A 24 kDa leucine-rich protein from ion exchange fractions of Solanum trilobatum, which has anti-bacterial activity against both the Gram-negative Vibrio cholerae and Gram-positive Staphylococcus aureus bacteria has been purified. In this study, mass spectrometry analysis identified the leucine richness and found a luminal binding protein (LBP). Circular dichroism suggests that the protein was predominantly composed of α- helical contents of its secondary structure. Scanning electron microscopy visualized the characteristics and morphological and structural changes in LBP-treated bacterium. Further in vitro studies confirmed that mannose-, trehalose- and raffinose-treated LBP completely inhibited the hemagglutination ability towards rat red blood cells. Altogether, these studies suggest that LBP could bind to sugar moieties which are abundantly distributed on bacterial surface which are essential for maintaining the structural integrity of bacteria. Considering that Solanum triolbatum is a well-known medicinal and edible plant, in order to shed light on its ancient usage in this work, an efficient anti-microbial protein was isolated, characterized and its in vitro functional study against human pathogenic bacteria was evaluated.

In the end of December 2019, a new strain of coronavirus was identified in the Wuhan city of Hubei province in China. Within a shorter period of time, an unprecedented outbreak of this strain was witnessed over the entire Wuhan city. This novel coronavirus strain was later officially renamed as COVID-19 (Coronavirus disease 2019) by the World Health Organization. The mode of transmission had been found to be human-to-human contact and hence resulted in a rapid surge across the globe where more than 1,100,000 people have been infected with COVID-19. In the current scenario, finding potent drug candidates for the treatment of COVID-19 has emerged as the most challenging task for clinicians and researchers worldwide. Identification of new drugs and vaccine development may take from a few months to years based on the clinical trial processes. To overcome the several limitations involved in identifying and bringing out potent drug candidates for treating COVID-19, in the present study attempts were made to screen the FDA approved drugs using High Throughput Virtual Screening (HTVS). The COVID-19 main protease (COVID-19 Mpro) was chosen as the drug target for which the FDA approved drugs were initially screened with HTVS. The drug candidates that exhibited favorable docking score, energy and emodel calculations were further taken for performing Induced Fit Docking (IFD) using Schrodinger’s GLIDE. From the flexible docking results, the following four FDA approved drugs Sincalide, Pentagastrin, Ritonavir and Phytonadione were identified. In particular, Sincalide and Pentagastrin can be considered potential key players for the treatment of COVID-19 disease.

Objective: Inflammatory diseases have a serious impact on one’s life and represent a diverse group of ailments stemming from various causes and presenting in various forms. p38α of the mitogen-activated protein kinase family plays a crucial role in regulating inflammation, where the activation of this kinase initiates a cascade of events resulting in the production of proinflammatory mediators and cellular stress responses. In this context, attempts were made to identify potent small-molecule inhibitors of p38α and assess their binding affinity through molecular docking studies. Methods: From comprehensive reviews of several published reports, a few compounds, such as P38, P39, VPC00628, and N17, have shown substantial inhibitory activity toward p38α at various concentrations. Hence, these four compounds were chosen as lead compounds, and small-molecule libraries were constructed on the basis of their structural similarity. Next, virtual screening docking was performed to investigate the inhibitory potency of the four libraries toward the p38α isoforms (DFG-out and DFG-in), providing insights into their potential mechanisms of action. Results: In addition, a comprehensive analysis of physicochemical and pharmacokinetic properties was also performed for the identified hits from each library. Our findings have shown that, compared with those of the p38α DFG-in motif, the binding energies of the p38α DFG-out motif are greater. Conclusion: Furthermore, a few compounds from each library presented binding energies higher than those of their respective lead compounds, confirming their potential as novel therapeutic agents against inflammation.

