TY - JOUR AU - Bognár, Balázs AU - Lemli, Beáta AU - Kőrösi, László Tamás AU - Mohamed Ameen, Hiba Farooq AU - Derdák, Diána AU - Isbera, Mostafa AU - Preisz, Zsolt AU - Úr, Györgyi AU - Pápayné Sár, Cecília AU - Kunsági-Máté, Sándor AU - Kálai, Tamás TI - Szemelvények a PTE GyTK Szerves és Gyógyszerkémiai Intézetének újabb (2013-2021) kutatási eredményeiből JF - MAGYAR KÉMIAI FOLYÓIRAT - KÉMIAI KÖZLEMÉNYEK (1997-) J2 - MAGY KÉM FOLY KÉM KÖZL VL - 128 PY - 2022 IS - 2 SP - 68 EP - 78 PG - 11 SN - 1418-9933 DO - 10.24100/MKF.2022.02.68 UR - https://m2.mtmt.hu/api/publication/33090440 ID - 33090440 LA - Hungarian DB - MTMT ER - TY - JOUR AU - Fliszár-Nyúl, Eszter AU - Faisal, Anna Zelma AU - Mohos, Violetta Karolin AU - Derdák, Diána AU - Lemli, Beáta AU - Kálai, Tamás AU - Pápayné Sár, Cecília AU - Zsidó, Balázs Zoltán AU - Hetényi, Csaba AU - Horváth, Ádám István AU - Helyes, Zsuzsanna AU - Deme, Ruth AU - Bogdán, Dóra AU - Czompa, Andrea AU - Mátyus, Péter AU - Poór, Miklós TI - Interaction of SZV 1287, a novel oxime analgesic drug candidate, and its metabolites with serum albumin JF - JOURNAL OF MOLECULAR LIQUIDS J2 - J MOL LIQ VL - 333 PY - 2021 PG - 10 SN - 0167-7322 DO - 10.1016/j.molliq.2021.115945 UR - https://m2.mtmt.hu/api/publication/31927621 ID - 31927621 N1 - Department of Pharmacology, Faculty of Pharmacy, University of Pécs, Szigeti út 12, Pécs, H-7624, Hungary Lab-on-a-Chip Research Group, János Szentágothai Research Centre, University of Pécs, Ifjúság útja 20, Pécs, H-7624, Hungary Institute of Organic and Medicinal Chemistry, Medical School, University of Pécs, Szigeti út 12, Pécs, H-7624, Hungary Green Chemistry Research Group, János Szentágothai Research Centre, University of Pécs, Ifjúság útja 20, Pécs, H-7624, Hungary Department of General and Physical Chemistry, Faculty of Sciences, University of Pécs, Ifjúság 6, Pécs, H-7624, Hungary Department of Pharmacology and Pharmacotherapy, Medical School, University of Pécs, Szigeti út 12, Pécs, H-7624, Hungary Molecular Pharmacology Research Group & Centre for Neuroscience, János Szentágothai Research Centre, University of Pécs, Ifjúság útja 20, Pécs, H-7624, Hungary PharmInVivo Ltd., Szondi György u. 10, Pécs, H-7629, Hungary Algonist Gmbh, 1030 Karl-Farkas-Gasse 22, Wien, Austria Department of Organic Chemistry, Faculty of Pharmacy, Semmelweis University, Hőgyes u. 7, Budapest, H-1092, Hungary Institute of Digital Health Sciences, Semmelweis University, Faculty of Health and Public Services, Ferenc tér 15, Budapest, H-1094, Hungary E-Group Ict Software Zrt, Kacsa u. 11, Budapest, H-1027, Hungary Cited By :10 Export Date: 31 August 2023 CODEN: JMLID Correspondence Address: Poór, M.; Department of Pharmacology, Szigeti út 12, Hungary; email: poor.miklos@pte.hu LA - English DB - MTMT ER - TY - JOUR AU - Derdák, Diána AU - Poór, Miklós AU - Kunsági-Máté, Sándor AU - Lemli, Beáta TI - Interaction of amphotericin B with human and bovine serum albumins: a fluorescence polarization study JF - CHEMICAL PHYSICS LETTERS J2 - CHEM PHYS LETT VL - 724 PY - 2019 SP - 13 EP - 17 PG - 5 SN - 0009-2614 DO - 10.1016/j.cplett.2019.03.049 UR - https://m2.mtmt.hu/api/publication/30612672 ID - 30612672 N1 - Export Date: 18 January 2024 CODEN: CHPLB LA - English DB - MTMT ER - TY - JOUR AU - Faisal, Anna Zelma AU - Vörös, Virág AU - Lemli, Beáta AU - Derdák, Diána AU - Kunsági-Máté, Sándor AU - Bálint, Mónika Enikő AU - Hetényi, Csaba AU - Jakabfi-Csepregi, Rita AU - Kőszegi, Tamás AU - Bergmann, Dominik AU - Sueck, Franziska AU - Humpf, Hans-Ulrich AU - Hübner, Florian AU - Poór, Miklós TI - Interaction of the mycotoxin metabolite dihydrocitrinone with serum albumin JF - MYCOTOXIN RESEARCH J2 - MYCOTOX RES VL - 35 ET - 0 PY - 2019 IS - 2 SP - 129 EP - 139 PG - 11 SN - 0178-7888 DO - 10.1007/s12550-018-0336-z UR - https://m2.mtmt.hu/api/publication/30319045 ID - 30319045 N1 - Export Date: 18 