Oxicam derivatives play an important role in the treatment of pain and inflammation. The mechanism of action of these compounds consists in the inhibition of cyclooxygenase (COX) and the blockade of isoform 1 of this enzyme (COX-1) is considered to generate adverse effects. The aim of this paper is to establish which of the atoms in the oxicams molecules are responsible for their inhibitory activities, using electronegativity as fingerprint descriptor. Using this descriptor and molecular docking programs, the atoms in the molecule that have a greater contribution to COX-1 inhibition have been identified. In the case of the studied molecules, the oxygen atoms and the nitrogen atoms are highlighted. The oxygen atoms participate in the interaction as electron acceptors through U-MO molecular levels (74.1%) and the nitrogen atoms participate in the interaction both as a nucleophilic center through the molecular state of HOMO (13.7%) and as an electrophilic center through the molecular state of LUMO (13.2%). In the case of three out of four of the studied compounds, the 4-hydroxyl group of the thiazine ring participates in the interaction with COX-1. The results are also supported by the 2D and 3Ddiagrams of the applied docking method.

The aim of this study is to investigate the molecular interactions of heparin, diclofenac, and their complexes with cyclooxygenase enzymes (COX-1 and COX-2) using computational docking techniques. Molecular modeling and docking simulations were performed with HyperChem and HEX software, utilizing receptor structures from the Protein Data Bank (PDB). Binding energies and lipophilicity (logP) values were analyzed to evaluate the interaction strength and hydrophobic properties of the complexes compared to the individual drugs. The results demonstrated that both the heparin-diclofenac and diclofenac-heparin complexes exhibit stronger binding affinities to COX-1 and COX-2 than the drugs alone. Notably, the heparin-diclofenac complex showed the strongest binding, sug-gesting that molecular orientation significantly influences interaction efficiency. Further-more, differences in binding behavior between COX-1 and COX-2 were observed, likely due to structural variations in their active sites, with COX-2 providing a more favorable environment for complex interactions. The analysis also highlighted the impact of lipophilicity on binding properties, emphasizing the relevance of physicochemical characteristics in drug-receptor dynamics. These findings suggest that the formation of heparin-diclofenac complexes may enhance COX inhibition, presenting a potential strategy for developing more effective pain management therapies.

In the conducted study, we investigated the total phenolic content of the alcoholic extracts from various vegetative organs of two plants of Romanian wild flora, Oltenia region: Dipsacus laciniatus and Armoracia rusticana. The antioxidant activities were determined by ferric reducing antioxidant power (FRAP), and 1,1-diphenyl-2-picryl hydrazyl (DPPH) radical scavenging methods. We also determined total polyphenol and flavonoid content. The results showed significant differences among plant various vegetative organs, the highest content of polyphenols being found for the leaves extract of Dipsacus laciniatus species, followed by Armoracia rusticana leaves. The highest antioxidant reducing power was obtained for the Armoracia leaf extract (IC50= 101.94 µg/ml), followed by the leaves of Dipsacus (IC50= 77.86 µg/ml).

Azoles are the main antifungal agents currently used in systemic therapy and local mycoses. The class of azole derivatives has been studied using fingerprint descriptors based on electronegativity of the occupied molecular orbitals (OMO) and unoccupied molecular orbitals (UMO). The Hansch equations that correlates partition coefficient with chemical structure allows us to identify the nature of the atoms involved in ligand (drug) - receptor interactions, as well as the nature of those interactions. The results indicate that in the most reactive molecular states, such as states HOMO and LUMO, the oxygen atoms are actually involved in the interaction of the ligand - receptor by the transfer of electrons from the biological receptor to the oxygen atoms.