Ratomir Jelic

Scopus Publications

Unraveling the binding mechanism of olanzapine with human serum transferrin: a multispectroscopic and computational investigation
Aleksandar Djurović, Emina Mrkalić, Žiko Milanović, Marina Ćendić Serafinović, Jadranka Odović, et al.
Molecular Diversity, 2026
In Vitro Pharmacokinetic Profiling of Thiourea Derivatives of Naproxen With Anti-Inflammatory and Anticancer Activity
Nikola Nedeljković, Vladimir Dobričić, Marina Vesović, Ratomir Jelić, Bojan Marković, et al.
Chemistry and Biodiversity, 2026
Pharmacokinetic deficiencies account for nearly 40% of clinical drug candidate failures, emphasising the importance of early in vitro evaluation. Following the 3Rs principle, this study assessed the in vitro pharmacokinetic properties of thiourea derivatives of naproxen ( 1 – 14 ). Permeability assessment using the parallel artificial membrane permeability assay method revealed that derivatives 4 (‐logPe = 4.13, p = 0.0859) and 7 (‐logPe = 3.94, p = 0.2291) exhibited the highest passive gastrointestinal absorption potential, comparable to naproxen. Evaluation of binding affinity to human serum albumin (HSA) using the high‐performance affinity chromatography method identified two groups of compounds: high‐binding aromatic amine derivatives (except derivative 5 ) and low‐binding aromatic amino acid ester derivatives. Microsomal stability assays indicated that compound 7 underwent the most extensive metabolic degradation (65.83% decrease). These findings suggest that further structural optimisation of compound 7 , such as esterification with higher or branched alcohols, should lead to the improvement of HSA binding and reduction of metabolic susceptibility. Conversely, compound 4 combines favorable biological activity with a pharmacokinetic profile closely resembling that of naproxen. Although limited by the exclusive use of in vitro models and the absence of in vivo validation, this study provides valuable insights for the rational design of naproxen‐based thiourea derivatives with enhanced anti‐inflammatory and anticancer potential.
Potentiometric titration, biomolecular interactions, and docking insights of N-heterocyclic carbene gold(I) complexes derived from the marine betaine 1,3-dimethylimidazolium-4-carboxylate
Seyedeh Mahbobeh Mahdavi, Angelina Z. Caković, Dušan Ćoćić, Snezana Jovanovic-Stević, Ratomir Jelić, et al.
Journal of Coordination Chemistry, 2026
Analysis of the Lipophilicity and HSA Binding Profile of Biologically Relevant 2-Mercaptobenzoic Acid Derivatives
Miloš Nikolić, Ratomir Jelić, Nikola Nedeljković, Marina Vesović, Gordana Radić, et al.
Chemistry and Biodiversity, 2025
One of the key factors determining a compound's distribution, metabolism, and therapeutic properties is its binding affinity to human serum albumin (HSA). This study investigated the binding interaction between potential biologically active S‐alkyl (methyl‐[L1], ethyl‐[L2], propyl‐[L3], butyl‐[L4], and benzyl‐[L5]) derivatives of 2‐mercaptobenzoic acid and HSA using various spectroscopic methods and molecular docking simulations. The protonation constants (βn) of the investigated ligands were determined potentiometrically in aqueous solutions, whereas their lipophilicity was assessed using different experimental methods and software packages. An increase in the absorption intensity of HSA upon interaction with the investigated compounds indicates static quenching and the formation of a complex between HSA and the ligands. The incorporation of alkyl groups into the ligand molecules results in a slight increase in the protonation constants of the tested compounds, as well as an enhancement lipophilicity compared to 2‐mercaptobenzoic acid. In silico analyses demonstrated that multiple amino acid residues are crucial for the binding process in Sudlow site I, situated within subdomain IIA, with salt bridges being the predominant interaction.
Quercetin, Catechin, and Diosmin as Modulators of Haloperidol–HSA Interactions: A Biophysical and Computational Study
Aleksandar Petrušić, Emina Mrkalić, Ratomir Jelić, Aleksandar Kočović, Miloš Milosavljević, et al.
