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.

• Klíčová slova
• N-myc, doxorubicin, ellipticine, etoposide, gold nanoparticles, liposome,
• MeSH
• antisense DNA chemie   terapeutické užití   MeSH
• doxorubicin chemie   terapeutické užití   MeSH
• elipticiny chemie   terapeutické užití   MeSH
• etoposid chemie   terapeutické užití   MeSH
• fluorescence MeSH
• lékové transportní systémy * MeSH
• lidé MeSH
• liposomy chemie   terapeutické užití   MeSH
• magnetické nanočástice chemie   terapeutické užití   MeSH
• nádory farmakoterapie   MeSH
• protoonkogen n-myc antagonisté a inhibitory   genetika   MeSH
• zlato chemie   MeSH
• Check Tag
• lidé MeSH
• Publikační typ
• časopisecké články MeSH
• práce podpořená grantem MeSH
• Názvy látek
• antisense DNA MeSH
• doxorubicin MeSH
• elipticiny MeSH
• etoposid MeSH
• liposomy MeSH
• magnetické nanočástice MeSH
• protoonkogen n-myc MeSH
• zlato 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
• barvení a značení * MeSH
• biosenzitivní techniky * MeSH
• elektrochemické techniky * MeSH
• hemaglutininové glykoproteiny viru chřipky chemie   MeSH
• kvantové tečky chemie   MeSH
• lidé MeSH
• telur chemie   MeSH
• vakcíny proti chřipce MeSH
• zvířata MeSH
• Check Tag
• lidé MeSH
• zvířata MeSH
• Publikační typ
• časopisecké články MeSH
• práce podpořená grantem MeSH
• Názvy látek
• hemaglutininové glykoproteiny viru chřipky MeSH
• telur MeSH
• vakcíny proti chřipce 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.

• Publikační typ
• časopisecké články MeSH
• práce podpořená grantem 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
• bodová mutace * MeSH
• elektrochemické techniky metody   MeSH
• lidé MeSH
• magnetismus metody   MeSH
• mutantní proteiny genetika   MeSH
• neuraminidasa genetika   MeSH
• taxonomické DNA čárové kódování metody   MeSH
• virologie metody   MeSH
• virová léková rezistence MeSH
• virové proteiny genetika   MeSH
• virus chřipky A, podtyp H5N1 klasifikace   enzymologie   genetika   MeSH
• zvířata MeSH
• Check Tag
• lidé MeSH
• zvířata MeSH
• Publikační typ
• časopisecké články MeSH
• Geografické názvy
• Čína MeSH
• Názvy látek
• mutantní proteiny MeSH
• NA protein, influenza A virus MeSH Prohlížeč
• neuraminidasa MeSH
• virové proteiny MeSH