Repurposing of Rutan showed effective treatment for COVID-19 disease.

Previously, from the tannic sumac plant (Rhus coriaria), we developed the Rutan 25 mg oral drug tablets with antiviral activity against influenza A and B viruses, adenoviruses, paramyxoviruses, herpes virus, and cytomegalovirus. Here, our re-purposing study demonstrated that Rutan at 25, 50, and 100 mg/kg provided a very effective and safe treatment for COVID-19 infection, simultaneously inhibiting two vital enzyme systems of the SARS-CoV-2 virus: 3C-like proteinase (3CLpro) and RNA-dependent RNA polymerase (RdRp). There was no drug accumulation in experimental animals' organs and tissues. A clinical study demonstrated a statistically significant decrease in the C-reactive protein and a reduction of the viremia period. In patients receiving Rutan 25 mg (children) and 100 mg (adults), the frequency of post-COVID-19 manifestations was significantly less than in the control groups not treated with Rutan tablets. Rutan, having antiviral activity, can provide safe treatment and prevention of COVID-19 in adults and children. Clinical Trial Registration: ClinicalTrials.gov, ID NCT05862883.

Synthesis and Characterization of Novel Chickpea Protein Hydrolysate-Vanadium Complexes Having Cell Inhibitory Effects on Lung Cancer A549 Cells Lines.

Designing new types of drugs with preferred properties against cancer is a great issue for scientists dealing with synthesis and study of biological activity. Several organometallic compounds used in chemotherapy reveal side effects. Peptides from edible sources having no side effects may play a transport role in the delivery of anticancer metal ions into targeted tumor cells. For the last two decades, peptide-metal complexes have been considered as potential anticancer agents. In this work, oxovanadium complexes of peptides from Chickpea (Cicer arietinum L.) seeds' protein hydrolysate were investigated. The albumin fraction of Chickpea seeds protein was hydrolyzed with a combination of enzymes papain, trypsin, and alcalase. The hydrolysate was combined with vanadyl ions and obtained oxovanadium complexes were studied by FTIR, SEM-EDX, and TG-DSC analyses, and cell inhibition activity against A549 cells was detected by MTT Assay. In a result, activity of the complexes (IC50 = 14.39 µg/mL) increased 1.7-fold compared to the activity of inorganic salt of vanadium (IC50 = 24.75 µg/mL) against A549 cells. The complexes (CPH-V) were fractionated through Sephadex G-15, and the second active fraction, named CPH-V G15-II was studied by nano-Q-TOF LC/MS. Nine peptides with a molecular mass range of 437-1864 Da were identified. Seven of them were theoretically considered as cell-penetrating peptides. These results could serve first steps for deeper fundamental research on food-derived peptide-vanadium complexes.