CBF team
Chemical Biology of Flatworms: Identifying the molecular determinants of Schistosoma mansoni reproduction

With a size smaller than 10 kDa and a stable tertiary structure, miniproteins are complementary in many aspects to small molecules or large protein scaffolds for drug development. An asset of miniproteins is that they can be accessed through chemical synthesis, which enable introducing a large diversity of modifications, including those that are not managed by living systems. The increasing interest of the pharma industry for miniproteins is also stimulated by the significant advances in the chemical synthesis of proteins, an innovation process to which our team has been contributing significantly since its creation.
The miniproteins initially studied by the team were designed starting from human proteins. This part of the CBF project continues with the development of K1K1 Met tyrosine kinase agonist, and promising outcomes in the field of regenerative medicine (CNRS and SATT press releases). Very recently, the team expanded its approach by mining proteins produced by some worms that represent a rich source of miniproteins endowed with potent biological activities. The worms we are studying have evolved for more than 400 million years in diverse habitats or hosts. These extreme adaptations promoted the production of original active molecules that we are discovering and exploring for medical applications.
In parallel, we are strongly involved in the conception and validation of innovative protein production methods and modification tools. This work is strongly connected to the others since it multiplies the possibilities to study the mechanisms of action of our miniproteins through chemical biology approaches, as well as to improve them according to the targeted specifications.
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Crystallographic structure of the K1K1 protein (pdb 7OCL), a mimic of hepatocyte growth factor. This molecule was patented in 2015 and was the subject of a maturation project funded by SATT Nord. An exclusive license agreement was concluded at the end of 2022 with the company Boehringer Ingelheim.
HIGHLIGHTS
This article describes a novel method for effecting the selective desulfurization of cysteine into alanine at the protein level, using an iron-catalyzed process reminiscent of aquatic chemistry.
Selected as a Hot Paper by the journal.
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