International Journal of Molecular Sciences, 2025
Potential interactions of haloperidol with food ingredients such as flavonoids may be of great importance both for understanding the pharmacokinetic interactions of xenobiotics with human serum albumin and for clinical practice itself. In this study, the effect of the flavonoids quercetin, catechin, and diosmin on the interaction of haloperidol and human serum albumin was examined. These flavonoids are very common in foods of plant origin. Haloperidol is a typical antipsychotic that has a pronounced binding affinity for human serum albumin. Fluorescence spectroscopy, molecular docking analysis, and molecular dynamics simulations were used for these tests. Previous studies have shown that all test substances bind to the same binding site on human serum albumin (Sudlow site I, Subdomain IIA). Fluorescence spectroscopy revealed that the tested flavonoids reduce the value of the haloperidol binding constant to human serum albumin (from 4.45 × 103 in the binary system to 3.75 × 102, 5.40 × 102 and 6.24 × 102 in the ternary systems, respectively), due to competition for the same binding site. Experimental results were confirmed by molecular docking analysis and molecular dynamics simulations.
The Molecular Recognition of Lurasidone by Human Serum Albumin: A Combined Experimental and Computational Approach
Nevena Živković, Emina Mrkalić, Ratomir Jelić, Jovica Tomović, Jadranka Odović, et al.
Molecules, 2025
Lurasidone (LUR) is an antipsychotic drug whose interaction with human serum albumin (HSA) plays a crucial role in its pharmacokinetic and pharmacodynamic properties. A thorough understanding of LUR’s binding mechanism to HSA is crucial for predicting its transport, distribution, and potential drug interactions. Methods: The interaction between LUR and HSA was investigated using fluorescence and circular dichroism (CD) spectroscopy, followed by molecular docking simulations. Binding characteristics were analyzed through quenching mechanisms, thermodynamic parameters, and competitive site marker experiments. Results: This study revealed a systematic decrease in HSA fluorescence intensity with increasing LUR concentration, indicating a static quenching mechanism driven by non-fluorescent complex formation. Binding constants suggest enhanced complex stability at higher temperatures, with thermodynamic analysis confirming an endothermic, hydrophobic interaction. Competitive site marker assays and synchronous fluorescence spectra confirmed that LUR primarily binds to site I (subdomain IIA) near tryptophan residues. Conformational changes in HSA, observed as a decrease in α-helix content, further demonstrate the structural impact of LUR binding. Conclusions: These findings offer key insights into the molecular interactions between LUR and HSA, enhancing our understanding of LUR’s pharmacokinetics and its potential interactions with other drugs. Understanding these binding characteristics can aid in optimizing LUR’s clinical application and predicting possible interactions with other biomolecules.
Investigation of the interaction between S-isoalkyl derivatives of the thiosalicylic acid and human serum albumin
Marina Vesović, Ratomir Jelić, Miloš Nikolić, Nikola Nedeljković, Ana Živanović, et al.
Journal of Biomolecular Structure and Dynamics, 2025
S-isoalkyl derivatives of thiosalicylic acid (isopropyl-(L1), isobutyl-(L2) and isoamyl-(L3)) were selected in order to investigate the binding interaction with the human serum albumin (HSA) using different spectroscopic methods and molecular docking simulation. Association constants and number of binding sites were used to analyze the quenching mechanism. The experimental results showed that the fluorescence quenching of HSA by L1, L2 and L3 occurs because of static quenching and that binding processes were spontaneous, with the leading forces in bonding by hydrogen bonding, hydrophobic interactions, and electrostatic interactions. Fluorescence spectroscopy, UV-Vis spectroscopy and synchronous fluorescence spectroscopy showed that ligands (L1, L2 and L3) can bind to HSA and that the binding of ligands induced some microenvironmental and conformational changes in HSA. The calculated distance between the donor and the acceptor according to fiFörster's theory confirms the energy transfer efficiency between the acceptor and HSA. Results of site marker competitive experiments showed that the tested compounds bind to HSA in domain IIA (Site I). Molecular dynamics and docking calculations demonstrated that L3 binds to the Sudlow site I of HSA with lower values of binding energies compared to L1 and L2, indicating the formation of the most stable ligand-HSA complex. Understanding the binding mechanisms of S-isoalkyl derivatives of the thiosalicylic acid to HSA may provide valuable data for the future studies of their biological activity and application as potential antitumor drugs.Communicated by Ramaswamy H. Sarma.
