Recombinant antibody technology is considered a fast and inexpensive method to recover new binders. It is also acknowledged that it enables to expand the repertoire represented by natural binders issued from immunization. This improvement can be realized by forcing the system at different levels: i) design of the library in terms of dimension and structural characteristics; ii) panning and screening conditions for selecting antibodies with specific biophysical features; iii) in vitro and in silico maturation procedures paired to molecular engineering for optimizing the binders in the function of their final applications.
In many cases, the advancement in this research field has been the consequence of applying in creative form combinations of methodologies which initially developed separately. Examples are the alternate use of phage and yeast/ribosomal/bacterial display, the introduction of rational mutagenesis based on computational modeling to optimize the initial hits recovered by conventional panning, the use of automated systems that allow the analysis of huge amounts of biochemical (from ELISA, flow-cytometry, affinity measurement) and NGS data. These approaches simplified the isolation of antibodies for difficult targets (membrane proteins, toxic and non-immunogenic targets), specific applications (structural chaperones, allosteric inhibitors, detectors of structural conformation), and better biophysical characteristics (higher stability and yields, stronger and more selective binding, lower immunogenicity).
This special issue presents significant examples of some of these achievements and therefore should inspire to further challenge the potential of recombinant antibody technology.
Edited by Ario de Marco, University of Nova Gorica, Slovenia. If you are interested in contributing to the Special Issue, please contact the Editor: Ario.DeMarco@ung.si.