The agglomeration of metal-organic frameworks (MOFs) has long been a problem, and achieving stable monodispersity in water remains a great challenge. This paper reports a universal strategy that functionalizes MOFs by using an endogenous bioenzyme namely glucose oxidase (GOx), to achieve stable water monodispersity, and integrates it as a highly efficient nanoplatform for cancer synergistic therapy. Phenolic hydroxyl groups in GOx chain confers robust coordination interactions with MOFs, which not only endows stable monodispersion in water, but also provides many reactive sites for further modification. Silver nanoparticles are uniformly deposited onto MOFs@GOx to achieve high conversion efficiency from near-infrared light to heat, resulting in an effective starvation and photothermal synergistic therapy model. In vitro and in vivo experiments confirm excellent therapeutic effect at very low doses without using any chemotherapeutics. In addition, the nanoplatform generates large amounts of reactive oxygen species, induces heavy cell apoptosis, and demonstrates the first experimental example to effectively inhibit cancer migration. Our universal strategy enables stable monodispersity of various MOFs via GOx functionalization and establishes a non-invasive platform for efficient cancer synergistic therapy.
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http://dx.doi.org/10.1016/j.jcis.2023.03.178 | DOI Listing |
Food Chem
December 2024
Department of Nutrition and Food Hygiene, School of Public Health, Tianjin Medical University, 300070 Tianjin, People's Republic of China; Tianjin Key Laboratory of Environment, Nutrition and Public Health, Center for International Collaborative Research on Environment, Nutrition and Public Health, Tianjin Medical University, Tianjin, People's Republic of China. Electronic address:
A novel biomimetic molecular imprinted polymer chip with fluorescence (FL) and structural (STR) states, inspired by color patterns of chameleon skin, is fabricated for detecting diethylstilbestrol (DES). The chip features a regularly structured, non-closed-packed (NCP) colloidal photonic crystal (CPC) lattice made monodisperse MIP spheres containing fluorescence poly ionic liquid (FPIL) pigments. The FL color originates from FPIL pigments and is further enhanced by the Purcell effect, while the STR color results from the periodic arrangement of the NCP CPC structure.
View Article and Find Full Text PDFActa Crystallogr F Struct Biol Commun
January 2025
Unité de Glycobiologie Structurale et Fonctionnelle (UGSF), UMR 8576 CNRS and University of Lille, Villeneuve d'Ascq, France.
Monoclonal antibodies recognizing nonprotein antigens remain largely underrepresented in our understanding of the molecular repertoire of innate and adaptive immunity. One such antibody is Mannitou, a murine IgM that recognizes paucimannosidic glycans. In this work, we report the production and purification of the recombinant antigen-binding fragment (Fab) of Mannitou IgM (Mannitou Fab) and employ a combination of biochemical and biophysical approaches to obtain its initial structural characterization.
View Article and Find Full Text PDFACS Nano
December 2024
Department of Biochemistry and Molecular Biology, Tulane University School of Medicine, New Orleans, Louisiana 70112, United States.
The synthetically evolved pHD family of peptides is known to self-assemble into macromolecule-sized nanopores of 2-10 nm diameter in synthetic lipid bilayers, but only when the pH is below ∼6. Here, we show that a representative family member, pHD108, has the same pH-responsive nanopore-forming activity in the endosomal membranes of living human cells, which is triggered by endosomal acidification. This enables the cytosolic delivery of endocytosed proteins and other macromolecules.
View Article and Find Full Text PDFBiochem Biophys Res Commun
December 2024
Institute of Cytology of the Russian Academy of Sciences, St. Petersburg, Tikhoretsky av.4, 194064, Russia. Electronic address:
In addition to the well-known monomeric and polymeric forms of actin there is another unique thermodynamically stable state of this protein, called "inactivated actin" (I-actin). I-actin is formed at moderate concentration of a denaturant, release of Ca ions and/or ATP, or after heating. This state is a monodisperse associate and it has the same spectral characteristics regardless of the method of preparation.
View Article and Find Full Text PDFNat Commun
November 2024
Division of Structural Biology, Wellcome Centre for Human Genetics, University of Oxford, Oxford, UK.
The cryo-electron microscopy (cryoEM) method has enabled high-resolution structure determination of numerous biomolecules and complexes. Nevertheless, cryoEM sample preparation of challenging proteins and complexes, especially those with low abundance or with preferential orientation, remains a major hurdle. We developed an affinity-grid method employing monodispersed single particle streptavidin on a lipid monolayer to enhance particle absorption on the grid surface and alleviate sample exposure to the air-water interface.
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