Supplementary data for article: Cvijetić, I.; Vitorović-Todorović, M. D.; Juranić, I. O.; Drakulić, B. J. Reactivity of (E)-4-Aryl-4-Oxo-2-Butenoic Acid Arylamides toward 2-Mercaptoethanol. A LFER Study. Monatshefte Fur Chemie 2013, 144 (12), 1815–1824. https://doi.org/10.1007/s00706-013-1084-6

Supplementary material for: [https://doi.org/10.1007/s00706-013-1084-6]Related to published version: [http://cherry.chem.bg.ac.rs/handle/123456789/1441

Supplementary data for the article: Vitorović-Todorović, M. D.; Koukoulitsa, C.; Juranić, I. O.; Mandić, L. M.; Drakulić, B. J. Structural Modifications of 4-Aryl-4-Oxo-2-Aminylbutanamides and Their Acetyl- and Butyrylcholinesterase Inhibitory Activity. Investigation of AChE-Ligand Interactions by Docking Calculations and Molecular Dynamics Simulations. European Journal of Medicinal Chemistry 2014, 81, 158–175. https://doi.org/10.1016/j.ejmech.2014.05.008

Supplementary material for: [https://doi.org/10.1016/j.ejmech.2014.05.008]Related to published version: [http://cherry.chem.bg.ac.rs/handle/123456789/1808]Related to accepted version:[http://cherry.chem.bg.ac.rs/handle/123456789/2907

Human Serum Albumin Binding of 2-[(Carboxymethyl)sulfanyl]-4-oxo-4-(4-tert-butylphenyl)butanoic Acid and its Mono-Me Ester

Interactions of 2-[(carboxymethyl)sulfanyl]-4-oxo-4-(4-tert-butylphenyl)butanoic acid (compound 1) and its mono-Me ester (compound 2) with the human serum albumin (HSA) have been studied by fluorescence spectroscopy. Comp. 1 exerts antiproliferative activity toward human tumor cells and significant selectivity (tumor vs. healthy cells) in vitro. Competitive binding study with warfarin and ibuprofen as binding site probes, revealed that one molecule of comp. 1 selectively binds to HSA Sudlow site I (warfarin site) with moderate binding constant (Kb = (2.8 ± 0.5) x 104 M-1 at 37 ± 1 oC), while comp. 2 binds to Sudlow site II (Kb = (3.2 ± 0.9) x 104 M-1 at 37 ± 1 oC). Fluorescence quenching at different temperatures was analyzed using classical Stern-Volmer equation, and a static quenching mechanism was proposed. Energy resonance transfer between HSA and comp. 1 was examined according to Förster’s non-radiative energy transfer theory. Distance of about 10 Å between ligand and Trp214 (HSA) was obtained. Docking studies confirmed HSA Sudlow site I as a preferable comp. 1 binding site, and Sudlow site II as comp. 2 binding site. Molecular dynamics simulations proved the stability of comp. 1/HSA complex

Supplementary data for the article: Cvijetić, I. N.; Tanç, M.; Juranić, I. O.; Verbić, T. Ž.; Supuran, C. T.; Drakulić, B. J. 5-Aryl-1H-Pyrazole-3-Carboxylic Acids as Selective Inhibitors of Human Carbonic Anhydrases IX and XII. Bioorganic and Medicinal Chemistry 2015, 23 (15), 4649–4659. https://doi.org/10.1016/j.bmc.2015.05.052

Supplementary material for: [https://doi.org/10.1016/j.bmc.2015.05.052]Related to published version: [http://cherry.chem.bg.ac.rs/handle/123456789/1742]Related to accepted version: [http://cherry.chem.bg.ac.rs/handle/123456789/3327

Antiferromagnetic Excitations and Van Hove Singularities in YBa2_2Cu3_3O6+x_{6+x}

We show that in quasi-two-dimensional $d$-wave superconductors Van Hove singularities close to the Fermi surface lead to novel magnetic quasi-particle excitations. We calculate the temperature and doping dependence of dynamical magnetic susceptibility for YBCO and show that the proposed excitations are in agreement with inelastic neutron scattering experiments. In addition, the values of the gap parameter and in-plane antiferromagnetic coupling are much smaller than usually believed.Comment: REVTeX, 4 pages + 3 PostScript (compressed) figures; to appear in Phys. Rev. B (Rap. Comm.