Refolding
For proteins expressed in E. coli as inclusion bodies, we have developed a custom matrix-based refolding approach (potentially compatible with GMP production process). This refolding study is based on an advanced preparation of inclusion bodies combined with the screening of up to 128 conditions including:
Example
of Refolding Project
Human Metalloprotease MMP-12 Refolding
Morales R, Perrier S, Florent JM, Beltra J, Dufour S, De Mendez I, Manceau P, Tertre A, Moreau F,
Compere D, Dublanchet AC, O’Gara M, (2004), Journal of Molecular Biology, 341(4), 1063-1076
Human macrophage elastase (MMP-12) plays an important role in inflammatory processes
and has been implicated in diseases such as emphysema and chronic obstructive pulmonary disease (COPD). It is therefore an attractive target for therapeutic agents.
By using our protein engineering and refolding tools, we have designed a MMP-12 protease
domain compatible with X-Ray structure resolution.
For proteins expressed in E. coli as inclusion bodies, we have developed a custom matrix-based refolding approach (potentially compatible with GMP production process). This refolding study is based on an advanced preparation of inclusion bodies combined with the screening of up to 128 conditions including:
| • protein
concentration • buffer • pH |
• redox potential • ionic strength • divalent cations |
Example
of Refolding ProjectHuman Metalloprotease MMP-12 Refolding
Morales R, Perrier S, Florent JM, Beltra J, Dufour S, De Mendez I, Manceau P, Tertre A, Moreau F,
Compere D, Dublanchet AC, O’Gara M, (2004), Journal of Molecular Biology, 341(4), 1063-1076
Human macrophage elastase (MMP-12) plays an important role in inflammatory processes
and has been implicated in diseases such as emphysema and chronic obstructive pulmonary disease (COPD). It is therefore an attractive target for therapeutic agents.
By using our protein engineering and refolding tools, we have designed a MMP-12 protease
domain compatible with X-Ray structure resolution.