]
ER  - 
TY  - JOUR
A1  - Wollenberger, Ursula
A1  - Schubert, Florian
A1  - Pfeiffer, Dorothea
A1  - Scheller, Frieder W.
T1  - Recycling sensors based on kinases : proceedings of Mosbach Symposion on Biochemical Technology
Y1  - 1996
ER  - 
TY  - JOUR
A1  - Scheller, Frieder W.
A1  - Wollenberger, Ursula
A1  - Pfeiffer, Dorothea
A1  - Schubert, Florian
T1  - Overview of biosensor technology : proceedings of Mosbach Symposion on Biochemical Technology
Y1  - 1996
ER  - 
TY  - JOUR
A1  - Scheller, Frieder W.
A1  - Schubert, Florian
A1  - Bier, Frank Fabian
T1  - Vom Biosensor zur Nanobiotechnologie
Y1  - 1995
ER  - 
TY  - JOUR
A1  - Scheller, Frieder W.
A1  - Wollenberger, Ursula
A1  - Schubert, Florian
A1  - Pfeiffer, Dorothea
A1  - Markower, Alexander
A1  - McNeil, C. J.
T1  - Multienzyme biosensors : coupled enzyme reactions and enzyme activation
Y1  - 1993
ER  - 
TY  - JOUR
A1  - Pfeiffer, Dorothea
A1  - Scheller, Frieder W.
A1  - Schubert, Florian
A1  - Setz, K.
T1  - Amperometric enzyme electrodes for lactate and glucose determinations in highly diluted and undiluted media
Y1  - 1993
ER  - 
TY  - JOUR
A1  - Scheller, Frieder W.
A1  - Kirstein, Dieter
A1  - Schubert, Florian
A1  - Pfeiffer, Dorothea
A1  - McNeil, C. J.
T1  - Enzymes in electrochemical biosensors
Y1  - 1993
ER  - 
TY  - JOUR
A1  - Scheller, Frieder W.
A1  - Pfeiffer, Dorothea
A1  - Schubert, Florian
A1  - Wollenberger, Ursula
T1  - Enzyme - based electrodes
Y1  - 1995
ER  - 
TY  - JOUR
A1  - Wollenberger, Ursula
A1  - Schubert, Florian
A1  - Pfeiffer, Dorothea
A1  - Scheller, Frieder W.
T1  - Enhancing biosensor performance using multienzyme systems
Y1  - 1993
ER  - 
TY  - GEN
A1  - Peng, Lei
A1  - Yarman, Aysu
A1  - Jetzschmann, Katharina J.
A1  - Jeoung, Jae-Hun
A1  - Schad, Daniel
A1  - Dobbek, Holger
A1  - Wollenberger, Ursula
A1  - Scheller, Frieder W.
T1  - Molecularly imprinted electropolymer for a hexameric heme protein with direct electron transfer and peroxide electrocatalysis
N2  - 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).
T3  - Zweitveröffentlichungen der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe - 362 
KW  - molecularly imprinted polymers
KW  - self-assembled monolayer
KW  - direct electron transfer
KW  - hydrogen peroxide
KW  - bioelectrocatalysis
Y1  - 2017
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:kobv:517-opus4-400627
ER  - 
TY  - JOUR
A1  - Peng, Lei
A1  - Yarman, Aysu
A1  - Jetzschmann, Katharina J.
A1  - Jeoung, Jae-Hun
A1  - Schad, Daniel
A1  - Dobbek, Holger
A1  - Wollenberger, Ursula
A1  - Scheller, Frieder W.
T1  - Molecularly Imprinted Electropolymer for a Hexameric Heme Protein with Direct Electron Transfer and Peroxide Electrocatalysis
JF  - SENSORS
N2  - 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).
KW  - hydrogen peroxide
KW  - bioelectrocatalysis
KW  - molecularly imprinted polymers
KW  - direct electron transfer
KW  - self-assembled monolayer
Y1  - 2016
U6  - https://doi.org/10.3390/s16030272
SN  - 1424-8220
VL  - 16
SP  - 1343
EP  - 1364
PB  - MDPI
CY  - Basel
ER  - 
TY  - JOUR
A1  - Tadjoung Waffo, Armel Franklin
A1  - Yesildag, Cigdem
A1  - Caserta, Giorgio
A1  - Katz, Sagie
A1  - Zebger, Ingo
A1  - Lensen, Marga C.
A1  - Wollenberger, Ulla
A1  - Scheller, Frieder W.
A1  - Altintas, Zeynep
T1  - Fully electrochemical MIP sensor for artemisinin
JF  - Sensors and actuators : B, Chemical
N2  - 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.
