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Iron deficiency anemia is a global health concern, affecting around 2 billion people. Oral iron therapy often causes severe gastro‐intestinal issues. Eruca sativa, member of the Brassicaceae family, is valued in traditional medicine and renowned for its rich iron and vitamin C content. This study aims to evaluate the anti‐anemic properties of E. sativa extract in vivo and identify its compounds targeting anemia mechanisms using network pharmacology. Thirty‐two Sprague–Dawley rats (200 ± 250 g) were split into two distinct groups, iron‐deficient and iron‐sufficient. Three different doses (200, 400, and 800 mg/kg) of aqueous extract of E. sativa were checked against anemia by studying hematological, oxidative stress, and histopathological parameters. GC–MS analysis of E. sativa revealed its phytochemical profile, followed by ADME screening. Network pharmacology explored targets related to iron deficiency anemia, with oral bioavailability and drug likeness assessment for compounds. The administration of extracts significantly improved various blood parameters, including osmotic fragility, Hb, RBCs, MCV, PCV, and alkaline phosphatase; catalase activity; and histopathological parameters such as liver in both iron‐deficient and iron‐sufficient rats (p <.001). Seventy‐nine compounds were identified in E. sativa aqueous extract, with only six of them found to be bioavailable and drug‐like against multiple targets. Gene ontology and pathway analysis revealed their diverse molecular, biological, and cellular functions. One gene EGFR was found to have functional association with ID anemia, suggesting potential for using E. sativa extracts. The study concludes that E. sativa extract has potential for iron deficiency anemia treatment, offering hope for future pharmaceutical interventions. [ABSTRACT FROM AUTHOR]

The viral pandemic has resulted in a growing demand for antiviral drugs. The existing small‐molecule antiviral drugs are limited, due to their incidence of drug resistance and adverse side effects. As potential drugs, antiviral peptides have the benefits of high activity, high stability, and few side effects. Furthermore, the diversity of acquisition methods allows antiviral peptides to be quickly designed and yielded. The drug properties (such as high bioavailability and in vivo stability) of antiviral peptides can be improved by the developed modifications. Currently, two peptide antiviral drugs have been approved for the treatment of acquired immunodeficiency syndrome (AIDS). Many antiviral peptides have entered clinical trials for the treatment of diseases caused by viruses. In addition, new antiviral peptides are continuously being identified and validated against virus infections. Given the benefits of antiviral peptides, they will become major antiviral drugs to combat new outbreaks caused by unknown viruses in the future. This review provides an overview of recent developments in antiviral peptides with in vivo activity. [ABSTRACT FROM AUTHOR]

Amino acid (AA) sequences of 807 bioactive peptides from foods of animal origin were examined in order to correlate peptide structure with activity (antihypertensive, antioxidative, immunomodulatory, antimicrobial, hypolipidemic, antithrombotic, and opioid) and stability in vivo. Food sources, such as milk, meat, eggs, and marine products, show different frequencies of bioactive peptides exhibiting specific effects. There is a correlation of peptide structure and effect, depending on type and position of AA. Opioid peptides contain a high percentage of aromatic AA residues, while antimicrobial peptides show an excess of positively charged AAs. AA residue position is significant, with those in the first and penultimate positions having the biggest effects on peptide activity. Peptides that have activity in vivo contain a high percentage (67%) of proline residues, but the positions of proline in the sequence depend on the length of the peptide. We also discuss the influence of processing on activity of these peptides, as well as methods for predicting release from the source protein and activity of peptides. [ABSTRACT FROM AUTHOR]

Abstract: Calmodulin is known to bind to various amphipathic helical peptide sequences, and the calmodulin–peptide binding surface has been shown to be remarkably tolerant sterically. d‐Amino acid peptides, therefore, represent potential non‐hydrolysable intracellular antagonists of calmodulin. In the present study, synthetic combinatorial libraries have been used to develop novel d‐amino acid hexapeptide antagonists to calmodulin‐regulated phosphodiesterase activity. Five hexapeptides were identified from a library containing over 52 million sequences. These peptides inhibited cell proliferation both in cell culture using normal rat kidney cells and by injection via the femoral vein following partial hepatectomy of rat liver cells. These hexapeptides showed no toxic effect on the cells. Despite their short length, the identified hexapeptides appear to adopt a partial helical conformation similar to other known calmodulin‐binding peptides, as shown by CD spectroscopy in the presence of calmodulin and NMR spectroscopy in DMSO. The present peptides are the shortest peptide calmodulin antagonists reported to date showing potential in vivo activity. [ABSTRACT FROM AUTHOR]