Liposome-based drug delivery systems hold great potential for cancer therapy. The aim of this study was to design a nanodevice for targeted anchoring of liposomes (with and without cholesterol) with encapsulated anticancer drugs and antisense N-myc gene oligonucleotide attached to its surface. To meet this main aim, liposomes with encapsulated doxorubicin, ellipticine and etoposide were prepared. They were further characterized by measuring their fluorescence intensity, whereas the encapsulation efficiency was estimated to be 16%. The hybridization process of individual oligonucleotides forming the nanoconstruct was investigated spectrophotometrically and electrochemically. The concentrations of ellipticine, doxorubicin and etoposide attached to the nanoconstruct in gold nanoparticle-modified liposomes were found to be 14, 5 and 2 µg·mL(-1), respectively. The study succeeded in demonstrating that liposomes are suitable for the transport of anticancer drugs and the antisense oligonucleotide, which can block the expression of the N-myc gene.

• Keywords
• N-myc, doxorubicin, ellipticine, etoposide, gold nanoparticles, liposome,
• MeSH
• DNA, Antisense chemistry   therapeutic use   MeSH
• Doxorubicin chemistry   therapeutic use   MeSH
• Ellipticines chemistry   therapeutic use   MeSH
• Etoposide chemistry   therapeutic use   MeSH
• Fluorescence MeSH
• Drug Delivery Systems * MeSH
• Humans MeSH
• Liposomes chemistry   therapeutic use   MeSH
• Magnetite Nanoparticles chemistry   therapeutic use   MeSH
• Neoplasms drug therapy   MeSH
• N-Myc Proto-Oncogene Protein antagonists & inhibitors   genetics   MeSH
• Gold chemistry   MeSH
• Check Tag
• Humans MeSH
• Publication type
• Journal Article MeSH
• Research Support, Non-U.S. Gov't MeSH
• Names of Substances
• DNA, Antisense MeSH
• Doxorubicin MeSH
• Ellipticines MeSH
• Etoposide MeSH
• Liposomes MeSH
• Magnetite Nanoparticles MeSH
• N-Myc Proto-Oncogene Protein MeSH
• Gold MeSH

In this study we describe a beads-based assay for rapid, sensitive and specific isolation and detection of influenza vaccine hemagglutinin (HA). Amplification of the hemagglutinin signal resulted from binding of an electrochemical label as quantum dots (QDs). For detection of the metal and protein part of the resulting HA-CdTe complex, two differential pulse voltammetric methods were used. The procedure includes automated robotic isolation and electrochemical analysis of the isolated product. The isolation procedure was based on the binding of paramagnetic particles (MPs) with glycan (Gly), where glycan was used as the specific receptor for linkage of the QD-labeled hemagglutinin.

• MeSH
• Staining and Labeling * MeSH
• Biosensing Techniques * MeSH
• Electrochemical Techniques * MeSH
• Hemagglutinin Glycoproteins, Influenza Virus chemistry   MeSH
• Quantum Dots chemistry   MeSH
• Humans MeSH
• Tellurium chemistry   MeSH
• Influenza Vaccines MeSH
• Animals MeSH
• Check Tag
• Humans MeSH
• Animals MeSH
• Publication type
• Journal Article MeSH
• Research Support, Non-U.S. Gov't MeSH
• Names of Substances
• Hemagglutinin Glycoproteins, Influenza Virus MeSH
• Tellurium MeSH
• Influenza Vaccines MeSH

In this study, we focused on microfluidic electrochemical analysis of zinc complexes (Zn(phen)(his)Cl2, Zn(his)Cl2) and ZnS quantum dots (QDs) using printed electrodes. This method was chosen due to the simple (easy to use) instrumentation and variable setting of flows. Reduction signals of zinc under the strictly defined and controlled conditions (pH, temperature, flow rate, accumulation time and applied potential) were studied. We showed that the increasing concentration of the complexes (Zn(phen)(his)Cl2, Zn(his)Cl2) led to a decrease in the electrochemical signal and a significant shift of the potential to more positive values. The most likely explanation of this result is that zinc is strongly bound in the complex and its distribution on the electrode is very limited. Changing the pH from 3.5 to 5.5 resulted in a significant intensification of the Zn(II) reduction signal. The complexes were also characterized by UV/VIS spectrophotometry, chromatography, and ESI-QTOF mass spectrometry.

• Publication type
• Journal Article MeSH
• Research Support, Non-U.S. Gov't MeSH

Since its first official detection in the Guangdong province of China in 1996, the highly pathogenic avian influenza virus of H5N1 subtype (HPAI H5N1) has reportedly been the cause of outbreaks in birds in more than 60 countries, 24 of which were European. The main issue is still to develop effective antiviral drugs. In this case, single point mutation in the neuraminidase gene, which causes resistance to antiviral drug and is, therefore, subjected to many studies including ours, was observed. In this study, we developed magnetic electrochemical bar code array for detection of single point mutations (mismatches in up to four nucleotides) in H5N1 neuraminidase gene. Paramagnetic particles Dynabeads® with covalently bound oligo (dT)₂₅ were used as a tool for isolation of complementary H5N1 chains (H5N1 Zhejin, China and Aichi). For detection of H5N1 chains, oligonucleotide chains of lengths of 12 (+5 adenine) or 28 (+5 adenine) bp labeled with quantum dots (CdS, ZnS and/or PbS) were used. Individual probes hybridized to target molecules specifically with efficiency higher than 60%. The obtained signals identified mutations present in the sequence. Suggested experimental procedure allows obtaining further information from the redox signals of nucleic acids. Moreover, the used biosensor exhibits sequence specificity and low limits of detection of subnanogram quantities of target nucleic acids.

• MeSH
• Point Mutation * MeSH
• Electrochemical Techniques methods   MeSH
• Humans MeSH
• Magnetics methods   MeSH
• Mutant Proteins genetics   MeSH
• Neuraminidase genetics   MeSH
• DNA Barcoding, Taxonomic methods   MeSH
• Virology methods   MeSH
• Drug Resistance, Viral MeSH
• Viral Proteins genetics   MeSH
• Influenza A Virus, H5N1 Subtype classification   enzymology   genetics   MeSH
• Animals MeSH
• Check Tag
• Humans MeSH
• Animals MeSH
• Publication type
• Journal Article MeSH
• Geographicals
• China MeSH
• Names of Substances
• Mutant Proteins MeSH
• NA protein, influenza A virus MeSH Browser
• Neuraminidase MeSH
• Viral Proteins MeSH