Synthesis, comprehensive characterization and investigation of biological properties of newly synthesized Pt(II)-aminothiazole complexes: Combining experimental and computational approach
Danijela Lj. Stojković, Edina H. Avdović, Maja B. Đukić, Verica V. Jevtić, Đorđe S. Petrović, et al.
Journal of Organometallic Chemistry, 2025
Linamarin Binding to Human Serum Albumin. A Spectroscopic and Molecular Docking Approach
Ratomir Jelić, Emina Mrkalić, Marina Ćendić‐Serafinović, Jadranka Odović, Miroslav Sovrlić
Chemistryselect, 2024
The interaction between linamarin (LIN), a cyanogenic glycoside, and human serum albumin (HSA) was studied by multiple spectroscopic techniques and molecular docking simulation. All measurements were performed under physiological conditions. The obtained results (including the binding constants, effective quenching constant and a number of binding sites) showed that the complex of HSA‐LIN is formed. The values of Stern‐Volmer constants (6.70×103, 5.53×103 and 1.95×103) indicate that fluorescence quenching of HSA was static. Results of site marker experiments showed that the binding site of LIN is mainly located in site I (subdomain IIA) of HSA. The thermodynamic parameters showed that binding process occurs spontaneously through hydrophobic interactions. Molecular docking results are in good agreement with experimental data. Furthermore, computational results revealed LIN binds in the cavity of TRP 214, that is, subdomain IIA (site I) of HSA. This comprehensive study provides a deeper insight into ligand binding in HSA which may be useful in drug design and pharmacology.
Exploring heterometallic bridged Pt(II)-Zn(II) complexes as potential antitumor agents
Tanja V. Soldatović, Biljana Šmit, Emina M. Mrkalić, Sanja Lj. Matić, Ratomir M. Jelić, et al.
Journal of Inorganic Biochemistry, 2023
Synthesis, characterization and investigating the binding mechanism of novel coumarin derivatives with human serum albumin: Spectroscopic and computational approach
Edina H. Avdović, Žiko B. Milanović, Krešimir Molčanov, Sunčica Roca, Dražen Vikić-Topić, et al.
Journal of Molecular Structure, 2022
Effect of Caffeine and Flavonoids on the Binding of Tigecycline to Human Serum Albumin: A Spectroscopic Study and Molecular Docking
Miroslav Sovrlić, Emina Mrkalić, Ratomir Jelić, Marina Ćendić Serafinović, Stefan Stojanović, et al.
Pharmaceuticals, 2022
Synthesis, characterization, HSA/DNA binding, cytotoxicity study, and antimicrobial activity of new palladium(II) complexes with some esters of (S,S)-propylenediamine-N,N'-di-2-(3-methyl)butanoic acid
Đorđe S. Petrović, Sandra S. Jovičić Milić, Maja B. Đukić, Ivana D. Radojević, Ratomir M. Jelić, et al.
Inorganica Chimica Acta, 2021
Interaction between olanzapine and human serum albumin and effect of metal ions, caffeine and flavonoids on the binding: A spectroscopic study
Emina Mrkalić, Ratomir Jelić, Stefan Stojanović, Miroslav Sovrlić
Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy, 2021
INFLUENCE OF THE CAFFEINE ON THE INTERACTION BETWEEN HALOPERIDOL AND HUMAN SERUM ALBUMIN: SPECTROSCOPIC AND MOLECULAR DOCKING APPROACH
Sovrlic Miroslav, Jelic Ratomir, Antonijevic Marko, Markovic Zoran, Tomovic Jovica, et al.
Studia Universitatis Babes Bolyai Chemia, 2021
Synthesis, characterization, HSA/DNA interactions and antitumor activity of new [Ru(η6-p-cymene)Cl2(L)] complexes
Maja B. Đukić, Marija S. Jeremić, Ignjat P. Filipović, Olivera R. Klisurić, Vesna V. Kojić, et al.
Journal of Inorganic Biochemistry, 2020
Homo- And hetero-dinuclear Pt(ii)/Pd(ii) complexes: Studies of hydrolysis, nucleophilic substitution reactions, DNA/BSA interactions, DFT calculations, molecular docking and cytotoxic activity
Dušan Ćoćić, Snežana Jovanović-Stević, Ratomir Jelić, Sanja Matić, Suzana Popović, et al.
