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  • ISSN: 2379-089X
    Volume 2, Issue 1
    Research Article
    Toshihiko Hanai*
    Abstract: The enzyme activity of alcohol dehydrogenases 4W6Z and 1MG5 demonstrated good agreement with the calculated a-carbon atomic partial charges of the substrates. The correlation coefficients were found to be more than 0.8 (n = 9) for both the oxidation and reduction reactions. The stereo structure of cinnamylalcohol dehydrogenase (ELI3-2) was constructed modification in 1PIW (cinnamyl alcohol dehydrogenase) structure. The enzyme activity of ELI3-2 was related to the atomic partial charges on the aldehyde a-carbon atom (r = 0.785, n = 6). The oxidation process was an electron transfer-deprotonation reaction, whereas the reduction process involved direct protonation. A combination of the molecular mechanics and MOPAC-PM5 programs was used for the quantitative analysis of the enzyme reactivity.
    Gulseren Petek Sen-Caglar1, Serap Yalcin2 and Ufuk Gunduz1*
    Abstract: The TAT peptide is a drug delivery tools which has been efficiently proven to deliver drugs, peptides and nucleic acids. A specific sequence of HIV1 protein transduction domain TAT was evaluated for its ability to carry Doxorubicin (Dox) into drug resistant MCF-7 tumor cells. TAT was conjugated to Dox via the formation of a disulfide bond. In this study, we developed an optimal formulation for the conjugation of Dox by this delivery system for tumor treatment. The in vitro study showed that Dox-TAT peptide conjugate was only more potent than free drug at higher concentration on Dox resistance cells. The concentration of drug in resistant cancer cells was increased indicating a partial reversal of drug resistance.
    Sitansu Kumar Verma1*, Soni Yadav1 and Ajay Kumar2
    Abstract: Lassa fever is an acute viral zoonotic illness caused by Lassa virus, a member of the Arenaviridae family and responsible for a severe hemorrhagic fever characterized by fewer, sour throat, muscle pain, nausea. In this work, we performed virtual screening against Nucleoprotein with entire 45 analogs compounds from Zinc Database using Auto Dock 4.2 software. These complexes were ranked according to their docking score, using methodology that was shown to achieve maximum accuracy. Finally we got six potent compounds with the best Auto dock docking Score. These six compounds were analyzed through Python Molecular Viewer for their interaction studies. From the docking result it was observed that ZINC79045769, ZINC04900951, ZINC21986245, ZINC75626110 have the lowest docking energy and thus have potential to inhibit the activity of nucleoprotein of Lassa virus. A 2-D pharmacophore was generated for these analogs using LigandScout to confirm it. A shared feature pharmacophore was also constructed that shows four common features (one hydrogen bond Donar, Two hydrogen bond Acceptor and one ionizable area) help compounds to interact with this enzyme.
    Mohammed Ali*
    Abstract: The dry powder inhaler (DPI) is a popular, effective and convenient drug delivery device for inhalation therapy to treat asthma. However, a large quantity (approximately 54%) of inhaled aerosols deposit in the oropharyngeal region. Deposition in this region is undesirable because it provides minimum therapeutic benefits and has adverse localized or systemic side effects. This study reports a method of examining electrostatic charge effects on deposition of three DPI aerosols (Spiriva™ Handihaler, Advair Diskus™, and Pulmicort™ Turbohaler) in a cadaver-based cast of the human oral-pharyngeal-laryngeal (OPL) regions. Experimental aerosols were generated from the three commercially available DPIs by means of inhalation as boluses, and then characterized with an electronic single particle aerodynamic relaxation time analyzer with or without passing through the OPL regions. The results showed that aerosol particles were not only of different sizes but also carried different positive, negative and zero electrostatic charges. The deposition fraction of total particles (charged and uncharged) in the OPL regions for the Spiriva, Advair and Pulmicort were 22%, 61% and 7%, respectively, whereas the deposition fraction of charged particles in the Spiriva, Advair and Pulmicort generated aerosols were 62%, 67% and 28%, respectively. The inherent net charge to mass ratio were Spiriva 0.76 ± 0.11 µC/g (negative), Advair Diskus 0.49 ± 0.3 µC/g (negative), and Pulmicort 0.46 ± 0.02 (µC/g (negative), respectively. The study results also revealed that inherent charges of smaller (aerodynamic diameter, da < 2.0 ∝m) particles influenced their agglomeration, and therefore, increased their deposition due to inertial impaction and electrostatic space charge forces. In addition, the deposition fraction of these charged particles rapidly increased for Spiriva and Advair but marginally increased for Pulmicort with increasing particle sizes. Electromechanical properties (both aerodynamic size and electrostatic charge) play significant roles in the deposition of dry powder inhaler aerosols in the human oral-pharyngeal-laryngeal regions.
    Karel Bastl1, Sylvie Skalickova1, Zbynek Heger1,2, Ondrej Zitka1,2, Vojtech Adam1,2 and Rene Kizek1,2*
    Abstract: Influenza is a highly pathogenic virus well known by a higher mutation rate, resulted from antigenic drift and shift of its surface proteins. The hemagglutinin- influenza major virus surface protein is responsible for viral entry through targeting sialic acid present on the lipid membrane of the host cell. Nowadays, peptides become the perspective therapeutic agents for various infection diseases including influenza. Utilization of peptides could provide high specifity, attained by a number of possible modifications, which can be simply proposed by using in silico modeling.
    Molecular modeling of peptides with high affinity towards sialic acid binding site of influenza hemagglutinin may be thus helpful for inhibition of viral entry. Hence, we employed Yasara program for molecular modeling to estimate a binding energy of selected peptides to specific hemagglutinin binding site in the amino acids range of 116 – 261. We designed a mimicking peptide with sequence WLVFFVIFYIFR showing binding energy 412.669 kcal/mol, which could be suitable to inhibit the influenza infection.
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