Jadeja RA, Mayani SV.
PMID:PPR1178661
Free PMC article
Abstract Green synthesis of metal oxide nanoparticles using plant-derived phytochemicals represents a sustainable and surface-engineered approach for developing functional nanomaterials. In the present study, an aqueous root extract of Butea monosperma was employed as a bio reducing and stabilizing agent for the synthesis of zinc oxide nanoparticles (ZnO NPs). Phytochemical profiling using qualitative assays, thin-layer chromatography (TLC), high-performance liquid chromatography (HPLC), and LC–MS confirmed the presence of polyphenols, flavonoids, tannins, and triterpenoids, which are known to facilitate metal ion reduction and nanoparticle stabilization. UV–visible spectroscopy revealed a characteristic absorption edge in the UV region with an optical band gap of 3.69 eV, indicating nanoscale ZnO formation. Powder X-ray diffraction (PXRD) confirmed the formation of crystalline hexagonal wurtzite ZnO (JCPDS No. 36-1451) with an average crystallite size of 12–18 nm. Dynamic light scattering analysis showed a hydrodynamic diameter of 255.8 nm with a polydispersity index of 0.389, while a negative zeta potential (–25 mV) indicated moderate colloidal stability due to phytochemical surface capping. FTIR spectra demonstrated the involvement of hydroxyl and carbonyl functional groups in nanoparticle formation. SEM–EDX analysis confirmed nanoscale morphology and elemental purity (Zn 74.48 wt%, O 25.52 wt%). The synthesized ZnO NPs exhibited concentration-dependent antibacterial activity, with a maximum inhibition zone of 20 mm against Bacillus sp. and 15 mm against Escherichia coli at 1000 µg/mL. These findings establish a direct correlation between root phytochemical composition, nanoparticle physicochemical properties, and antimicrobial performance, demonstrating the potential of B. monosperma -mediated ZnO NPs as phytochemical-engineered antibacterial nanomaterials.
Patlan-Velázquez LF, González-Olivares LG, García-Garibay M, Alatorre-Santamaría S, Gómez-Ruiz L, Rodríguez-Serrano G, Carrasco-Navarro U, Cruz-Guerrero A.
Food Sci Nutr
PMID:42005323
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Requeson, a traditional Mexican whey cheese, represents a promising avenue for the valorization of dairy by-products. However, its functional potential remains underexplored. This study evaluated the enhancement of bioactive properties in Requeson cheese through lactic acid bacteria (LAB) fermentation, comparing two monocultures ( Lactobacillus delbrueckii subsp. bulgaricus NCFB 2772 and Streptococcus thermophilus SY-102) and a co-culture of both strains, cultured in sweet whey. Fermented whey was used to produce Requeson cheese, and peptide-rich extracts were analyzed for antioxidant activity (DPPH and FRAP), mineral-chelating capacity (Fe 2+ , Ca 2+ , Mg 2+ ), enzymatic inhibition (ACE-I, DPP-IV), and antimicrobial activity against E. coli , M. luteus , and L. innocua . Liquid chromatography-tandem mass spectrometry (LC-MS/MS) was employed to identify peptides, and their potential bioactivities were predicted using the UniDL4BioPep platform. The co-culture fermentation yielded significantly higher values across all assays, including antioxidant capacity (41.3 mg Trolox), ACE-I inhibition (31.8%), DPP-IV inhibition (14.2%), and antimicrobial activity. Several peptides with predicted antioxidant, antihypertensive, antidiabetic, and antimicrobial properties were exclusive to the co-culture formulation. These findings suggest that LAB co-culture fermentation of sweet whey is an effective strategy to develop peptide-enriched functional Requeson cheese with health-promoting properties. This approach supports the sustainable use of dairy by-products and contributes to the advancement of functional dairy products in the bioeconomy.
Camunas-Alberca SM, Bartolini F, Cermakova H, Sánchez-Illana Á, Perez-Guaita D, Cañadas-Miquel P, Gil-de-la-Fuente A, Galano JM, Durand T, Gradillas A, Barbas C.
