Pesticide use in agriculture poses risks to the environment and consumer health. This study analyzed 10 pesticide residues in wine grapes affected by Downy Mildew. Red and white grape samples were extracted using the roQ-QuEChERS kit, and pesticide levels were measured with LC-MS/MS. Results showed contamination with one to three pesticide residues in 72 % of the analyzed samples, with 31 % containing over four different pesticides. Metalaxyl and dimethomorph were the most frequently detected, while mandipropamid had the highest average concentration (12.5 ng/mL). All detected pesticide levels were below safety thresholds, indicating no health risks. Risk assessment using PRIMo 4 confirmed no risks for adults or children at the detected residue levels. Moreover the cumulative risk associated with the simultaneous presence of multiple pesticides in the same grape sample, calculated by the HI approach, resulted below the EFSA reference values and was therefore considered acceptable.

6-Nitrodopamine is an endogenous catecholamine responsible for numerous biological activities. Here, an improved method for the synthesis of both 6-nitrohomovanillic acid (6-NHVA) and its regioisomer 5-nitrohomovanillic acid (5-NHVA) is reported. The developed one-step synthetic procedures ensured the efficient preparation of the target compounds in good yields. Comprehensive structural characterization was achieved through one- and two-dimensional NMR studies and by high-resolution mass spectrometry (HR-MS/MS). The presence of both substances was identified in human amniotic fluid by LC-MS/MS.

A focused library of 1,2,4-thiadiazolidin-3,5-diones (THIA-1–10), previously characterized as hydrogen sulfide (H₂S) donors, was evaluated for inhibitory activity against cysteine proteases. We included two key cysteine proteases aiming at antiviral drug development—SARS-CoV-2 3CLpro (Mpro) and PLpro—alongside reference enzymes Papain and Cathepsin L. The compounds exhibited distinct selectivity profiles and inhibition mechanisms. The ability to act as covalent inhibitors of 3CLpro in the nanomolar range is of particular interest, with compounds THIA-6, -7, and -10 proving to be the most potent inhibitors of the series, and compounds THIA-1, -2, and -8 proving to be the most selective with respect to the other proteases. We explored the molecular bases of the observed activity profile of THIA-1–10 through computational studies, which supported and complemented the experimental findings, paving the way for future structure optimization. The results highlight that inhibitory potency depends not only on electrophilicity but also on the ability to access the catalytic cysteine within the active site. The dual functionality of THIA-1–10 as H₂S donors and selective cysteine protease inhibitors underscores its potential as a promising lead for therapeutic development.