RESUMO
In vitro and in vivo anti-leishmanial efficacy of copper salisylaldoxime (CuSAL), a transition metal complex, was evaluated and the underlying mechanism was studied. In vitro studies revealed that 30 µM of CuSAL causes 96% reduction in parasite burden in infected macrophages. CuSAL is least toxic in host cells. A dose of 5 mg/kg bodyweight per mice on alternate days (5 doses) gives â¼97% protection in both liver and spleen. Moreover, CuSAL potentially inhibits the catalytic activity of LdTOPILS and causes apoptosis of Leishmania parasites through induction of intracellular ROS generation and activation of caspase-like proteases. Interestingly, CuSAL does not inhibit the catalytic activity of human topoisomerase I. The present study illuminated that CuSAL, has potent anti-leishmanial activity, which selectively targets LdTOPILS; and is a safe for human. Therefore, this compound might be highly promising candidate to develop the rational approaches for chemotherapy of human leishmaniasis.
Assuntos
Antiprotozoários/farmacologia , Complexos de Coordenação/farmacologia , Leishmania donovani/efeitos dos fármacos , Leishmaniose Visceral/tratamento farmacológico , Oximas/farmacologia , Animais , Antiprotozoários/uso terapêutico , Apoptose , Caspase 3/metabolismo , Ciclo Celular/efeitos dos fármacos , Linhagem Celular Tumoral , Complexos de Coordenação/uso terapêutico , Fragmentação do DNA , Leishmania donovani/enzimologia , Leishmania donovani/crescimento & desenvolvimento , Fígado/parasitologia , Fígado/fisiopatologia , Testes de Função Hepática , Macrófagos/efeitos dos fármacos , Macrófagos/parasitologia , Camundongos , Camundongos Endogâmicos BALB C , Oximas/uso terapêutico , Espécies Reativas de Oxigênio/análise , Baço/parasitologia , Inibidores da Topoisomerase I/farmacologia , Inibidores da Topoisomerase I/uso terapêuticoRESUMO
A Fischer carbene complex was grafted onto self-assembled monolayers (SAMs) on gold or glass by a copper-free "click" reaction. Pendant lysine residues of protein A obtained from Staphylococcus aureus rapidly reacted with the electrophilic metal complex on SAM effecting a covalent attachment of protein A with the surface. The protein A coated surface further led to bioaffinity immobilization of rabbit IgG in an oriented manner, a feature that also permits its purification from rabbit serum. Rabbit IgG could be removed from protein A coated surface by pH adjustment. The regenerated protein A surface was reused three times without loss of activity.
Assuntos
Imunoglobulina G/imunologia , Membranas Artificiais , Metano/análogos & derivados , Compostos Organometálicos/imunologia , Proteína Estafilocócica A/imunologia , Animais , Química Click , Vidro/química , Ouro/química , Concentração de Íons de Hidrogênio , Imunoglobulina G/sangue , Imunoglobulina G/isolamento & purificação , Metano/química , Estrutura Molecular , Compostos Organometálicos/síntese química , Compostos Organometálicos/química , Tamanho da Partícula , Coelhos , Proteína Estafilocócica A/química , Staphylococcus aureus/química , Estereoisomerismo , Propriedades de Superfície , Tungstênio/químicaRESUMO
Fischer carbene complex anchored on glass or silicon surface using a Cu-free 'click' reaction allows facile and swift covalent grafting of protein molecules like Bovine Serum Albumin (BSA).
Assuntos
Azidas/síntese química , Proteínas Imobilizadas/química , Metano/análogos & derivados , Animais , Azidas/química , Bovinos , Compostos de Dansil/síntese química , Compostos de Dansil/química , Metano/química , Soroalbumina Bovina/química , Silicatos/síntese química , Silicatos/química , Espectrometria de FluorescênciaRESUMO
An efficient synthesis of Pd nanoparticles in water has been developed using a Fischer carbene complex of tungsten as the reductant and PEG as the capping agent. The colloidal palladium (1 mol %) efficiently catalyzes Hiyama cross-coupling reactions performed in air. Excellent yields of products were obtained with a wide range of substrates. Catalytic activity and stability of the nanoparticles were found to be inversely correlated.
RESUMO
Suitably designed, hydrophilic Fischer carbene complexes reduce HAuCl4 to produce stable gold nanoparticles localized on proteins in aqueous buffer solution.
