boron has been researched along with Hemolysis* in 3 studies
3 other study(ies) available for boron and Hemolysis
Article | Year |
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Photodynamic activity of the boronated chlorin e6 amide in artificial and cellular membranes.
Photodynamic tumor-destroying activity of the boronated chlorin e6 derivative BACE (chlorin e6 13(1)-N-{2-[N-(1-carba-closo-dodecaboran-1-yl)methyl]aminoethyl}amide-15(2), 17(3)-dimethyl ester), previously described in Moisenovich et al. (2010) PLoS ONE 5(9) e12717, was shown here to be enormously higher than that of unsubstituted chlorin e6, being supported by the data on much higher photocytotoxicity of BACE in M-1 sarcoma cell culture. To validate membrane damaging effect as the basis of the enhanced tumoricidal activity, BACE was compared with unsubstituted chlorin e6 in the potency to photosensitize dye leakage from liposomes, transbilayer lipid flip-flop, inactivation of gramicidin A ionic channels in planar lipid membranes and erythrocyte hemolysis. In all the models comprising artificial and cellular membranes, the photodynamic effect of BACE exceeded that of chlorin e6. BACE substantially differed from chlorin e6 in the affinity to liposomes and erythrocytes, as monitored by fluorescence spectroscopy, flow cytometry and centrifugation. The results support the key role of membrane binding in the photodynamic effect of the boronated chlorin e6 amide. Topics: Amides; Animals; Boron; Cell Membrane; Cells, Cultured; Chlorophyllides; Erythrocytes; Female; Flow Cytometry; Hemolysis; Humans; Light; Lipid Bilayers; Liposomes; Membranes, Artificial; Photosensitizing Agents; Porphyrins; Rats; Sarcoma | 2014 |
Homogeneous immunoconjugates for boron neutron-capture therapy: design, synthesis, and preliminary characterization.
The application of immunoprotein-based targeting strategies to the boron neutron-capture therapy of cancer poses an exceptional challenge, because viable boron neutron-capture therapy by this method will require the efficient delivery of 10(3) boron-10 atoms by each antigen-binding protein. Our recent investigations in this area have been focused on the development of efficient methods for the assembly of homogeneous immunoprotein conjugates containing the requisite boron load. In this regard, engineered immunoproteins fitted with unique, exposed cysteine residues provide attractive vehicles for site-specific modification. Additionally, homogeneous oligomeric boron-rich phosphodiesters (oligophosphates) have been identified as promising conjugation reagents. The coupling of two such boron-rich oligophosphates to sulfhydryls introduced to the CH2 domain of a chimeric IgG3 has been demonstrated. The resulting boron-rich immunoconjugates are formed efficiently, are readily purified, and have promising in vitro and in vivo characteristics. Encouragingly, these studies showed subtle differences in the properties of the conjugates derived from the two oligophosphate molecules studied, providing a basis for the application of rational design to future work. Such subtle details would not have been as readily discernible in heterogeneous conjugates, thus validating the rigorous experimental design employed here. Topics: Animals; Binding Sites, Antibody; Boron; Boron Neutron Capture Therapy; Drug Design; Erythrocytes; Hemolysis; Humans; Immunoglobulin Fragments; Immunoglobulin G; Immunoproteins; Isotopes; Mice; Models, Molecular; Protein Conformation; Receptors, IgG; Recombinant Fusion Proteins; Sheep; Tissue Distribution | 1998 |
[INDUCED HEMOLYSIS TIME STUDIED WITH SOME METALLOIDS IN POWDERED FORM].
Topics: Antacids; Arsenic; Bismuth; Boron; Carbon; Hemolysis; Metalloids; Powders; Research; Sulfur; Toxicology | 1964 |