@article{MTMT:33090440,
	title = {Szemelvények a PTE GyTK Szerves és Gyógyszerkémiai Intézetének újabb (2013-2021) kutatási eredményeiből},
	url = {https://m2.mtmt.hu/api/publication/33090440},
	author = {Bognár, Balázs and Lemli, Beáta and Kőrösi, László Tamás and Mohamed Ameen, Hiba Farooq and Derdák, Diána and Isbera, Mostafa and Preisz, Zsolt and Úr, Györgyi and Pápayné Sár, Cecília and Kunsági-Máté, Sándor and Kálai, Tamás},
	doi = {10.24100/MKF.2022.02.68},
	journal-iso = {MAGY KÉM FOLY KÉM KÖZL},
	journal = {MAGYAR KÉMIAI FOLYÓIRAT - KÉMIAI KÖZLEMÉNYEK (1997-)},
	volume = {128},
	unique-id = {33090440},
	issn = {1418-9933},
	year = {2022},
	eissn = {1418-8600},
	pages = {68-78},
	orcid-numbers = {Lemli, Beáta/0000-0001-8903-1337}
}

@article{MTMT:31927621,
	title = {Interaction of SZV 1287, a novel oxime analgesic drug candidate, and its metabolites with serum albumin},
	url = {https://m2.mtmt.hu/api/publication/31927621},
	author = {Fliszár-Nyúl, Eszter and Faisal, Anna Zelma and Mohos, Violetta Karolin and Derdák, Diána and Lemli, Beáta and Kálai, Tamás and Pápayné Sár, Cecília and Zsidó, Balázs Zoltán and Hetényi, Csaba and Horváth, Ádám István and Helyes, Zsuzsanna and Deme, Ruth and Bogdán, Dóra and Czompa, Andrea and Mátyus, Péter and Poór, Miklós},
	doi = {10.1016/j.molliq.2021.115945},
	journal-iso = {J MOL LIQ},
	journal = {JOURNAL OF MOLECULAR LIQUIDS},
	volume = {333},
	unique-id = {31927621},
	issn = {0167-7322},
	year = {2021},
	eissn = {1873-3166},
	orcid-numbers = {Fliszár-Nyúl, Eszter/0000-0003-0923-0059; Mohos, Violetta Karolin/0000-0001-6248-060X; Lemli, Beáta/0000-0001-8903-1337; Deme, Ruth/0000-0002-0798-6912; Bogdán, Dóra/0000-0003-4455-8914; Czompa, Andrea/0000-0001-8442-8554; Mátyus, Péter/0000-0003-3963-9445}
}

@article{MTMT:30612672,
	title = {Interaction of amphotericin B with human and bovine serum albumins: a fluorescence polarization study},
	url = {https://m2.mtmt.hu/api/publication/30612672},
	author = {Derdák, Diána and Poór, Miklós and Kunsági-Máté, Sándor and Lemli, Beáta},
	doi = {10.1016/j.cplett.2019.03.049},
	journal-iso = {CHEM PHYS LETT},
	journal = {CHEMICAL PHYSICS LETTERS},
	volume = {724},
	unique-id = {30612672},
	issn = {0009-2614},
	year = {2019},
	eissn = {1873-4448},
	pages = {13-17},
	orcid-numbers = {Lemli, Beáta/0000-0001-8903-1337}
}

@article{MTMT:30319045,
	title = {Interaction of the mycotoxin metabolite dihydrocitrinone with serum albumin},
	url = {https://m2.mtmt.hu/api/publication/30319045},
	author = {Faisal, Anna Zelma and Vörös, Virág and Lemli, Beáta and Derdák, Diána and Kunsági-Máté, Sándor and Bálint, Mónika Enikő and Hetényi, Csaba and Jakabfi-Csepregi, Rita and Kőszegi, Tamás and Bergmann, Dominik and Sueck, Franziska and Humpf, Hans-Ulrich and Hübner, Florian and Poór, Miklós},
	doi = {10.1007/s12550-018-0336-z},
	journal-iso = {MYCOTOX RES},
	journal = {MYCOTOXIN RESEARCH},
	volume = {35},
	unique-id = {30319045},
	issn = {0178-7888},
	abstract = {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.},
	keywords = {Serum Albumin; Fluorescence spectroscopy; citrinin; albumin-ligand interaction; Dihydrocitrinone},
	year = {2019},
	eissn = {1867-1632},
	pages = {129-139},
	orcid-numbers = {Lemli, Beáta/0000-0001-8903-1337}
}

