Researchers from Ludwig-Maximilians-Universitaet (LMU) in Munich, together with colleagues based in Berlin, have developed a rapid and efficient technique for targeted chemoenzymatic functionalization of proteins. The new method has a wide range of potential therapeutic applications. Selective intermolecular recognition is at the heart of all biological processes. Thus, proteins that bind specifically to complementary chemical structures are also indispensable for many biochemical and biotechnological applications. Targeted modification of such proteins therefore plays a significant role in medical diagnostics and therapies. Now, researchers led by Professor Heinrich Leonhardt at LMU's Biocenter and Professor Christian Hackenberger of the Leibniz Institute for Molecular Pharmacology in Berlin have developed a new strategy that permits specific chemical modification of virtually any protein more rapidly and more efficiently than was hitherto possible. Their results were published online on September 25, 2015 in the journal Angewandte Chemie. The article is titled “Versatile and Efficient Site-Specific Protein Functionalization by Tubulin Tyrosine Ligase.” Many of the methods routinely used in the biosciences are based on the specific modification of proteins, in particular antibodies, to endow them with novel properties for specific purposes. For example, chemotherapeutic agents used in the treatment of cancer are often chemically linked to antibodies that recognize antigens found only on the surface of the target tumor. In this way, the cytoxic drug can be delivered directly to the cells it is intended to eradicate. Ideally, the methods used to introduce such modifications should be as specific, efficient and versatile as possible. Unfortunately, the techniques currently in use fulfill these criteria only in part.
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