Dalton Transactions, 2020
Ruthenium(II) Complexes of Isothiazole Ligands: Crystal Structure, HSA/DNA Interactions, Cytotoxic Activity and Molecular Docking Simulations
Maja B. Djukić, Marija S. Jeremić, Ignjat P. Filipović, Olivera R. Klisurić, Ratomir M. Jelić, et al.
Chemistryselect, 2020
Spectroscopic studies on the drug–drug interaction: the influence of fluoroquinolones on the affinity of tigecycline to human serum albumin and identification of the binding site
Stefan D. Stojanović, Jovan M. Nićiforović, Sandra M. Živanović, Jadranka V. Odović, Ratomir M. Jelić
Monatshefte Fur Chemie, 2020
Rhodium(III) in a cage of the 1,3-propanediamine-N,N,N′-triacetate chelate: X-ray structure, solution equilibria, computational study and biological behavior
Marija S. Jeremić, Marko D. Radovanović, Franco Bisceglie, Vesna V. Kojić, Ratomir Jelić, et al.
Polyhedron, 2018
Interaction of haloperidol with human serum albumin and effect of metal ions on the binding
Jelena D. Berić, Stefan D. Stojanović, Emina M. Mrkalić, Zoran D. Matović, Dragan R. Milovanović, et al.
Monatshefte Fur Chemie, 2018
Further insights into ruthenium(II) piano-stool complexes with N-alkyl imidazoles
Maja Djukić, Marija S. Jeremić, Ratomir Jelić, Olivera Klisurić, Vesna Kojić, et al.
Inorganica Chimica Acta, 2018
Prevalence of prolonged qtc interval in patients taking psychopharmacs
Zoran Jovanovic, Vesela Radonjic, Ratomir Jelic, Narcisa Petrovic-Subic, Ivan Soldatovic, et al.
Serbian Journal of Experimental and Clinical Research, 2018
The effect of tigecycline on the binding of fluoroquinolones to human serum albumin
Ratomir M. Jelic, Stefan D. Stojanovic, Jelena D. Beric, Jadranka Odovic
Serbian Journal of Experimental and Clinical Research, 2018
Stereospecific ligands and their complexes. XXIV. Synthesis, characterization and some biological properties of Pd(II) and Pt(II) complexes with R2-: S, S -eddtyr
Danijela Lj. Stojković, Verica V. Jevtić, Gordana P. Radić, Maja B. Đukić, Ratomir M. Jelić, et al.
New Journal of Chemistry, 2018
The evaluation of angiotensin-converting enzyme inhibitors in renal elimination with selected molecular descriptors
Jovana Trbojevic, Jadranka Odovic, Jasna Trbojevic-Stankovic, Biljana Stojimirovic, Ratomir Jelic
Serbian Journal of Experimental and Clinical Research, 2017
Assessment of the relationship between the molecular properties of calcium channel blockers and plasma protein binding data
Jadranka Odovic, Jovana Trbojevic, Jasna Trbojevic-Stankovic, Dejan Nesic, Ratomir Jelic
Archives of Biological Sciences, 2017
Estimation of plasma protein binding of selected antipsychotics using computed molecular properties
Jelena Beric, Ratomir Jelic, Dejan Nesic, Jasna Trbojevic-Stankovic, Jadranka Odovic
Archives of Biological Sciences, 2017
Synthesis, structural analysis, solution equilibria and biological activity of rhodium(III) complexes with a quinquedentate polyaminopolycarboxylate
Marija S. Jeremić, Hubert Wadepohl, Vesna V. Kojić, Dimitar S. Jakimov, Ratomir Jelić, et al.
Rsc Advances, 2017
Synthesis and characterisation of bismacrocyclic DO3A-amide derivatives - An approach towards metal-responsive PARACEST agents
Nevenka Cakić, Tatjana Ž. Verbić, Ratomir M. Jelić, Carlos Platas-Iglesias, Goran Angelovski
Dalton Transactions, 2016
Relationship between the bioavailability and molecular properties of angiotensin II receptor antagonists
Jovana Trbojevic, Jadranka Odovic, Jasna Trbojevic-Stankovic, Dejan Nesic, Ratomir Jelic
Archives of Biological Sciences, 2016
Study of inclusion complex of β-cyclodextrin and levofloxacin and its effect on the solution equilibria between gadolinium(III) ion and levofloxacin
Ratomir Jelić, Marina Tomović, Stefan Stojanović, Ljubinka Joksović, Ivan Jakovljević, et al.
