Navegando por Autor "Paula, Sergio O. de"
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Item Complete genome sequence of vB_EcoM-UFV13, a new bacteriophage able to disrupt Trueperella pyogenes biofilm(Genome Announcements, 2016-12-08) Duarte, Vinícius S.; Dias, Roberto S.; Kropinski, Andrew M.; Vidigal, Pedro M. P.; Sousa, Flávia O.; Sousa, Flávia O.; Xavier, André S.; Silva, Cynthia C.; Paula, Sergio O. devB_EcoM-UFV13, a member of the T4virus genus, shows lytic activity against Escherichia coli and effectiveness in controlling the biofilm formed by Trueperella pyogenes, which qualifies it as a promising component of phage cocktails for mastitis and metritis control.Item Zirconium catalyzed synthesis of 2-arylidene Indan-1,3-diones and evaluation of their inhibitory activity against NS2B-NS3 WNV protease(European Journal of Medicinal Chemistry, 2018-04-10) Oliveira, Ana Flávia C. da S.; Souza, Ana Paula M. de; Oliveira, André S. de; Silva, Milene L. da; Oliveira, Fabrício M. de; Santos, Edjon G.; Silva, Ítalo Esposti P. da; Ferreira, Rafaela S.; Villela, Filipe S.; Martins, Felipe T.; Leal, Daniel H.S.; Vaz, Boniek G.; Teixeira, Róbson R.; Paula, Sergio O. deA simple and efficient Knoevenagel procedure for the synthesis of 2-arylidene indan-1,3-diones is herein reported. These compounds were prepared via ZrOCl2·8H2O catalyzed reactions of indan-1,3-dione with several aromatic aldehydes and using water as the solvent. The 2-arylidene indan-1,3-diones were obtained with 53%-95% yield within 10–45 min. The synthesized compounds were evaluated as inhibitors of the NS2B-NS3 protease of West Nile Virus (WNV). It was found that hydroxylated derivatives impaired enzyme activity with varying degrees of effectiveness. The most active hydroxylated derivatives, namely 2-(4-hydroxybenzylidene)-1H-indene-1,3(2H)-dione (14) and 2-(3,4-dihydroxybenzylidene)-1H-indene-1,3(2H)-dione (17), were characterized as noncompetitive enzymes inhibitors, with IC50 values of 11 μmol L−1 and 3 μmol L−1, respectively. Docking and electrostatic potential surfaces investigations provided insight on the possible binding mode of the most active compounds within an allosteric site.
