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Immobilization of cellulase on functionalized cobalt ferrite nanoparticles
Shivaji Hariba Pawar,Raghvendra Ashok Bohara,Nanasaheb Devappa Thorat 한국화학공학회 2016 Korean Journal of Chemical Engineering Vol.33 No.1
Amine functionalized cobalt ferrite (AF-CoFe2O4) magnetic nanoparticles (MNPs) were used for immobilization of cellulase enzyme via 1-ethyl-3-[3-dimethylaminopropyl] carbodiimide hydrochloride (EDS) and N-hydroxysuccinimide (NHS) coupling reaction. The structural, morphological and magnetic properties of AF-CoFe2O4 were determined. TEM micrograph revealed a mean diameter of ~8 nm and showed that the AF-CoFe2O4 remain distinct with no significant change in size after binding with cellulase. Fourier transform infrared (FT-IR) spectroscopy confirmed the binding of cellulase to AF-CoFe2O4. The properties of immobilized cellulase were investigated by optimizing binding efficiency, pH, temperature and reusability. The results showed that the immobilized cellulase has higher thermal stability than free cellulase, which might be due to covalent interaction between cellulase and AF-CoFe2O4 surface. The immobilized cellulase also showed good reusability after recovery. Therefore, AF-CoFe2O4 MNPs can be considered as promising candidate for enzyme immobilization.
Lee, Sunho,Kim, Changhoon,Ann, Jihyae,Thorat, Shivaji A.,Kim, Eunhye,Park, Jongmi,Choi, Sun,Blumberg, Peter M.,Frank-Foltyn, Robert,Bahrenberg, Gregor,Stockhausen, Hannelore,Christoph, Thomas,Lee, Jee Pergamon Press 2017 Bioorganic & medicinal chemistry letters Vol.27 No.18
<P><B>Abstract</B></P> <P>A series of 1-substituted 3-(<I>t</I>-butyl/trifluoromethyl)pyrazole C-region analogues of 2-(3-fluoro-4-methylsulfonamidophenyl)propanamides were investigated for <I>h</I>TRPV1 antagonism. The structure activity relationship indicated that the 3-chlorophenyl group at the 1-position of pyrazole was the optimized hydrophobic group for antagonistic potency and the activity was stereospecific to the <I>S</I>-configuration, providing exceptionally potent antagonists <B>13<I>S</I> </B> and <B>16<I>S</I> </B> with <I>K<SUB>i(CAP)</SUB> </I> =0.1nM. Particularly significant, <B>13<I>S</I> </B> exhibited antagonism selective for capsaicin and NADA and not for low pH or elevated temperature. Both compounds also proved to be very potent antagonists for <I>r</I>TRPV1, blocking <I>in vivo</I> the hypothermic action of capsaicin, consistent with their <I>in vitro</I> mechanism. The docking study of compounds <B>13<I>S</I> </B> and <B>16<I>S</I> </B> in our <I>h</I>TRPV1 homology model indicated that the binding modes differed somewhat, with that of <B>13<I>S</I> </B> more closely resembling that of <B>GRT12360</B>.</P> <P><B>Graphical abstract</B></P> <P>[DISPLAY OMISSION]</P>
Pearce, Larry V.,Ann, Jihyae,Jung, Aeran,Thorat, Shivaji A.,Herold, Brienna K. A.,Habtemichael, Amelework D.,Blumberg, Peter M.,Lee, Jeewoo American Chemical Society 2017 Journal of medicinal chemistry Vol.60 No.19
<P>Transient receptor potential vanilloid 1 (TRPV1) has emerged as a promising therapeutic target. While radiolabeled resiniferatoxin (RTX) has provided a powerful tool for characterization of vanilloid binding to TRPV1, TRPV1 shows 20-fold weaker binding to the human TRPV1 than to the rodent TRPV1. We now describe a tritium radiolabeled synthetic vanilloid antagonist, 1-((2-(4-(methyl-[<SUP>3</SUP>H])piperidin-1-yl-4-[<SUP>3</SUP>H])-6-(trifluoromethyl)pyridin-3-yl)methyl)-3-(3-oxo-3,4-dihydro-2<I>H</I>-benzo[<I>b</I>][1,4]oxazin-8-yl)urea ([<SUP>3</SUP>H]MPOU), that embodies improved absolute affinity for human TRPV1 and improved synthetic accessibility.</P><P><B>Graphic Abstract</B> <IMG SRC='http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jmcmar/2017/jmcmar.2017.60.issue-19/acs.jmedchem.7b00859/production/images/medium/jm-2017-008593_0010.gif'></P><P><A href='http://pubs.acs.org/doi/suppl/10.1021/jm7b00859'>ACS Electronic Supporting Info</A></P>