TY - CHAP AU - Domonkos, Celesztina Diána AU - Zsila, F AU - Fitos, Ilona AU - Benéné Visy, Júlia ED - Magyar, Kémikusok Egyesülete TI - Evodiamin szérumfehérje kötődésének vizsgálata T2 - Vegyészkonferencia 2013 PB - Magyar Kémikusok Egyesülete (MKE) CY - Budapest SN - 9789639970366 PY - 2013 UR - https://m2.mtmt.hu/api/publication/2595161 ID - 2595161 LA - Hungarian DB - MTMT ER - TY - CHAP AU - Németh, K AU - Domonkos, Celesztina Diána AU - Szemán, Julianna AU - Mallareddy, J R AU - Sarnyai, V AU - Tóth, G AU - Jicsinszky, L AU - Szente, Lajos AU - Péter, Antal AU - Benéné Visy, Júlia ED - Kilár, Ferenc ED - Nagy, Laura ED - Kiss, Ibolya TI - Stereoselective analysis of amino acids and endomorphin analogue tetrapeptides by CE T2 - CECE 2013 10th International Interdisciplinary Meeting on Bioanalysis PB - University of Pécs CY - Pécs SN - 9789636425173 PY - 2013 SP - 80 EP - 80 PG - 1 UR - https://m2.mtmt.hu/api/publication/2594314 ID - 2594314 LA - English DB - MTMT ER - TY - JOUR AU - Domonkos, Celesztina Diána AU - Fitos, Ilona AU - Benéné Visy, Júlia AU - Zsila, Ferenc TI - Fatty acid modulated human serum albumin binding of the β-carboline alkaloids norharmane and harmane JF - MOLECULAR PHARMACEUTICS J2 - MOL PHARM VL - 10 PY - 2013 IS - 12 SP - 4706 EP - 4716 PG - 11 SN - 1543-8384 DO - 10.1021/mp400531n UR - https://m2.mtmt.hu/api/publication/2446448 ID - 2446448 AB - Harmane and norharmane are representative members of the large group of natural β-carboline alkaloids featured with diverse pharmacological activities. In blood, these agents are transported by human serum albumin (HSA) which has a profound impact on the pharmacokinetic and pharmacodynamic properties of many therapeutic drugs and xenobiotics. By combination of various spectroscopic methods, the present contribution is aimed to elucidate how non-esterified fatty acids (FAs), the primary endogenous ligands of HSA, affect the binding properties of harmane and norharmane. Analysis of induced circular dichroism (CD) and fluorescence spectroscopic data indicates the inclusion of the neutral form of both molecules into the binding pocket of subdomain IIIA, which hosts two FA binding sites, too. The induced CD and UV absorption spectra of harmane and norharmane exhibit peculiar changes upon addition of FAs suggesting the formation of ternary complexes in which the lipid ligands significantly alter the binding mode of the alkaloids via cooperative allosteric mechanism. To our knowledge, it is the first instance of the demonstration of drug-FA co-binding at site IIIA. In line with these results, molecular docking calculations showed two distinct binding positions of norharmane within subdomain IIIA. The profound increase in the affinity constants of β-carbolines estimated in the presence of FAs predicts that the unbound, pharmacologically active serum fraction of these compounds strongly depends on the actual lipid binding profile of HSA. LA - English DB - MTMT ER - TY - JOUR AU - Zsila, Ferenc TI - Circular dichroism spectroscopic detection of ligand binding induced subdomain IB specific structural adjustment of human serum albumin JF - JOURNAL OF PHYSICAL CHEMISTRY B J2 - J PHYS CHEM B VL - 117 PY - 2013 IS - 37 SP - 10798 EP - 10806 PG - 9 SN - 1520-6106 DO - 10.1021/jp4067108 UR - https://m2.mtmt.hu/api/publication/2391104 ID - 2391104 AB - This work demonstrates for the first time that binding of various compounds within subdomain IB of human serum albumin (HSA) provokes characteristic changes in the near-UV circular dichroism (CD) spectrum of the protein. It can be inferred from the spectroscopic features of difference ellipticity signals and from CD displacement experiments that tyrosine residues located in subdomain IB are the source of the observed spectral alterations. It is proposed that inclusion of some ligand molecules (bile acids, dehydroepiandrosterone sulfate, steroidal terpenes, fatty acids, ibuprofen, and gemfibrozil) into the pocket of subdomain IB disrupts the Tyr138?Tyr161 interhelical π?