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Selma Ozturk  - - - 
Top co-authors See all
Ozlem Ertekin

6 shared publications

TÜBİTAK, The Scientific and Technological Research Council of Turkey, Marmara Research Center, Genetic Engineering and Biotechnology Institute, Gebze, Kocaeli 41400, Turkey

Zafer Ziya Ozturk

6 shared publications

Esin Akçael

3 shared publications

Özlem Ertekin

2 shared publications

Fatma Betul Guloglu

1 shared publications

TÜBİTAK, The Scientific and Technological Research Council of Turkey, Marmara Research Center, Genetic Engineering and Biotechnology Institute, 41400 Gebze, Kocaeli, Turkey

Publication Record
Distribution of Articles published per year 
(2012 - 2018)
Total number of journals
published in
Publications See all
Article 0 Reads 0 Citations Biological Activity of the Carrier as a Factor in Immunogen Design for Haptens Özlem Ertekin, Esin Akçael, Harun Kocaağa, Selma Öztürk Published: 14 November 2018
Molecules, doi: 10.3390/molecules23112977
DOI See at publisher website ABS Show/hide abstract
Immunoanalytical methods are frequently employed in the detection of hazardous small molecular weight compounds. However, antibody development for these molecules is a challenge, because they are haptens and cannot induce a humoral immune response in experimental animals. Immunogenic forms of haptens are usually prepared by conjugating them to a protein carrier which serves as an immune stimulator. However, the carrier is usually considered merely as a bulk mass, and its biological activity is ignored. Here, we induced an endocytic receptor, transferrin receptor, by selecting its ligand as a carrier protein to enhance antibody production. We conjugated aflatoxin, a potent carcinogenic food contaminant, to transferrin and evaluated its potential to stimulate antibody production with respect to ovalbumin conjugates. Transferrin conjugates induced aflatoxin-specific immune responses in the second immunization, while ovalbumin conjugates reached similar antibody titers after 5 injections. Monoclonal antibodies were successfully developed with mice immunized with either of the conjugates.
Article 0 Reads 3 Citations Label-Free QCM Immunosensor for the Detection of Ochratoxin A Şerife Pirinçci, Ozlem Ertekin, Duygu Laguna, Fehime Özen, Z... Published: 11 April 2018
Sensors, doi: 10.3390/s18041161
DOI See at publisher website ABS Show/hide abstract
Ochratoxin A (OTA) is a potent mycotoxin that poses a risk in food and feed moieties and subject to worldwide regulation. Laboratory-based analytical methods are traditionally employed for reliable OTA quantification, but these methods cannot provide rapid and on-site analysis, where biosensors fill this gap. In this study a label-free quartz crystal microbalance (QCM)-based immunosensor for the detection of OTA, which is one of the most important small molecule contaminants, was developed by direct immobilization of OTA to amine-bearing sensor surfaces using 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide (EDC)/N-Hydroxysuccinimide (NHS) chemistry. The protein-free sensor surface enabled regeneration of sensor surface with 50 mM NaOH and 1% SDS up to 13 times without loss of performance, which would disrupt a protein-containing sensor surface. We developed a QCM immunosensor using the developed sensor surface with a 17.2–200 ng/mL detection range which can be used for on-site detection of feedstuffs.
Article 0 Reads 0 Citations Label-Free QCM Immunosensor for the Detection of Ochratoxin A Serife Seyda Pirincci, Ozlem Ertekin, Duygu Ercan Laguna, Fe... Published: 27 November 2017
Proceedings, doi: 10.3390/proceedings1080706
DOI See at publisher website ABS Show/hide abstract
Mycotoxins are one of the most important food and feed contaminants threatening human health.
Article 1 Read 5 Citations Label Free QCM Immunobiosensor for AFB1 Detection Using Monoclonal IgA Antibody as Recognition Element Özlem Ertekin, Selma Öztürk, Zafer Öztürk Published: 11 August 2016
Sensors, doi: 10.3390/s16081274
DOI See at publisher website PubMed View at PubMed ABS Show/hide abstract
This study introduces the use of an IgA isotype aflatoxin (AF) specific monoclonal antibody for the development of a highly sensitive Quartz Crystal Microbalance (QCM) immunobiosensor for the detection of AF in inhibitory immunoassay format. The higher molecular weight of IgA antibodies proved an advantage over commonly used IgG antibodies in label free immunobiosensor measurements. IgA and IgG antibodies with similar affinity for AF were used in the comparative studies. Sensor surface was prepared by covalent immobilization of AFB1, using self assembled monolayer (SAM) formed on gold coated Quartz Crystal, with 1-Ethyl-3-(3-dimethylaminopropyl) carbodiimide/N-hydroxy succinimide (EDC/NHS) method using a diamine linker. Nonspecific binding to the surface was decreased by minimizing the duration of EDC/NHS activation. Sensor surface was chemically blocked after AF immobilization without any need for protein blocking. This protein free sensor chip endured harsh solutions with strong ionic detergent at high pH, which is required for the regeneration of the high affinity antibody-antigen interaction. According to the obtained results, the detection range with IgA antibodies was higher than IgG antibodies in QCM immunosensor developed for AFB1.
Article 0 Reads 2 Citations Monoclonal IgA Antibodies for Aflatoxin Immunoassays Özlem Ertekin, Şerife Şeyda Pirinçci, Selma Öztürk Published: 12 May 2016
Toxins, doi: 10.3390/toxins8050148
DOI See at publisher website PubMed View at PubMed ABS Show/hide abstract
Antibody based techniques are widely used for the detection of aflatoxins which are potent toxins with a high rate of occurrence in many crops. We developed a murine monoclonal antibody of immunoglobulin A (IgA) isotype with a strong binding affinity to aflatoxin B1 (AFB1), aflatoxin B2 (AFB2), aflatoxin G1 (AFG1), aflatoxin G2 (AFG2) and aflatoxin M1 (AFM1). The antibody was effectively used in immunoaffinity column (IAC) and ELISA kit development. The performance of the IACs was compatible with AOAC performance standards for affinity columns (Test Method: AOAC 991.31). The total binding capacity of the IACs containing our antibody was 111 ng, 70 ng, 114 ng and 73 ng for AFB1, AFB2, and AFG1 andAFG2, respectively. Furthermore, the recovery rates of 5 ng of each AF derivative loaded to the IACs were determined as 104.9%, 82.4%, 85.5% and 70.7% for AFB1, AFB2, AFG1 and AFG2, respectively. As for the ELISA kit developed using non-oriented, purified IgA antibody, we observed a detection range of 2–50 µg/L with 40 min total test time. The monoclonal antibody developed in this research is hitherto the first presentation of quadruple antigen binding IgA monoclonal antibodies in mycotoxin analysis and also the first study of their utilization in ELISA and IACs. IgA antibodies are valuable alternatives for immunoassay development, in terms of both sensitivity and ease of preparation, since they do not require any orientation effort.
Article 0 Reads 1 Citation Antibody based systems for the determination of mycotoxins in food and feed Özlem Ertekin, Fatma Betul Guloglu, Seyda Pirincci, Sevecen ... Published: 01 July 2013
Current Opinion in Biotechnology, doi: 10.1016/j.copbio.2013.05.028
DOI See at publisher website