4-4-difluoro-4-bora-3a-4a-diaza-s-indacene and Carcinoma--Hepatocellular

Tumor environmental sensitive polypeptide integrated photosensitizer is a platform for imaging-guided photodynamic therapy (PDT). However, the photosensitizer leakage during blood circulation, poor accumulation in tumor tissue and inferior quantum yield of singlet oxygen are still challenges. Herein, NHS-active boron-dipyrromethene derivative with bromine substituted NHS-BODIPY-Br

Topics: Animals; Apoptosis; Boron Compounds; Breast Neoplasms; Carcinoma, Hepatocellular; Cell Proliferation; Female; Humans; Hydrogen-Ion Concentration; Infrared Rays; Liver Neoplasms; Mice; Mice, Inbred BALB C; Mice, Nude; Nanoparticles; Peptide Fragments; Photochemotherapy; Radiotherapy, Image-Guided; Singlet Oxygen; Tumor Cells, Cultured; Xenograft Model Antitumor Assays

A novel type of multivalent and highly specific fluorescent hyperbranched glycopolymers h-P(GalEA-co-VBPT-co-BYMA) (hPGVB) is designed and prepared successfully via a facile "bottom-up" strategy. The acetylated hPGVB is prepared by one-pot reversible addition-fragmentation chain transfer (RAFT) copolymerization of acrylate-type galactose monomers AcGalEA and methacrylate-type fluorescent monomers BYMA in presence of an inimer-type RAFT chain transfer agent. After deacetylation, the resulting amphiphilic hPGVB can self-assemble into stable nanoparticles in aqueous media, showing strong green fluorescence with relative high quantum yields and good photostability. The cell viability study indicates the excellent biocompatibility of the hPGVB fluorescent nanoparticles (FNPs) against HepG2 and NIH3T3 cells. More importantly, comparing with the galactose-free fluorescent hyperbranched polymers h-P(OEGMA-co-VBPT-co-BYMA), hPEVB FNPs can be selectively internalized by asialoglycoprotein (ASGP) receptor-rich HepG2 cells, indicating their potential application in the bioimaging fields.

Topics: Animals; Boron Compounds; Carcinoma, Hepatocellular; Hep G2 Cells; Humans; Liver Neoplasms; Mice; Nanoparticles; NIH 3T3 Cells; Optical Imaging; Polysaccharides

A highly selective and sensitive turn-on red fluorescent 1-amino BODIPY-based probe (where BODIPY denotes indole-based boron-dipyrromethene) with high off-to-on contrast ratio has been developed. The probe displayed selective response to thiophenols over aliphatic thiols. Probe 1 is promising for the quantitative detection of thiophenol with a linear response from 6 × 10(-6) M to 1 × 10(-4) M, and the detection limit for thiophenol (PhSH) reaches 4 × 10(-6) M measured in acetonitrile/PBS buffer. The detection limit could be improved to 37 nM (detection limit to 4 ppb) in water when 1% Tween 20 was used to assist the dissolvation of probe 1 in water. Probe 1 is also a useful fluorescent probe for detecting thiophenols in living cells in red emission, which may greatly improve the detectable sensitivity.

Topics: Boron Compounds; Carcinoma, Hepatocellular; Contrast Media; Crystallography, X-Ray; Fluorescent Dyes; Humans; Hydrogen-Ion Concentration; Image Processing, Computer-Assisted; Limit of Detection; Liver Neoplasms; Microscopy, Fluorescence; Phenols; Sensitivity and Specificity; Sulfhydryl Compounds; Tumor Cells, Cultured

We studied the topography of Lp[a]-LDL-cell interactions by means of fluorescence microscopy, using fluorescence-labeled lipoproteins. In contrast to known methods which are based on noncovalent labeling of lipoproteins by positively charged amphiphiles, the protein moiety of LDL and Lp[a] was covalently labeled with either BODIP-succinimide-ester (green) or rhodamine X iodoacetamide (red). The interaction of the fluorescent lipoproteins with cultured HepG2 cells was studied using a confocal laser scanning fluorescence microscope. LDL and Lp[a], each labeled with a different dye, could be examined separately within a mixture of both lipoproteins during their interaction with HepG2 cells. At 4 degrees C, the majority of both fluorescent particles co-localized and only a few separate LDL- or Lp[a]-binding domains could be observed. Quantification of the amount of fluorescent lipoprotein associated with the cell surface at 4 degrees C showed that binding of Lp[a] was increased in the presence of LDL under these conditions, probably via formation of an Lp[a]-LDL complex. At 37 degrees C, LDL and Lp[a] were taken up by the cells within 10 min. Again the majority of LDL and Lp[a] particles co-localized intracellularly. Only minor amounts of LDL and Lp[a] could be observed separately. As the entire fluorescence of labeled Lp[a] co-localized with excess of LDL in cells, and taking into account the high tendency of LDL-Lp[a] association in solution and on cell surfaces, it is concluded that a significant portion of the internalized Lp[a] is taken up into the cells by the LDL receptor via LDL by a hitchhiking-like process.

Topics: Animals; Boron Compounds; Carcinoma, Hepatocellular; Cattle; Fluorescent Dyes; Humans; Lipoprotein(a); Lipoproteins, LDL; Membrane Proteins; Microscopy, Confocal; Microscopy, Fluorescence; Molecular Structure; Protein Binding; Receptors, LDL; Rhodamines; Spectrometry, Fluorescence; Tumor Cells, Cultured