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About Us

We provide Peptides and Proteins for therapeutic, diagnostic and cosmetic applications

GENEPEP is a privately held company that specializes in design, chemical synthesis and optimization of peptides, peptide libraries and proteins.

We are experts in the synthesis, purification and characterization of classical and complex compounds (chemically modified peptides and proteins, cyclic peptides, tagged peptides, toxins).

We assure Quality, Short Delivery Times, Flexibility and Absolute Confidentiality. During the projects timelines we provide meaningful communication on regular basis.

GENEPEP provides products and services for research and drug discovery.

  • Custom Peptide Synthesis
  • Catalog Peptides
  • Custom and Catalog Peptide Libraries
  • Custom and Catalog Proteins
  • Hit Generation and Lead Optimization
  • Platform for Peptide Analyses (impurity identification, solubility and stability studies)


  • More than 20 000 peptides synthesized
  • Over 30 Chemically Synthesized Proteins and analogs
  • Solution and Solid Phase Synthesis
  • Several Scientific Publications and Patents,
  • Strong skills in design and optimization of peptides
  • Highly Qualified Team
  • State-of-the-art equipment
  • Strong problem solving skills


We work on Fee-for-service or FTE based programs.

GENEPEP can be the partner of your R&D projects, from research steps to development milestones.
The company is located in Montpellier, South of France.
GENEPEP has been awarded by French Research Ministry (innovative company) and Aventis (innovative technology).

GENEPEP, specialist in peptide and protein chemistry

Quality, skills, confidentiality, advice, flexibility, customized follow-up are our major assets in order to meet your requirements. Provider or partner for your R&D projects - We work on Fee-for-service or FTE based programs.



  • Valentine’s day by GENEPEP

    Are you targeting the best for your peptides ?

    Fall for GENEPEP assets :

    • An experimented team of peptides chemistry specialists
    • More than 20 000 synthetized peptides in 15 years
    • Programs for peptides synthesis and optimization in cardio, obesity, cancer, vectorization, imagery, diagnostics…

    We offer peptides & proteins synthesis, stability and solubility studies, lead optimization…

  • [Job offer] Chemistry Technician


    GENEPEP is looking for a new team member by early february. The work will prioritize polymer synthesis by polycondensation but will also consist in peptide synthesis.

    You can see below the full offer.


  • GENEPEP stability studies

    Do you observe a decrease in your peptide activity ?

    Try GENEPEP stability services :

    • Peptide stability studies
    • Impurity identification
    • Design of analogs with better stability

    And also : Peptide custom synthesis


  • Karine PUGET

    PhD, CEO

    Karine did her PhD in Peptides area chemistry-Biology interface at Prof. Jean Martinez lab as Ipsen employee (CIFRE). She won several national contests from the french research Minister and Aventis in innovative company projects. She founded GENEPEP in March 2003 and since then she is actively involved in many collaborations with Pharma and Biotech companies.

  • Marie-Christine GIOLLENT

    Marie-Christine has joined GENEPEP in 2007 after a long experience in medical devices field (Hill Rom, Getinge). She is in charge of financial control and reporting, accounts, HR matters, sales, administration, suppliers relationships, quality system control.

  • Mathieu GALIBERT

    PhD, R&D Project Manager

    Mathieu Galibert joined GENEPEP as Project Manager in October of 2016. He is in charge of the R&D programs for the chemical synthesis of proteins. Mathieu has extensive experience in peptide synthesis, chemical ligation and bioconjugation. He holds a PhD in Organic Chemistry from Joseph Fourier University in Pascal Dumy’s team. The main objective of his PhD project was the synthesis and design of peptide vectors for cancer applications. After his studies he was a research associate at The National Center for Scientific Research (CNRS) in Agnès Delmas’ lab at Orleans. He worked on the development of a solid-supported strategy for the synthesis of protein and glycoprotein by chemical ligation. Before joining GENEPEP, his last position was project manager in Smartox Biotechnology.

  • Said JEBORS


    Saïd JEBORS has joined GENEPEP in October 2016 to develop the company’s polymer sector. He has more than 10 years of experience in the field of chemistry. After starting his research activities focused on the supramolecular chemistry, and then in the development of some hybrid peptide materials, he was in charge of the design of bioactive medical devices. He holds a doctorate in organic chemistry from the University Claude Bernard, Lyon 1.

  • Magali JULLIAN

    Production manager

    Magali arrived in GENEPEP in 2006 after finishing her Master Degree in Chemistry at University of Montpellier and since then she acquired all necessary knowledge in Peptide Synthesis. She is now in charge of Custom and Catalog Peptide Synthesis.

