作者: Reza Aboofazeli , Nastaran Nafissi-Varcheh , Faranak Salmannejad , Alireza Shafaati
关键词:
摘要: A major problem in the formulation of therapeutic proteins is irreversible protein aggregation. Recombinant human interferon alpha2b (rhIFNα2b) has poor stability and undergoes physical degradation. The aim this study was to investigate effect solution conditions on heat-induced aggregation rhIFNα2b. incubated for 1 h at 40–70 °C up 240 50 its tendency then studied using optical density (at 350 nm), SE-HPLC, dynamic light scattering SDS-PAGE methods. various pH (5, 6 7) buffer concentrations (10, 55 100 mM) following incubation 72 also evaluated. results obtained samples showed that OD amount higher molecular weight aggregates (HMW) increased monomer content decreased significantly (p<0.05) as time increased. Following temperatures, a significant increase , drop HMW were observed (p<0.05). Data from confirmed regardless concentration, percentage than 7 5 At constant pH, although not significant, same trend when concentration mM. In conclusion, change can influence extent rhIFN α2b.