January 2024 AB - Citrinin (CIT) is a nephrotoxic mycotoxin produced by Penicillium, Monascus, and Aspergillus species. CIT appears as a contaminant in cereals, cereal-based products, fruits, nuts, and spices. During the biotransformation of CIT, its major urinary metabolite dihydrocitrinone (DHC) is formed. Albumin interacts with several compounds (including mycotoxins) affecting their tissue distribution and elimination. CIT-albumin interaction is known; however, the complex formation of DHC with albumin has not been reported previously. In this study, we aimed to investigate the interaction of DHC with albumin, employing fluorescence spectroscopy, circular dichroism, and molecular modeling studies. Furthermore, species differences and thermodynamics of the interaction as well as the effects of albumin on the acute in vitro toxicity of DHC and CIT were also tested. Our main observations/conclusions are as follows: (1) Fluorescence signal of DHC is strongly enhanced by albumin. (2) Formation of DHC-albumin complexes is supported by both fluorescence spectroscopic and circular dichroism studies. (3) DHC forms similarly stable complexes with human albumin (K~105 L/mol) as CIT. (4) DHC-albumin interaction did not show significant species differences (tested with human, bovine, porcine, and rat albumins). (5) Based on modeling studies and investigations with site markers, DHC occupies the Heme binding site (subdomain IB) on human albumin. (6) The presence of albumin significantly decreased the acute in vitro cytotoxic effects of both DHC and CIT on MDCK cell line. LA - English DB - MTMT ER - TY - CONF AU - Faisal, Anna Zelma AU - Vörös, Virág AU - Derdák, Diána AU - Lemli, Beáta AU - Bálint, Mónika Enikő AU - Hetényi, Csaba AU - Jakabfi-Csepregi, Rita AU - Sueck, Franziska AU - Humpfg, Hans-Ulrich AU - Cramer, Benedikt AU - Poór, Miklós TI - Ochratoxin A és 2'R-Ochratoxin A kölcsönhatásainak vizsgálata szérum albuminnal T2 - TOX'2018 Tudományos Konferencia Program, kivonatok PY - 2018 SP - 48 EP - 48 PG - 1 UR - https://m2.mtmt.hu/api/publication/30699187 ID - 30699187 LA - Hungarian DB - MTMT ER - TY - GEN AU - Faisal, Anna Zelma AU - Vörös, Virág AU - Derdák, Diána AU - Lemli, Beáta AU - Bálint, Mónika Enikő AU - Hetényi, Csaba AU - Jakabfi-Csepregi, Rita AU - Sueck, Franziska AU - Humpf, Hans-Ulrich AU - Cramer, Benedikt AU - Poór, Miklós TI - Ochratoxin A és 2’R-Ochratoxin A kölcsönhatásainak vizsgálata szérum albuminnal PY - 2018 UR - https://m2.mtmt.hu/api/publication/30613515 ID - 30613515 LA - Hungarian DB - MTMT ER - TY - JOUR AU - Faisal, Anna Zelma AU - Derdák, Diána AU - Lemli, Beáta AU - Kunsági-Máté, Sándor AU - Bálint, Mónika Enikő AU - Hetényi, Csaba AU - Jakabfi-Csepregi, Rita AU - Kőszegi, Tamás AU - Sueck, Franziska AU - Cramer, Benedikt AU - Humpf, Hans-Ulrich AU - Poór, Miklós TI - Interaction of 2'R-ochratoxin A with Serum Albumins : Binding Site, Effects of Site Markers, Thermodynamics, Species Differences of Albumin-binding, and Influence of Albumin on Its Toxicity in MDCK Cells JF - TOXINS J2 - TOXINS VL - 10 PY - 2018 IS - 9 PG - 16 SN - 2072-6651 DO - 10.3390/toxins10090353 UR - https://m2.mtmt.hu/api/publication/3408877 ID - 3408877 N1 - Funding Agency and Grant Number: Hungarian National Research, Development and Innovation Office [FK125166, K123836]; Deutsche Forschungsgemeinschaft, Bonn, Germany [HU 730/10-2] Funding text: This study was supported by the Hungarian National Research, Development and Innovation Office (FK125166) and the Deutsche Forschungsgemeinschaft, Bonn, Germany (HU 730/10-2). The work of M.B. and C.H. is supported by the Hungarian National Research, Development and Innovation Office (K123836). AB - Ochratoxin A (OTA) is a nephrotoxic mycotoxin. Roasting of OTA-contaminated coffee results in the formation of 2'R-ochratoxin A (2'R-OTA), which appears in the blood of coffee drinkers. Human serum