TY - JOUR
T1 - The effects of dodecyl maltoside and sodium dodecyl sulfate surfactants on the stability and aggregation of recombinant interferon Beta-1b
AU - Haji Abdolvahab, Mohadeseh
AU - Fazeli, Ahmad
AU - Fazeli, Mohammad Reza
AU - Brinks, Vera
AU - Schellekens, Huub
PY - 2014/11
Y1 - 2014/11
N2 - Aggregation often occurs during manufacturing and storage of protein drugs. Detergents such as sodium dodecyl sulfate are commonly used to prevent aggregation but need to be eliminated before final formulation for safety reasons. We studied the ability of dodecylmaltoside (DDM), a nontoxic alkyl saccharide surfactant, to reduce aggregation and increase the stability of interferon beta-1b (IFN)-β-1b. An increase of 8°C in the Tm of IFN-β-1b was observed when 0.1% of DDM was present in the protein solution. The absorption of DDM on hydrophobic surfaces of IFN-β-1b enables the surface to become hydrophilic and non-ionic, and increases the stability of the protein. 0.1% DDM also results in a 62% increase in helical and a 25% decrease in β-sheet structures. 0.1% DDM not only suppresses aggregate formation but also improves IFN-β-1b solubilization. Furthermore, we have showed the protective effect of DDM on the anti-viral activity of IFN-β-1b in solution.
AB - Aggregation often occurs during manufacturing and storage of protein drugs. Detergents such as sodium dodecyl sulfate are commonly used to prevent aggregation but need to be eliminated before final formulation for safety reasons. We studied the ability of dodecylmaltoside (DDM), a nontoxic alkyl saccharide surfactant, to reduce aggregation and increase the stability of interferon beta-1b (IFN)-β-1b. An increase of 8°C in the Tm of IFN-β-1b was observed when 0.1% of DDM was present in the protein solution. The absorption of DDM on hydrophobic surfaces of IFN-β-1b enables the surface to become hydrophilic and non-ionic, and increases the stability of the protein. 0.1% DDM also results in a 62% increase in helical and a 25% decrease in β-sheet structures. 0.1% DDM not only suppresses aggregate formation but also improves IFN-β-1b solubilization. Furthermore, we have showed the protective effect of DDM on the anti-viral activity of IFN-β-1b in solution.
U2 - 10.1089/jir.2013.0131
DO - 10.1089/jir.2013.0131
M3 - Article
C2 - 24956236
SN - 1079-9907
VL - 34
SP - 894
EP - 901
JO - Journal of interferon & cytokine research
JF - Journal of interferon & cytokine research
IS - 11
ER -