π stacking interaction, which is reflected in the CD spectrum. This phenomenon can be utilized for the CD detection of subdomain IB specific binding of endo- as well as exogenous agents and to study the drug binding associated local conformational adaptation of the HSA molecule. LA - English DB - MTMT ER - TY - JOUR AU - Zsila, Ferenc TI - Subdomain IB is the third major drug binding region of human serum albumin: Toward the three-sites model. JF - MOLECULAR PHARMACEUTICS J2 - MOL PHARM VL - 10 PY - 2013 IS - 5 SP - 1668 EP - 1682 PG - 15 SN - 1543-8384 DO - 10.1021/mp400027q UR - https://m2.mtmt.hu/api/publication/2229453 ID - 2229453 AB - According to the conventional view, noncovalent association of small molecules with human serum albumin (HSA) occurs principally at the so-called Sudlow’s sites located in subdomain IIA and IIIA. By employing a circular dichroism (CD) spectroscopic approach, it is shown that biliverdin is the specific CD label of an additional drug binding area in subdomain IB. CD competition experiments disclosed the entrapment of a diverse assortment of acidic, neutral, and basic molecules within subdomain IB including anticancer agents (camptothecin, doxorubicin, daunorubicin, teniposide, suramin, tyrosine kinase inhibitors), anticoagulants (dicoumarol), various steroids (bile acids, carbenoxolone), nonsteroidal antiinflammatory drugs, natural substances (aristolochic acid, glycyrrhetinic acid), and synthetic dyes (methyl orange, azocarmine B). These finding imply that subdomain IB can be considered as the third major drug binding region of HSA featured with promiscuous ligand recognition ability. Additionally, subdomain IB is allosterically coupled with the Sudlow’s sites, the ligand binding of which is shown to alter the HSA binding mode and affinity of biliverdin and hemin. Brief case studies are presented to illustrate how the evaluation of spectral changes of tetrapyrrole CD probes gains new insight into the HSA binding properties of endogenous as well as pharmaceutical compounds. LA - English DB - MTMT ER - TY - CONF AU - Domonkos, Celesztina Diána AU - Fitos, Ilona AU - Zsila, F AU - Németh, Krisztina AU - Benéné Visy, Júlia ED - Majdik, Cornelia TI - β-Karbolin származékok szérumfehérje kötődésének vizsgálata. Serum Protein Binding Study of Β-Carboline Derivatives TS - Serum Protein Binding Study of Β-Carboline Derivatives T2 - XVIII. Nemzetközi Vegyészkonferencia PB - Erdélyi Magyar Műszaki Tudományos Társaság (EMT) C1 - Kolozsvár T3 - Nemzetközi Vegyészkonferencia, ISSN 1843-6293 PY - 2012 SP - n EP - nn PG - 1 UR - https://m2.mtmt.hu/api/publication/2595138 ID - 2595138 LA - Hungarian DB - MTMT ER - TY - CHAP AU - Domonkos, Celesztina Diána AU - Fitos, Ilona AU - Zsila, F AU - Németh, Krisztina AU - Benéné Visy, Júlia ED - Tóth, Á TI - β-Karbolin származékok szérumfehérje kötődésének vizsgálata T2 - Kálmán Erika Doktori Konferencia 2012 PB - MTA Természettudományi Kutatóközpont CY - Budapest SN - 9789635086245 PY - 2012 SP - 22 EP - 23 PG - 2 UR - https://m2.mtmt.hu/api/publication/2595114 ID - 2595114 LA - Hungarian DB - MTMT ER - TY - CHAP AU - Domonkos, Celesztina Diána AU - Fitos, Ilona AU - Zsila, F AU - Németh, K AU - Benéné Visy, Júlia ED - Tóth, Á TI - SERUM PROTEIN BINDING STUDY OF β -CARBOLINE DERIVATIVES T2 - Kálmán Erika Doktori Konferencia 2012 PB - MTA Természettudományi Kutatóközpont CY - Budapest SN - 9789635086245 PY - 2012 SP - 23 EP - 23 PG - 1 UR - https://m2.mtmt.hu/api/publication/2594308 ID - 2594308 LA - English DB - MTMT ER - TY - CONF AU - Magda, Balázs AU - Tóth, Katalin AU - Temesvári, Manna AU - Monostory, Katalin AU - Szabó, Pál Tamás TI - Valproát és metabolitjai vérszintjének meghatározása LC-MS/MS technikával T2 - TOX'2012 Tudományos Konferencia, Magyar toxikológusok társasága PY - 2012 UR - https://m2.mtmt.hu/api/publication/2521076 ID - 2521076 LA - Hungarian DB - MTMT ER - TY - JOUR AU - Varga, G AU - Fodor, G AU - Ilisz, István AU - Szemán, Julianna AU - Benéné Visy, Júlia AU - Szente, Lajos AU - Péter, Antal TI - Comparison of separation performances of novel β-cyclodextrin-based chiral stationary phases in high-performance liquid chromatographic enantioseparation JF - JOURNAL OF PHARMACEUTICAL AND BIOMEDICAL ANALYSIS J2 - J PHARMACEUT BIOMED ANAL VL - 70 PY - 2012 SP - 71 EP - 76 PG - 6 SN - 0731-7085 DO - 10.1016/j.jpba.2012.05.023 UR - https://m2.mtmt.hu/api/publication/2067021 ID - 2067021 AB - Three β-cyclodextrin-based chiral stationary phases were developed applying novel bonding chemistry. The separation performances of β-cyclodextrin, (R,S)-2-hydroxypropyl-β-cyclodextrin, and permethyl-β-cyclodextrin-based CSPs were compared in the resolution of structurally divergent analytes, such as coumarins, dansyl amino acids, and propionic acid derivatives. Separations were carried out in reversed phase mode applying 0.1% triethylammonium phosphate (pH 3.5)/MeOH mobile phase systems in different compositions. Of the three novel CSPs the permethyl-β-cyclodextrin bonded phase proved to be the most effective one for the enantioseparation of investigated analytes. © 2012. LA - English DB - MTMT ER -