Electron spin resonance spectra of DNA labeled with each of four spin-labeling compounds have been studied to detect interaction between the antibiotic bleomycin and DNA. Only one of these labels, compound IV, resulted in a modified spectrum when bound to DNA and the latter was subjected to bleomycin. This property has been used to monitor DNA-bleomycin interactions under physiological and hyperthermic conditions. Bleomycin produced an increase in rotational correlation time of the residue bound to DNA at 37 degrees C and a significantly higher increase at 43 degrees C. Some effect was still detected with bleomycin at 37 degrees C after preheating at 43 degrees C. Parallel studies have revealed enhanced binding of 59Fe-bleomycin to DNA during and after hyperthermic treatment.
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J Am Chem Soc
January 2025
Department of Chemistry, Southern University of Science and Technology, Shenzhen 518055, China.
A small but growing set of radical SAM (-adenosyl-l-methionine) enzymes catalyze the radical mediated dehydration or dehydrogenation of 1,2-diol substrates. In some cases, these activities can be interchanged via minor structural perturbations to the reacting components raising questions regarding the relative importance of hyperconjugation, proton circulation and leaving group stability in determining the reaction outcome. The present work describes trapping and electron paramagnetic resonance (EPR) characterization of an α-hydroxyalkyl radical intermediate during dehydration and dehydrogenation of cytosylglucuronic acid and its derivatives catalyzed by the radical SAM enzyme BlsE and its Glu189Ala mutant from the blasticidin S biosynthetic pathway.
View Article and Find Full Text PDFMolecules
January 2025
School of Chemistry and Chemical Engineering, Shandong University, Jinan 250100, China.
Developing a new type of circularly polarized luminescent active small organic molecule that combines high fluorescence quantum yield and luminescence dissymmetric factor in both solution and solid state is highly challenging but promising. In this context, we designed and synthesized a unique triarylborane-based [2.2]paracyclophane derivative, , in which an electron-accepting [(2-dimesitylboryl)phenyl]ethynyl group and an electron-donating -diphenylamino group are introduced into two different benzene rings of [2.
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January 2025
Department of Chemistry & Biochemistry, Miami University, Oxford, OH 45056, USA.
Epigallocatechin gallate (EGCg), an abundant phytochemical in green tea, is an antioxidant that also binds proteins and complex metals. After gastrointestinal absorption, EGCg binds to serum albumin in the hydrophobic pocket between domains IIA and IIIA and overlaps with the Sudlow I site. Serum albumin also has two metal binding sites, a high-affinity N-terminal site (NTS) site that selectively binds Cu(II), and a low-affinity, less selective multi-metal binding site (MBS).
View Article and Find Full Text PDFMaterials (Basel)
January 2025
Faculty of Dental Medicine, Carol Davila University of Medicine and Pharmacy, 8 Eroii Sanitari Street, 050474 Bucharest, Romania.
Infections continue to pose significant challenges in dentistry, necessitating the development of innovative solutions that can effectively address these issues. This study focuses on creating coatings made from polymethyl methacrylate (PMMA) enriched with zinc oxide-silver composite nanoparticles, layered to Ti6Al4V-titanium alloy substrates. The application of these materials aims to create a solution for the abutments utilized in complete dental implant systems, representing the area most susceptible to bacterial infections.
View Article and Find Full Text PDFBiomolecules
January 2025
Department of Chemistry and Institute of Nanotechnology and Advanced Materials, Faculty of Exact Sciences, Bar-Ilan University, Ramat-Gan 5290002, Israel.
Ctr1 is a membrane-spanning homotrimer that facilitates copper uptake in eukaryotic cells with high affinity. While structural details of the transmembrane domain of human Ctr1 have been elucidated using X-ray crystallography and cryo-EM, the transfer mechanisms of copper and the conformational changes that control the gating mechanism remain poorly understood. The role of the extracellular N-terminal domains is particularly unclear due to the absence of a high-resolution structure of the full-length hCtr1 protein and limited biochemical and biophysical characterization of the transporter in solution and in cell.
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