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Four previously undescribed cyclic peptides, reniochpeptins A-D (1-4), were isolated from the marine sponge Reniochalina sp. Their structures were elucidated through comprehensive spectroscopic analyses and a modified advanced Marfey's method. This method utilized ultra-high-performance liquid chromatography coupled with tandem multiple reaction monitoring mass spectrometry, employing a CORTECS T column to achieve simultaneous separation of derivatized -Leu, -Ile, -allo-Ile, -Leu, -Ile, and -allo-Ile within 25 min in a single analytical run. Reniochpeptin A displayed moderate inhibitory activity against NCI-H460 cells, with an IC value of 4.7 μM, by inducing cell cycle arrest at the G2/M phase and promoting apoptosis.
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http://dx.doi.org/10.1016/j.phytochem.2025.114412 | DOI Listing |
ACS Appl Mater Interfaces
September 2025
Department of Materials Science and Engineering, Gwangju Institute of Science and Technology (GIST), Gwangju 61005, Republic of Korea.
Cyclic peptides (CPs) are versatile building blocks whose conformational constraints foster ordered supramolecular architectures with potential in biomedicine, nanoelectronics, and catalysis. Herein, we report the development of biomimetic antifreeze materials by conjugating CPs bearing ice-binding residues to 4-arm polyethylene glycol (PEG) via click chemistry. The concentration-dependent self-assembly of these CP-PEG conjugates induces programmable morphological transitions, forming nanotube networks above the critical aggregation concentration (CAC) and two-dimensional nanosheet networks near the CAC.
View Article and Find Full Text PDFFront Immunol
September 2025
Department of Pediatrics, Division of Infectious Diseases, Emory University School of Medicine, Atlanta, GA, United States.
Introduction: Interferon-induced transmembrane proteins (IFITMs) inhibit the entry of diverse enveloped viruses. The spectrum of antiviral activity of IFITMs is largely determined by their subcellular localization. IFITM1 localizes to and primarily blocks viral fusion at the plasma membrane, while IFITM3 prevents viral fusion in late endosomes by accumulating in these compartments.
View Article and Find Full Text PDFFront Endocrinol (Lausanne)
September 2025
Pediatric Endocrinology Department, Obesity, Endocrine and Metabolism Center, King Fahd Medical City, Riyadh, Saudi Arabia.
McCune-Albright syndrome (MAS) is a rare genetic disorder characterized by a triad of café-au-lait spots, fibrous dysplasia, and hyperfunctioning endocrinopathies, resulting from a mosaic mutation in the guanine nucleotide-binding protein (GNAS) gene. This case report presents the long-term follow-up of an eight-year-old girl diagnosed with MAS, who first presented at 22 months of age with skin pigmentation, hyperthyroidism, and precocious puberty, later developing additional features such as fibrous dysplasia and growth hormone excess. This complex presentation of MAS-featuring more than two hyperfunctioning endocrinopathies along with fibrous dysplasia-has rarely been described in the literature.
View Article and Find Full Text PDFJ Appl Microbiol
September 2025
Sivas Cumhuriyet University, Faculty of Medicine, Department of Medical Microbiology, 58140 Sivas, Türkiye.
Aims: The increasing antimicrobial resistance, particularly in Acinetobacter baumannii, complicates the treatment of infections, leading to higher morbidity, mortality, and economic costs. Herein, we aimed to determine the in vitro antimicrobial, synergistic, and antibiofilm activities of colistin (COL), meropenem, and ciprofloxacin antibiotics, and curcumin, punicalagin, geraniol (GER), and linalool (LIN) plant-active ingredients alone and in combination against 31 multidrug-resistant (MDR) A. baumannii clinical isolates.
View Article and Find Full Text PDFFungal Biol
October 2025
University of Tuscia, Department of Agriculture and Forest Sciences (DAFNE), Via San Camillo de Lellis SNC, Viterbo, Italy.
Fusarium Head Blight (FHB), caused by various Fusarium species, is a major threat to global cereal production. F. avenaceum is an important FHB pathogen producing enniatin mycotoxins.
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