Project R-3508

Oriented covalent coupling of site-specific modified nanobodies onto functionalized conjugated polymers using 'click chemistry' (Research)

The quality of many biosurface applications, including biosensing systems relies on the resulting physicochemical properties of the biomolecules after immobilization on the surface. The sensitivity and selectivity of such systems are directly related to the accessibility and activity, determined by the orientation, of the immobilized biomolecules. It is well known that immobilization by physical adsorption leads to a weak reproducibility. In the last decade, much progress has been made in the field of bioactive surfaces, especially with covalently coupled DNA (fragments). However, due to diversity and multiplicity of the functional groups present in the natural amino acids, much less attention was paid to the combined covalent and oriented coupling of proteins to functionalized surfaces. A deeper understanding of it is of utmost importance towards further breakthroughs in the field of protein-based surface materials. This project aims to obtain fundamental insights about the impact of a covalent and oriented proteinsurface coupling on the interaction properties with target molecules. Therefore, proteins are sitespecifically modified and covalently coupled by click-chemistry to surfaces coated with side chain functionalized semi-conducting polymers. Nanobodies (camelid derived single-domain antibody fragments) are used as protein model system.

01 January 2012 - 31 December 2015