Recombinant proteins are of great importance in several biological key processes. On the engineer point of view, their specific binding properties are of great interest and are widely used in biosensing. Since their bioactivity and efficiency are related to their conformation, a better understanding of their behaviour and organization at interfaces is needed in optimizing their use for such purposes. The present study was undertaken in order to get a better knowledge of recombinant Protein G molecular organization using the air/water interface as a model system. Surface pressure isotherms, PM-IRRAS and circular dichroism were used to monitor the impact of surface concentration on the molecular organization of the recombinant Protein G. Its maximal insertion pressure (MIP) in a self-assembled monolayer of PS-PEO block copolymer was determined. Such a system presents the advantages of combining bioactivity and reduction of non-specific interactions.

Behaviour of a recombinant protein G at the air/water interface

247th National Meeting (2014)

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.