RESUMO
Mannan and carboxymethylcellulose, previously activated by periodate oxidation, were grafted with mono-6-butylenediamino-6-deoxy-beta-cyclodextrin derivatives by reductive alkylation in the presence of sodium borohydride. The formation of supramolecular complexes between these polymers and Naproxen was confirmed by fluorescence spectroscopy. The solubility of the drug was 3.8-4.6 fold increased in the presence of the cyclodextrin-grafted polysaccharides. The in vivo anti-inflammatory property of Naproxen was 1.7 times higher after supramolecular association with beta-cyclodextrin-branched mannan.
Assuntos
Anti-Inflamatórios não Esteroides/química , Anti-Inflamatórios não Esteroides/farmacologia , Carboximetilcelulose Sódica/química , Ciclodextrinas/química , Mananas/química , Naproxeno/química , Naproxeno/farmacologia , Animais , Anti-Inflamatórios não Esteroides/síntese química , Carragenina/metabolismo , Fluorescência , Espectroscopia de Ressonância Magnética , Masculino , Naproxeno/síntese química , Ratos , Ratos Wistar , SolubilidadeRESUMO
Bovine liver catalase (EC 1.11.1.6) was chemically modified with mannan, carboxymethylcellulose, and carboxymethylchitin. The enzyme retained about 48-97% of the initial specific activity after glycosidation with the polysaccharides. The prepared neoglycoenzyme was 1.9-5.7 fold more stable against the thermal inactivation processes at 55 degrees C, in comparison with the native counterpart. Also, the modified enzyme was more resistant to proteolytic degradation with trypsin. Pharmacokinetics studies revealed higher plasma half-life time for all the enzyme-polymer preparations, but better results were achieved for the enzyme modified with the anionic macromolecules.
Assuntos
Catalase/farmacocinética , Polissacarídeos/química , Animais , Área Sob a Curva , Sequência de Carboidratos , Carboximetilcelulose Sódica/química , Carboximetilcelulose Sódica/metabolismo , Catalase/administração & dosagem , Catalase/química , Bovinos , Estabilidade Enzimática , Meia-Vida , Temperatura Alta , Concentração de Íons de Hidrogênio , Injeções Intravenosas , Fígado/enzimologia , Masculino , Dados de Sequência Molecular , Estrutura Molecular , Ratos , Ratos Wistar , Solubilidade , Espectrofotometria , Especificidade por Substrato , Água/químicaRESUMO
O-carboxymethylchitin (molecular weight = 1.07 x 10(5), degree of carboxymethylation = 80%, degree of N-acetylation = 91%) was chemically attached to superoxide dismutase by the formation of amide linkages through a carbodiimide catalyzed reaction. The glycosidated enzyme contained about 1.8 mole of polysaccharide per mole of protein and retained 57% of the initial catalytic activity. The anti-inflammatory activity of the enzyme was 2.4 times increased after conjugation with the polysaccharide. The modified superoxide dismutase preparation was remarkably more resistant to inactivation with H(2)O(2) and its plasma half-life time was prolonged from 4.8 min to 69 h.