KW  - Electro-synthesized molecularly imprinted polymer
KW  - o-Phenylenediamine
KW  - Artemisinin
KW  - Antimalarial drug detection
KW  - Electrochemical sensor
Y1  - 2018
U6  - https://doi.org/10.1016/j.snb.2018.08.018
SN  - 0925-4005
VL  - 275
SP  - 163
EP  - 173
PB  - Elsevier
CY  - Lausanne
ER  - 
TY  - JOUR
A1  - Zhang, Xiaorong
A1  - Caserta, Giorgio
A1  - Yarman, Aysu
A1  - Supala, Eszter
A1  - Tadjoung Waffo, Armel Franklin
A1  - Wollenberger, Ulla
A1  - Gyurcsanyi, Robert E.
A1  - Zebger, Ingo
A1  - Scheller, Frieder W.
T1  - "Out of Pocket" protein binding
BT  - a dilemma of epitope imprinted polymers revealed for human hemoglobin
JF  - Chemosensors
N2  - 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.
KW  - Molecularly Imprinted Polymers
KW  - epitope imprinting
KW  - non-specific
KW  - binding
KW  - redox gating
KW  - SEIRA spectroelectrochemistry
Y1  - 2021
U6  - https://doi.org/10.3390/chemosensors9060128
SN  - 2227-9040
VL  - 9
IS  - 6
PB  - MDPI
CY  - Basel
ER  - 
TY  - JOUR
A1  - Menger, Marcus
A1  - Yarman, Aysu
A1  - Erdössy, Júlia
A1  - Yildiz, Huseyin Bekir
A1  - Gyurcsányi, Róbert E.
A1  - Scheller, Frieder W.
T1  - MIPs and Aptamers for Recognition of Proteins in Biomimetic Sensing
JF  - Biosensors : open access journal
N2  - 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.
KW  - biomimetic recognition elements
KW  - aptamers
KW  - molecularly imprinted polymers
KW  - chemical sensors
KW  - aptasensors
KW  - in vitro selection
KW  - SELEX
Y1  - 2016
U6  - https://doi.org/10.3390/bios6030035
SN  - 2079-6374
VL  - 6
SP  - 4399
EP  - 4413
PB  - MDPI
CY  - Basel
ER  - 
TY  - GEN
A1  - Menger, Marcus
A1  - Yarman, Aysu
A1  - Erdőssy, Júlia
A1  - Yildiz, Huseyin Bekir
A1  - Gyurcsányi, Róbert E.
A1  - Scheller, Frieder W.
T1  - MIPs and aptamers for recognition of proteins in biomimetic sensing
N2  - 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.
T3  - Zweitveröffentlichungen der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe - 357 
KW  - biomimetic recognition elements
KW  - aptamers
KW  - molecularly imprinted polymers
KW  - chemical sensors
KW  - aptasensors
KW  - in vitro selection
KW  - SELEX
Y1  - 2017
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:kobv:517-opus4-400496
ER  - 
TY  - CHAP
A1  - Lück, Erika
A1  - Balderjahn, Ingo
A1  - Kamm, Birgit
A1  - Greil, Holle
A1  - Wallschläger, Hans-Dieter
A1  - Jessel, Beate
A1  - Böckmann, Christine
A1  - Oberhänsli, Roland
A1  - Soyez, Konrad
A1  - Schmeer, Ernst
A1  - Blumenstein, Oswald
A1  - Berndt, Klaus-Peter
A1  - Edeling, Thomas
A1  - Friedrich, Sabine
A1  - Kaden, Klaus
A1  - Scheller, Frieder W.
A1  - Petersen, Hans-Georg
A1  - Asche, Hartmut
A1  - Bronstert, Axel
A1  - Giest, Hartmut
A1  - Gaedke, Ursula
A1  - Löhmannsröben, Hans-Gerd
A1  - Jeltsch, Florian
A1  - Jänkel, Ralph
A1  - Gzik, Axel
A1  - Bork, Hans-Rudolf
A1  - Bork, Hans-Rudolf
T1  - Umweltforschung für das Land Brandenburg : Arbeitsgruppen und Professuren
Y1  - 2000
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:kobv:517-opus-3797
ER  - 
TY  - CHAP
A1  - Asche, Hartmut
A1  - Böckmann, Christine
A1  - Laue, Steffen
A1  - Löhmannsröben, Hans-Gerd
A1  - Lemke, Matthias
A1  - Schober, Lars
A1  - Reich, Oliver
A1  - Lück, Erika
A1  - Schütte, Marc
A1  - Domsch, Horst
A1  - Makower, Alexander
A1  - Scheller, Frieder W.
A1  - Stöcklein, Wolfgang
A1  - Wollenberger, Ursula
A1  - Schultze, Rainer
A1  - Hengstermann, Theo
A1  - Schael, Frank
T1  - Umweltforschung für das Land Brandenburg : Projekt Umweltanalytik / Umweltmeßtechnik / Informationssysteme
Y1  - 2000
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:kobv:517-opus-3862
SP  - 176
EP  - 227
ER  -