Long interest in affinity protein biotechnology, including different aspects of the broad field such as affinity chromatography, diagnostics, serum half-life extension of biologicals, biotherapy, protein expresssion. Extensive track record concerning work with natural and engineered forms of bacterial serum protein binding proteins, incl. in particular the immunoglobulin binding regions of staphylococcal protein A (SPA) and the serum albumin regions of streptococcal protein G (SPG).
Leading the group introducing the concept of affibody binding proteins in the mid 1990´s, i.e. using combinatorial protein engineering and protein library technology to develop novel non-immunoglobulin binding proteins based on a SPA-derived three-helix bundle scaffold domain (Nord et al. (1997) Nature Biotechnology. 304 citations).
The focus on affinity protein technology has continued and in later years involved investigations of different applications for engineered variants of developed affinity proteins, incl. use as capture probes in protein microarrays, as fluorescently labeled reagents in homogenous diagnostic assays, as ligands in affinity chromatography, intracellularly expressed binders, as affinity proteins as reagents in cancer diagnostics and as protein biologicals for therapy, incl. ultra-high affinity serum albumin binding domains for half-life extension of fused proteins. These activities have been accompanied by parallel studies towards refinement and development of different protein library selection systems, incl. phage display, protein fragment complementation assay (PCA), microbead display and ribosome display.