Anal Chem
PMID:41997579
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Oxylipins are bioactive lipid mediators that play key roles in biological and pathological processes. Their remarkable chemical diversity makes their identification by untargeted LC-MS/MS analyses challenging. To date, effective solutions for their comprehensive characterization remain unavailable. Here, we present the first implementation of the recently refined Ion Identity Molecular Networking (IIMN) strategy to map the chemical space of oxylipins, together with a systematic evaluation of factors that hinder accurate annotation in MS/MS datasets. Building on recent mzmine software developments, we implemented a fully local strategy to perform the IIMN analysis without requiring web platforms or external tools. We established a high-quality MS/MS spectral library from 67 commercially available oxylipin standards using LC-MS data obtained in data-dependent acquisition mode. Integrating the detailed characterization of ion species generated during electrospray ionization into IIMN reduced network complexity. Across configurations, the modified cosine algorithm proved most effective for separating full-length from cyclized forms and for clustering oxylipins through structurally coherent relationships. Application of the IIMN workflow to mouse spleen extracts, in combination with our in-house and publicly available experimental MS/MS libraries, enabled the organization of oxylipins into molecular families, facilitating their structural characterization and the discovery of novel species. Although manual curation remained necessary for certain coeluting isomers and ambiguous fragments, the IIMN-based approach significantly improved network interpretability and understanding. Overall, this study establishes IIMN as a robust bioinformatic tool for decoding oxylipin diversity and provides a successful strategy for mapping their chemical space, characterizing them within samples, and discovering novel mediators in biological matrices. The new combined reference spectral library has been made publicly available and will serve as a valuable resource for future redox lipidomics research.
Msobo A, Maphari PW, Koorsen G, Singab ANB, Mhlongo MI.
In Silico Pharmacol
PMID:42005985
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The COVID-19 pandemic highlighted critical limitations in the speed, scalability and translational efficiency of conventional antiviral drug discovery. Although vaccines and repurposed antivirals have reduced disease severity, the continued emergence of SARS-CoV-2 variants and breakthrough infections underscores the need for sustained discovery of novel therapeutics. The main protease (Mpro), an essential and highly conserved enzyme required for viral replication remains a validated and attractive antiviral target. Medicinal plants represent a vast and underexplored source of structurally diverse bioactive compounds with antiviral potential; however, traditional plant-based drug discovery approaches are often constrained by reliance on ethnobotanical knowledge and fragmented screening workflows. This review critically examines emerging strategies that integrate machine learning, LC-MS-based metabolomics and network pharmacology to modernise medicinal plant-based antiviral discovery. We highlight how machine learning enables data-driven prioritisation of candidate compounds and plant species beyond well-studied taxa, while metabolomics provides experimental validation through comprehensive chemical profiling and dereplication. Molecular docking and molecular dynamics further refine candidate selection by evaluating binding modes and stability, whereas network pharmacology offers systems-level insight into multitarget and multipathway effects. Importantly, we discuss key limitations of these approaches, including data bias, model interpretability, and gaps between in silico prediction and experimental validation. By synthesising these methodologies into a unified computational-experimental pipeline, this review provides a critical framework for accelerating the discovery of plant-derived Mpro inhibitors and supports the development of resilient antiviral strategies for current and future pandemics.
Chen S, Wang M, Zeng Y, Li X, Zhong H, Liu Y, Tao Y, Yang X, Luo C, Chen S, Xiong H.
Eur J Med Chem
PMID:42001546
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Ubiquitin-specific protease 7 (USP7) is a key member of the deubiquitinating enzyme family. It is abnormally overexpressed in various malignancies, including breast cancer, chronic lymphocytic leukemia, and prostate cancer. By regulating pathways such as the p53-MDM2 signaling axis, USP7 promotes tumorigenesis and progression, making it a highly promising therapeutic target for anticancer treatment. Although multiple USP7 inhibitors have been reported, existing screening and evaluation assays exhibit limitations: the ubiquitin-phospholipase A 2 (Ub-PLA 2 ) assay frequently produces false-positive results, while the ubiquitin-rhodamine (Ub-Rho) assay is susceptible to interference from compound autofluorescence. To address this challenge, we developed a fluorescence polarization (FP) assay. This employs a rationally designed strategy that exhibits excellent characteristics, making it a simple-to-operate and cost-effective method, suitable for the evaluation of compound bioactivity against USP7. To further validate the practicality and reliability of this FP assay, we conducted a structure-based drug design campaign involving two rounds of systematic structural optimization, yielding 51 novel derivatives featuring pyrazolo[4,3-d]pyrimidine and piperidol scaffolds. Following FP evaluation and Ub-Rho enzyme activity validation, we performed a comprehensive structure-activity relationship (SAR) analysis. Ultimately, in vitro cellular assays identified three compounds (LC-U7-44, LC-U7-48, and LC-U7-50) that exhibit potent USP7 inhibitory activity alongside favorable cellular anti-proliferative effects. Overall, the established FP assay in this study closes a methodological gap in the evaluation of USP7 inhibitors, and the detailed SAR analysis provides a foundation for the further development of potent USP7 inhibitors.
