Christoph Hiemenz
Ruprecht Karls-University Heielberg, Europe
Title: Application of modular chemoenzymatic conjugation strategies for the semi-rational engineering of biologicals
Biography
Biography: Christoph Hiemenz
Abstract
Binder drug conjugates such as antibody-drug conjugates have led to major improvements of personalized therapy of diseases such as cancer, autoimmunity and pathogenic virulence. The underlying methods which enable the position specific functionalization or semi-rational mutagenesis of bioactive proteins have been the key innovations. While academic research groups are already managing to computationally design small bioactive peptides, the majority of protein engineering projects are still relying on semi-rational directed evolution to identify the protein with desirable properties. Here a main leap forward has been the site-directed post-translational mutagenesis of proteins by means of state-of-the-art bioconjugation methods including enzymatic sortase A transpeptidation and chemical indium catalyzed the mild radical addition of diverse iodoalkanes to sp2-hybridized amino acids. Above all, a multitude of chemoenzymatic functionalization methods are continuously being improved and are fully compatible with directed evolution via cell surface display library screenings