Asunto(s)
Condrocitos/metabolismo , Colágeno/metabolismo , Factor de Crecimiento del Tejido Conjuntivo/genética , Hiperglucemia/metabolismo , MicroARNs/efectos de los fármacos , ARN Largo no Codificante/farmacología , Transducción de Señal/efectos de los fármacos , Factor de Crecimiento Transformador beta1/genética , Anciano , Cartílago/patología , Factor de Crecimiento del Tejido Conjuntivo/efectos de los fármacos , Diabetes Mellitus/patología , Femenino , Regulación de la Expresión Génica/efectos de los fármacos , Humanos , Hipoglucemiantes/farmacología , Masculino , Persona de Mediana Edad , Osteoartritis/patología , Pioglitazona/farmacología , Cultivo Primario de Células , Factor de Crecimiento Transformador beta1/efectos de los fármacosRESUMEN
Monomethyl poly(ethylene glycol) (mPEG)-modified bovine serum albumin (BSA) conjugates (BSA-mPEG) were obtained by the mild Cu(I)-mediated cycloaddition reaction of azided BSA (BSA-N(3) ) and alkyne-terminated mPEG. The structure and characteristics of BSA-mPEG conjugates were thoroughly investigated. There were about two PEG chains conjugated onto each BSA molecule as determined by matrix-assisted laser desorption/ionization time of flight (MALDI-TOF) analysis. The intrinsic nonspecific binding ability of BSA was used for adsorption and sustained release of both rifampicn and 5-fluorouracil (5-FU). The helical structures of BSA were preserved to a large extent after modification and drug adsorption on BSA was confirmed via circular dichroism spectroscopy. Drugs adsorbed onto the conjugated formulation to a lesser extent than on BSA due to mPEG modification. The in vitro release of both rifampicin and 5-FU, however, indicated that BSA-mPEG can function as a drug carrier. Overall, the click reaction provided a convenient tool for the pegylation of BSA. The biological activity of the BSA-mPEG conjugates, including the drug transportation capacity and biocompatibility, were largely retained.