Parkinson’s disease is a neurodegenerative disorder marked by dopaminergic neuron loss and α-synuclein aggregation. Non-motor symptoms, like gastrointestinal disturbances, often precede motor issues, implicating the gut–brain axis. The gut microbiome, influencing host metabolism, immunity, and barrier function, may drive neuroinflammation, α-synuclein aggregation, and neurodegeneration through metabolic, immune, and neural pathways. Caenorhabditis elegans is a powerful model for studying these interactions due to its genetic tractability, short lifecycle, and well-defined nervous system. Studies show that specific bacterial taxa, microbial metabolites (e.g., short-chain fatty acids, lipopolysaccharides), and bacterial amyloids (e.g., curli) directly impact α-synuclein aggregation, dopaminergic neuron degeneration, and locomotor deficits. Host genetics and transgenerational epigenetic effects further modulate these interactions. However, Caenorhabditis elegans lacks a blood–brain barrier and has a simplified immune system and microbiome, requiring validation in complex models and human studies. Future research should integrate multi-omics, AI, and synthetic microbiome engineering to bridge this gap. Microbiome-based therapies, like probiotics and fecal transplants, show potential but need clinical validation. A multi-model pipeline combining Caenorhabditis elegans, mammalian, and human data is essential to clarify the microbiome’s role in Parkinson’s disease and develop targeted interventions.

Emodin is a naturally occurring anthraquinone and has been of great interest as a multi-target anticancer agent with potential anti-metastatic effects. There is a growing body of evidence that emodin inhibits the progression of cancer by regulating essential events of epithelial–mesenchymal transition (EMT) and extracellular matrix remodeling. It suppresses matrix metalloproteinases and other associated proteolytic enzymes, thus hindering tumor invasion and metastatic spread. Emodin also suppresses key EMT-related transcription factors, such as Snail, Slug and Twist resulting in lower expression of mesenchymal markers, recovery of epithelial phenotype and lack of cellular motility. These effects are mechanistically mediated by disrupting central oncogenic pathways including transforming growth factor-β (TGF-β)/Smad, Akt/mTOR, MAPK and other signaling pathways that promote EMT plasticity. Recent research also indicates that emodin has a role in regulating cytoskeletal organization, ROS signal, and interactions with the tumor microenvironment that promote metastatic behavior. Although there is strong preclinical evidence, there are still a number of translational gaps. This limits its possible therapeutic use due to low bioavailability, low stability, and inconsistent tumor responsiveness. Possible resistance mechanisms, such as the compensatory activation of other pathways such as Wnt/ β-catenin and survival signaling cascades, are not sufficiently characterized. There is also lack of clinical validation with few controlled trials assessing safety and anti-metastatic efficacy across different types of cancer. The future directions are to focus on optimization of formulation and delivery, improvement of the pharmacokinetics, patient stratification, biomarker-based guided, and rigorous comparisons of combination regimens with chemotherapy, radiotherapy, and targeted agents. These approaches can be used to achieve the full potential of emodin as a therapeutic candidate, which is a metastasis-modulating agent.

Angiogenesis is central to tumor development and metastasis because it facilitates oxygen and nutrient supplies to cancer cells. Inhibiting angiogenic pathways is a commonly used strategy in the treatment of cancer, usually through inhibitory actions that first determine targeted apoptosis of the key proangiogenic factor, vascular endothelial growth factor (VEGF), and its upstream regulator, hypoxia-inducible factor 1-alpha (HIF-1α). Emodin, a common anthraquinone derivative of natural origins, has a variety of actions to inhibit angiogenesis, which include the ability to inhibit the expression of VEGF, as well as the ability to reverse stabilization of HIF-1α and inhibit tumor microvessel branching. Moreover, emodin is recognized for pathways other than those involving VEGF, such as fibroblast growth factor (FGF) and platelet-derived growth factor (PDGF), which impact endothelial cell proliferation and pericyte recruitment. Emodin can facilitate vessel destabilization by acting on several angiopoietins, causing the function of the tumor vasculature to be disrupted. Molecular docking studies have shown emodin can bind the ATP-binding pocket of VEGFR-2 and the degradation domain of HIF-1α, acting as a multi-target inhibitory compound. These mechanisms collectively obstruct tumor vascularization, deprive tumor cells of vital nutrients, and prevent cancer progression. Pre-clinical studies to date have determined it to be a significant anti-angiogenic agent and a synergistic agent in combination with chemotherapy and/or targeted therapies that can be given to patients. Future studies will address bioavailability issues, target the associated resistance mechanisms, and explore ways to increase its efficacy as an adjuvant in cancer treatment.