Organic Chemistry - CNRS URA2128  

  HEADDr MULARD Laurence /
  MEMBERSDr BAHRAMI Fariborz / Dr BALEUX Françoise / Dr BAY Sylvie / Dr BEAUD Diane
BOUTET Julien / COIC Yves-Marie / Dr DESCROIX Karine / Dr FREIRE GARD Teresa
Dr GARCIA Alphonse / Dr GASSE Cécile / GODET Angélique / Dr JANIN Yves
Dr JESTIN Jean-Luc / Dr KAMINSKI Alexandre / Dr KIM Tae Hee / LANDIRES Ivan

  Annual Report

The Organic Chemistry Unit contributes to several multidisciplinary programs dealing with the synthesis of new chemical entities and validation of biological targets of therapeutic interest.

Therapeutic chemistry

Within the “GPH tuberculosis” program, we have developed two series of original antimycobacterials which have so far led to two patent applications. The first class of compounds was designed to target nucleotide metabolism by inhibiting nucleoside monophosphate kinases. Interestingly, some inhibitors are also active on Mycobacterium tuberculosis growth in vitro. The second class stemmed from the structure of a compound with an activity specific to the mycobacteria genus in vitro. The ensuing structure/activity relationship studies have led to an improvement of this activity.

Opening the way to innovation in the field of anti-inflammatory drugs and/or anti-tumor agents, we also demonstrated that synthetic peptide fragments of the NEMO protein inhibited the NF-kB route.

Towards new glycoconjugate vaccines

We designed the MAG:Tn3, a synthetic immunogen based on the Tn antigen, as a promising vaccine candidate against breast, lung or prostate cancer. To further extend the scope of our approach to clinical applications, we developed enzymatic syntheses of the tumor-associated mucin MUC6 displaying high densities of the Tn antigen.

Within our anti-infectious subunit vaccine program, we designed a promising candidate against bacillary dysentery. A synthetic oligosaccharide acting as a functional mimic of the major protective antigen of the enterobacterium Shigella flexneri 2a was identified as the key carbohydrate component.

Identification and/or engineering of new enzymes

Characterization of the newly identified rat RCL, a N-deoxyribosyl-transferase, revealed an original enzyme activity, namely a deoxynucleoside-5’-monophosphate N-glycosidase of potent therapeutic interest. The sequence/structure/activity relationship of this new, recently patented, family of nucleoside catabolic enzymes is under study.

Using the chemistry of Inovirus, we have developed in vitro protein engineering methods based on selection protocols that allow the analysis of more than 108 proteins. Thermostable DNA polymerases endowed with reverse transcriptase activity were selected from Thermus aquaticus DNA polymerase I mutants according to catalytic activity.

Phosphatase-derived drug technology (DPT)

Relying on our DPT concept based on the design of penetrating peptides able to specifically disturb PP1/PP2A-directed intracellular pathways, we focused on (i) the role of PP1 in apoptotic pathways mediated by sequences from the Apoptotic Factors, (ii) the role of PP2A1 in apoptotic pathways mediated by peptides from viral HIV-1-Vpr and canine adenovirus E4orf4 proteins.

  Web Site

More informations on our web site


Publications 2006 of the unit on Pasteur's references database

Activity Reports 2006 - Institut Pasteur
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