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1.
Anaerobe ; 24: 43-8, 2013 12.
Artigo em Inglês | MEDLINE | ID: mdl-24036421

RESUMO

Staphylococcus aureus a natural inhabitant of nasopharyngeal tract survives in the host as biofilms. In the present study S. aureus ATCC12600 grown under anaerobic conditions showed biofilm units of 0.086 as compared to 0.07 when this pathogen grown in aerobic conditions with elevated lactate formation and the same was also observed with increased biofilm units of 0.06, 0.084 and 0.167 under 0.05%, 0.1% and 0.15% glucose supplementation in BHI broth. The lactate dehydrogenase (LDH) gene which catalyzes the formation of lactate was cloned, sequenced (Accession Numbers: JN645813) and expressed in Escherichia coli DH5α. The pure recombinant LDH exhibited molecular weight of 34 kDa in SDS-PAGE and the enzyme kinetics of recombinant enzyme was found to be in the direction of lactate to pyruvate Km of 2.03 ± 0.025 µM and Kcat of 1.69 ± 0.03/min and from pyruvate to lactate Km of 1.62 ± 0.10 µM and Kcat of 1.75 ± 0.03/min. In the LDH gene sequence "LKDIMA" was found to be conserved in all Gram positive bacteria and in all human LDH isoforms even though only 39% sequence homology was observed with all human LDH isoforms. However, 92% structural homology was observed with all human LDH isoforms. The molecular docking of pyruvate and lactate to the LDH structure showed -10.298 for pyruvate while -9.297 for lactate indicating higher affinity of pyruvate compared to lactate which concurred with the elevated LDH kinetics and rate of biofilm units in anaerobic conditions.


Assuntos
L-Lactato Desidrogenase/isolamento & purificação , L-Lactato Desidrogenase/metabolismo , Staphylococcus aureus/enzimologia , Motivos de Aminoácidos , Clonagem Molecular , Sequência Conservada , DNA Bacteriano/química , DNA Bacteriano/genética , Escherichia coli/genética , Expressão Gênica , Humanos , Cinética , L-Lactato Desidrogenase/química , L-Lactato Desidrogenase/genética , Ácido Láctico/metabolismo , Simulação de Acoplamento Molecular , Dados de Sequência Molecular , Peso Molecular , Ácido Pirúvico/metabolismo , Proteínas Recombinantes/química , Proteínas Recombinantes/genética , Proteínas Recombinantes/isolamento & purificação , Proteínas Recombinantes/metabolismo , Análise de Sequência de DNA , Staphylococcus aureus/genética
2.
Antiviral Res ; 95(2): 118-27, 2012 Aug.
Artigo em Inglês | MEDLINE | ID: mdl-22659095

RESUMO

A series of novel substituted dihydropyrimidine and 5H-thiazolo [3, 2-a] pyrimidine derivatives were designed and synthesized as a potential target to discover drugs fighting against the viral diseases. The main objective of the present work is to carry out the QSAR studies for all the series of the compounds starting from 4a to 6j to find out their molecular descriptors and predict the biological properties. All of them are showing the best QSAR descriptors, hence chosen for the prediction of anti-viral activity against Newcastle disease virus (NDV). Initially their inhibitory activity was predicted by molecular docking of these compounds against haemaglutinin-neuraminidase (HN) protein using molecular operating environment (MOE) software. Based on the best affinity and highest docking scores 4b, 5b and 6b were assayed in vivo on NDV infected chicks and it was found that there is significant improvement in the survival of the chicks with the treatment (P<0.05). 4b and 6b showed better curative effect than 5b at the dose concentration of 40 mg/kg body weight of chicks. The results from molecular docking study and biological assays can be inferred to consider these molecules as potential antiviral drugs.


Assuntos
Antivirais/química , Antivirais/farmacologia , Vírus da Doença de Newcastle/efeitos dos fármacos , Pirimidinas/química , Pirimidinas/farmacologia , Animais , Antivirais/administração & dosagem , Galinhas , Simulação de Dinâmica Molecular , Doença de Newcastle/tratamento farmacológico , Doenças das Aves Domésticas/tratamento farmacológico , Pirimidinas/administração & dosagem , Relação Quantitativa Estrutura-Atividade , Análise de Sobrevida
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