Monatshefte Fur Chemie, 2015
Interaction between tigecycline and human serum albumin in aqueous solution
Stefan D. Stojanović, Slobodan M. Janković, Zoran D. Matović, Ivan Ž. Jakovljević, Ratomir M. Jelić
Monatshefte Fur Chemie, 2015
The influence of certain molecular descriptors of fecal elimination of angiotensin II receptor antagonists
Jasna Trbojevic-Stankovic, Jadranka Odovic, Ratomir Jelic, Dejan Nesic, Biljana Stojimirovic
Archives of Biological Sciences, 2015
The effect of the molecular properties of calcium channel blockers on their elimination route
Jasna Trbojevic-Stankovic, Jadranka Odovic, Ratomir Jelic, Dejan Nesic, Biljana Stojimirovic
Archives of Biological Sciences, 2015
Synthesis of novel palladium(ii) complexes with oxalic acid diamide derivatives and their interaction with nucleosides and proteins. Structural, solution, and computational study
Emina M. Mrkalić, Ratomir M. Jelić, Olivera R. Klisurić, Zoran D. Matović
Journal of the Chemical Society Dalton Transactions, 2014
Kinetics, mechanism, and equilibrium studies of the reactions between a ruthenium(II) complex and some nitrogen- and sulfur-donor nucleophiles
Aleksandar M. Mijatović, Ratomir M. Jelić, Jovana Bogojeski, Živadin D. Bugarčić, Biljana Petrović
Monatshefte Fur Chemie, 2013
Configurational, LFDFT and NBO analysis of chromium(III) complexes of edta-type ligands
Zoran D. Matović, Marija S. Jeremić, Ratomir M. Jelić, Matija Zlatar, Ivan Ž. Jakovljević
Polyhedron, 2013
Antitumor effects of a tetradentate amido-carboxylate ligands and corresponding square-planar palladium(II) complexes toward some cancer cells. Crystal structure, DFT modeling and ligand to DNA probe Docking simulation
Zoran D. Matović, Emina Mrkalić, Gordana Bogdanović, Vesna Kojić, Auke Meetsma, et al.
Journal of Inorganic Biochemistry, 2013
HPLC Analysis, antimicrobial and antioxidant activities of Daphne cneorum L
Nedeljko Manojlovic, Pavle Maskovic, Perica Vasiljevic, Ratomir Jelic, Marina Juskovic, et al.
Hemijska Industrija, 2012
Equilibrium studies between some transition metal ions and Me 6[14]dieneN 4 ligand
Ratomir Jelić, Enisa Selimović, Radivoje Nikolić, Živadin D. Bugarčić, Jovana Bogojeski
Monatshefte Fur Chemie, 2012
Equilibrium studies on complex formation reactions of dichlorido[(R,R)- trans-1,2-diaminocyclohexane]platinum(II) complex with ligands of biological significance
Ratomir Jelić, Smiljana Marković, Biljana Petrović
Monatshefte Fur Chemie, 2011
Antiproliferative activity and QSAR studies of a series of new 4-aminomethylidene derivatives of some pyrazol-5-ones
Violeta Marković, Slavica Erić, Tatjana Stanojković, Nevenka Gligorijević, Sandra Aranđelović, et al.
Bioorganic and Medicinal Chemistry Letters, 2011
Equilibrium studies of the reactions of palladium(ii) bis(imidazolin-2- imine) complexes with biologically relevant nucleophiles. the crystal structures of [(TLtBu)PdCl]ClO4 and [(BLiPr)PdCl 2]
Jovana Bogojeski, Ratomir Jelić, Dejan Petrović, Eberhardt Herdtweck, Peter G. Jones, et al.
Dalton Transactions, 2011
Study of solution equilibria between gadolinium(III) ion and moxifloxacin
Acta Chimica Slovenica, 2010
Complexes of hydroxy(thio)pyrone and hydroxy(thio)pyridinone with Zn(II) and Mo(VI). Thermodynamic stability and insulin-mimetic activity
Sílvia Chaves, Ratomir Jelic, Catarina Mendonça, Marta Carrasco, Yutaka Yoshikawa, et al.
