Lanthio Pharma and MorphoSys scientists publish lanthipeptide phage display in Nature Communications

December 19, 2017 / 12:00 am, CET

Scientists of Lanthio Pharma and MorphoSys have published a joint article about phage display of lanthipeptides in Nature Communications. The presented proprietary platform synergistically combines MorphoSys’s unique expertise in phage display and library diversification of monoclonal antibodies with Lanthio Pharma’s knowledge on lanthipeptide biosynthesis. The resulting very impactful technology provides an effective tool to identify novel lanthipeptides with therapeutic potential. Lanthio Pharma is generating lanthipeptides, a new class of cyclical peptides, which have been engineered to achieve enhanced stability and selectivity.


Dr. Gert Moll, CSO and Managing Director of Lanthio Pharma, commented: “We are very pleased that we published this article in such a high ranked journal as Nature Communication. This certainly reflects the great scientific impact and innovation potential that lies in Lanthio Pharma’s proprietary platform technology. We have thus developed an innovative technology which provides an effective tool to identify novel lanthipeptides with therapeutic potential.”


The constrained cyclic structure of lanthipeptides enhances target specificity and confers drug-like properties, including proteolytic stability and improved in vivo half-life. In the now reported study, the enzymatic lanthipeptide biosynthesis pathway from the marine cyanobacterium Prochlorococcus MIT9313 was transferred to phage-producing cells to enable the display of highly diverse lanthipeptide libraries with ~ 100 million variants on the phage surface. Selection of lanthipeptide phage display libraries resulted in the identification of novel, highly specific, and cyclic lanthipeptides recognizing target molecules of choice, as exemplified in the study. To adapt phage display to the engineering of lanthipeptides, a rather unconventional mode of display on the carboxy-terminus of the phage minor coat protein was employed. The carboxy-terminal display was found to be instrumental to allow for prolonged interaction of lanthipeptide precursors with the modifying enzymes, to ensure efficient introduction of the characteristic thioether-bridges prior to phage assembly, and to support the display of extensively post-translationally modified peptides on the phage surface.

Links: article, supplementary information