@CONFERENCE{MTMT:30699187,
	title = {Ochratoxin A és 2'R-Ochratoxin A kölcsönhatásainak vizsgálata szérum albuminnal},
	url = {https://m2.mtmt.hu/api/publication/30699187},
	author = {Faisal, Anna Zelma and Vörös, Virág and Derdák, Diána and Lemli, Beáta and Bálint, Mónika Enikő and Hetényi, Csaba and Jakabfi-Csepregi, Rita and Sueck, Franziska and Humpfg, Hans-Ulrich and Cramer, Benedikt and Poór, Miklós},
	booktitle = {TOX'2018 Tudományos Konferencia Program, kivonatok},
	unique-id = {30699187},
	year = {2018},
	pages = {48-48},
	orcid-numbers = {Lemli, Beáta/0000-0001-8903-1337}
}

@misc{MTMT:30613515,
	title = {Ochratoxin A és 2’R-Ochratoxin A kölcsönhatásainak vizsgálata szérum albuminnal},
	url = {https://m2.mtmt.hu/api/publication/30613515},
	author = {Faisal, Anna Zelma and Vörös, Virág and Derdák, Diána and Lemli, Beáta and Bálint, Mónika Enikő and Hetényi, Csaba and Jakabfi-Csepregi, Rita and Sueck, Franziska and Humpf, Hans-Ulrich and Cramer, Benedikt and Poór, Miklós},
	unique-id = {30613515},
	year = {2018},
	orcid-numbers = {Lemli, Beáta/0000-0001-8903-1337}
}

@article{MTMT:3408877,
	title = {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},
	url = {https://m2.mtmt.hu/api/publication/3408877},
	author = {Faisal, Anna Zelma and Derdák, Diána and Lemli, Beáta and Kunsági-Máté, Sándor and Bálint, Mónika Enikő and Hetényi, Csaba and Jakabfi-Csepregi, Rita and Kőszegi, Tamás and Sueck, Franziska and Cramer, Benedikt and Humpf, Hans-Ulrich and Poór, Miklós},
	doi = {10.3390/toxins10090353},
	journal-iso = {TOXINS},
	journal = {TOXINS},
	volume = {10},
	unique-id = {3408877},
	issn = {2072-6651},
	abstract = {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.},
	keywords = {ochratoxin A; Serum Albumin; 2′R-ochratoxin A; albumin-ligand interaction; cellular toxicity; species differences},
	year = {2018},
	eissn = {2072-6651},
	orcid-numbers = {Lemli, Beáta/0000-0001-8903-1337}
}

@article{MTMT:3401784,
	title = {Noncovalent Interaction of Tilmicosin with Bovine Serum Albumin.},
	url = {https://m2.mtmt.hu/api/publication/3401784},
	author = {Lemli, Beáta and Derdák, Diána and Laczay, P and Kovacs, D and Kunsági-Máté, Sándor},
	doi = {10.3390/molecules23081915},
	journal-iso = {MOLECULES},
	journal = {MOLECULES},
	volume = {23},
	unique-id = {3401784},
	issn = {1420-3049},
	abstract = {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.},
	keywords = {BINDING; LIQUID-CHROMATOGRAPHY; DSC; milk; Fluoroquinolones; Veterinary drug; Biochemistry & Molecular Biology; macrolide antibiotic; albumin-drug interaction; binding properties; THERMAL-DENATURATION},
	year = {2018},
	eissn = {1420-3049},
	orcid-numbers = {Lemli, Beáta/0000-0001-8903-1337}
}

@CONFERENCE{MTMT:30699198,
	title = {Dihidrocitrinon kölcsönhatásának vizsgálata szérum albuminnal},
	url = {https://m2.mtmt.hu/api/publication/30699198},
	author = {Vörös, Virág and Faisal, Anna Zelma and Derdák, Diána and Lemli, Beáta and Bálint, Mónika Enikő and Hetényi, Csaba and Jakabfi-Csepregi, Rita and Poór, Miklós},
	booktitle = {TOX'2018 Tudományos Konferencia Program, kivonatok},
	unique-id = {30699198},
	year = {2018},
	pages = {140-140},
	orcid-numbers = {Lemli, Beáta/0000-0001-8903-1337}
}

@misc{MTMT:30613550,
	title = {Dihidrocitrinon kölcsönhatásának vizsgálata szérum albuminnal},
	url = {https://m2.mtmt.hu/api/publication/30613550},
	author = {Vörös, Virág and Faisal, Anna Zelma and Derdák, Diána and Lemli, Beáta and Bálint, Mónika Enikő and Hetényi, Csaba and Jakabfi-Csepregi, Rita and Poór, Miklós},
	unique-id = {30613550},
	year = {2018},
	orcid-numbers = {Lemli, Beáta/0000-0001-8903-1337}
}