Metallomics, 2010
Equilibrium and 1H NMR kinetic study of the reactions of dichlorido [S-methyl-L-cysteine(N,S)]platinum(II) complex with some relevant biomolecules
Tanja Soldatović, Predrag Čanović, Radivoje Nikolić, Ratomir Jelić, Živadin D. Bugarčić
Journal of Solution Chemistry, 2009
Acid-base equilibria of the Zn(II) and Fe(III) complexes with condensation products of 2-acetylpyridine and the dihydrazide of oxalic and malonic acid
Branka Drazic, Gordana Popovic, Ratomir Jelic, Dusan Sladic, Dragana Mitic, et al.
Journal of the Serbian Chemical Society, 2009
Biologically relevant O,S-donor compounds. Synthesis, molybdenum complexation and xanthine oxidase inhibition
Sílvia Chaves, Marco Gil, Sónia Canário, Ratomir Jelic, Maria João Romão, et al.
Dalton Transactions, 2008
Determination of moxifloxacin in human plasma by derivative UV spectrophotometry in a micellar medium
Canadian Journal of Analytical Sciences and Spectroscopy, 2007
Solution equilibria between aluminum(III) ion and some fluoroquinolone family members. Spectroscopic and potentiometric study
Predrag Djurdjević, Ljubinka Joksović, Ratomir Jelić, Aleksandra Djurdjević, Milena Jelikić Stankov
Chemical and Pharmaceutical Bulletin, 2007
Potentiometric and multinuclear magnetic resonance study of the solution equilibria between aluminium(III) ion and L-aspartic acid
Predrag Djurdjević, Ratomir Jelić, Ljubinka Joksović, Mirjana Cvijović
Monatshefte Fur Chemie, 2006
Potentiometric study of the effect of sodium dodecylsulfate and dioxane on the hydrolysis of the aluminum(III) ion
Ratomir M. Jelić, Ljubinka G. Joksović, Predrag T. Djurdjević
Journal of Solution Chemistry, 2005
Equilibrium, kinetic and HPLC study of the reactions between platinum(II) complexes and DNA constituents in the presence and absence of glutathione
Živadin D. Bugarčić, Tanja Soldatović, Ratomir Jelić, Berta Algueró, Anna Grandas
Dalton Transactions, 2004
Hydrolysis of [Pt(dien)H2O]2+ and [Pd(dien)H2O]2+ complexes in water
Živadin D. Bugarčić, Biljana V. Petrović, Ratomir Jelić
Transition Metal Chemistry, 2001
Solution equilibria between aluminum(III) ion and L-histidine or L-tyrosine
Predrag Djurdjevic, Ratomir Jelic, Dragana Dzajevic, Mirjana Cvijovic
Metal Based Drugs, 2001
The effect of surface active substances on hydrolysis of aluminium(III) ion
Predrag Djurdjevic,, Ratomir Jelic,, Dragana Dzajevic,
Main Group Metal Chemistry, 2000
Study of equilibria in aluminum(III) - L-glutamic acid or -L-serine solutions
Predrag Djurdjevic,, Ratomir Jelic,
Main Group Metal Chemistry, 1998
Solution equilibria in L-glutamic acid and L-serine + iron(III) systems
Predrag Djurdjevic´, Ratomir Jelic´
Transition Metal Chemistry, 1997
Hydrolysis of the zinc(II) ion in sodium nitrate, chloride and perchlorate medium: The effect of the anionic medium
Nikola B. Mili?, Ratomir M. Jeli?
Journal of the Chemical Society Dalton Transactions, 1995
Complex formation equilibria in iron(III)-L-alanine system
Predrag Djurdjević, Ratomir Jelić
Transition Metal Chemistry, 1993
Study of Equilibria in the Aluminium(III)‐Glycine and ‐Alanine Systems
Predrag T. Djurdjević, Ratomir Jelić
Zaac Journal of Inorganic and General Chemistry, 1989

Ratomir Jelic

RESEARCH, TEACHING, or OTHER INTERESTS

Scopus Publications