albumin (HSA) binds 2'R-OTA (and OTA) with high affinity; therefore, albumin may influence the tissue uptake and elimination of ochratoxins. We aimed to investigate the binding site of 2'R-OTA (verses OTA) in HSA and the displacing effects of site markers to explore which molecules can interfere with its albumin-binding. Affinity of 2'R-OTA toward albumins from various species (human, bovine, porcine and rat) was tested to evaluate the interspecies differences regarding 2'R-OTA-albumin interaction. Thermodynamic studies were performed to give a deeper insight into the molecular background of the complex formation. Besides fluorescence spectroscopic and modeling studies, effects of HSA, and fetal bovine serum on the cytotoxicity of 2'R-OTA and OTA were tested in MDCK kidney cell line in order to demonstrate the influence of albumin-binding on the cellular uptake of ochratoxins. Site markers displaced more effectively 2'R-OTA than OTA from HSA. Fluorescence and binding constants of 2'R-OTA-albumin and OTA-albumin complexes showed different tendencies. Albumin significantly decreased the cytotoxicity of ochratoxins. 2'R-OTA, even at sub-toxic concentrations, increased the toxic action of OTA. LA - English DB - MTMT ER - TY - JOUR AU - Lemli, Beáta AU - Derdák, Diána AU - Laczay, P AU - Kovacs, D AU - Kunsági-Máté, Sándor TI - Noncovalent Interaction of Tilmicosin with Bovine Serum Albumin. JF - MOLECULES J2 - MOLECULES VL - 23 PY - 2018 IS - 8 PG - 10 SN - 1420-3049 DO - 10.3390/molecules23081915 UR - https://m2.mtmt.hu/api/publication/3401784 ID - 3401784 AB - Tilmicosin is a widely used antibiotic in veterinary applications. Its antimicrobial activity is ranged from Gram-positive and some Gram-negative bacteria towards activities against Mycoplasma and Chlamydia. Adsorption affinity of tilmicosin antibiotics towards bovine serum albumin was investigated by both spectroscopic (UV-vis, Photoluminescence) and calorimetric methods. The interaction was determined on the basis of quenching of albumin by tilmicosin. Results confirm noncovalent binding of tilmicosin on bovine serum albumin with 1:1 stoichiometry associated with pK = 4.5, highlighting possible removal of tilmicosin molecules from the albumin surface through exchange reactions by known competitor molecules. Calorimetric measurements have confirmed the weak interaction between tilmicosin and albumin and reflect enhanced denaturation of the albumin in the presence of tilmicosin antibiotic. This process is associated with the decreased activation energy of conformational transition of the albumin. It opens a new, very quick reaction pathway without any significant effect on the product by noncovalent binding the tilmicosin molecules to the protein molecules. Results highlight the medical importance of these investigations by considerable docking of the selected antibiotic molecules on serum albumins. Although the binding may cause toxic effects in living bodies, the strength of the binding is weak enough to find competitor molecules for effective removals from their surface. LA - English DB - MTMT ER - TY - CONF AU - Vörös, Virág AU - Faisal, Anna Zelma AU - Derdák, Diána AU - Lemli, Beáta AU - Bálint, Mónika Enikő AU - Hetényi, Csaba AU - Jakabfi-Csepregi, Rita AU - Poór, Miklós TI - Dihidrocitrinon kölcsönhatásának vizsgálata szérum albuminnal T2 - TOX'2018 Tudományos Konferencia Program, kivonatok PY - 2018 SP - 140 EP - 140 PG - 1 UR - https://m2.mtmt.hu/api/publication/30699198 ID - 30699198 LA - Hungarian DB - MTMT ER - TY - GEN AU - Vörös, Virág AU - Faisal, Anna Zelma AU - Derdák, Diána AU - Lemli, Beáta AU - Bálint, Mónika Enikő AU - Hetényi, Csaba AU - Jakabfi-Csepregi, Rita AU - Poór, Miklós TI - Dihidrocitrinon kölcsönhatásának vizsgálata szérum albuminnal PY - 2018 UR - https://m2.mtmt.hu/api/publication/30613550 ID - 30613550 N1 - [Poszter] LA - Hungarian DB - MTMT ER -