  • Maxime LEROUX

    Production technician, HSE manager

    After obtaining his Bachelor Degree in Organic Chemistry at the IUT of Le Mans, Maxime has joined the GENEPEP team in 2014 as a lab technician. First specialized in the production of chemical libraries, he is now in charge of all the peptide production for our clients or intern R&D projects. Maxime is also the Health, Safety and Environment manager in the lab, and actively participates in developing our quality management process.


  • M. Bacchi, B. Fould, M. Jullian, A. Kreiter, A. Maurras, O. Nosjean, T. Coursindel, K. Puget, G. Ferry and J. A. Boutin, Screening ubiquitin specific protease activities using chemically synthesized ubiquitin and ubiquitinated peptides, Anal Biochem, 2017, 519, 57-70.
  • J. Neasta, C. Valmalle, A. C. Coyne, E. Carnazzi, G. Subra, J. C. Galleyrand, D. Gagne, C. M’Kadmi, N. Bernad, G. Berge, S. Cantel, P. Marin, J. Marie, J. L. Baneres, M. L. Kemel, V. Dauge, K. Puget and J. Martinez, The novel nonapeptide acein targets angiotensin converting enzyme in the brain and induces dopamine release, Br J Pharmacol, 2016, 173, 1314-28.
  • M. Bacchi, M. Jullian, S. Sirigu, B. Fould, T. Huet, L. Bruyand, M. Antoine, L. Vuillard, L. Ronga, L. M. Chavas, O. Nosjean, G. Ferry, K. Puget and J. A. Boutin, Total chemical synthesis, refolding, and crystallographic structure of fully active immunophilin calstabin 2 (FKBP12.6), Protein Sci, 2016, 25, 2225-2242.
  • L. Ronga, P. Verdie, P. Sanchez, C. Enjabal, A. Maurras, M. Jullian, K. Puget, J. Martinez and G. Subra, Supported oligomethionine sulfoxide and Ellman’s reagent for cysteine bridges formation, Amino Acids, 2013, 44, 733-42.
  • G. Miralles, P. Verdie, K. Puget, A. Maurras, J. Martinez and G. Subra, Microwave-mediated reduction of disulfide bridges with supported (tris(2-carboxyethyl)phosphine) as resin-bound reducing agent, ACS Comb Sci, 2013, 15, 169-73.
  • C. Echalier, S. Al-Halifa, A. Kreiter, C. Enjalbal, P. Sanchez, L. Ronga, K. Puget, P. Verdie, M. Amblard, J. Martinez and G. Subra, Heating and microwave assisted SPPS of C-terminal acid peptides on trityl resin: the truth behind the yield, Amino Acids, 2013, 45, 1395-403.
  • P. Verdié, L. Ronga, M. Cristau, M. Amblard, S. Cantel, C. Enjalbal, K. Puget, J. Martinez and G. Subra, Disulfide Bond Formation with Polymer-Supported Reagent, Synfacts, 2011, 2011, 1382-1382.
  • P. Verdie, L. Ronga, M. Cristau, M. Amblard, S. Cantel, C. Enjalbal, K. Puget, J. Martinez and G. Subra, Oxyfold: a simple and efficient solid-supported reagent for disulfide bond formation, Chem Asian J, 2011, 6, 2382-9.
  • E. Ambrosino, C. Dumoulin, E. Orlandi-Pradines, F. Remoue, A. Toure-Balde, A. Tall, J. B. Sarr, A. Poinsignon, C. Sokhna, K. Puget, J. F. Trape, A. Pascual, P. Druilhe, T. Fusai and C. Rogier, A multiplex assay for the simultaneous detection of antibodies against 15 Plasmodium falciparum and Anopheles gambiae saliva antigens, Malar J, 2010, 9, 317.
  • M. Jullian, A. Hernandez, A. Maurras, K. Puget, M. Amblard, J. Martinez and G. Subra, N-terminus FITC labeling of peptides on solid support: the truth behind the spacer, Tetrahedron Letters, 2009, 50, 260-263.
  • J. Colette, E. Ave, B. Grenier-Boley, A. S. Coquel, K. Lesellier and K. Puget, Bioinformatics-based discovery and identification of new biologically active peptides for GPCR deorphanization, J Pept Sci, 2007, 13, 568-74.



  • All you need to know about peptides and proteins

    You will find here our advices for optimal storage conditions and solubilization of delivered peptides. Please contact us for further information you might require.

  • We recommend to store the peptides in lyophilized form at -20°C. At this temperature, most of peptides remains stable during several years.

    In order to reduce peptide exposure to humidity, peptides should be aliquoted.

    After removing from the fridge or the freezer, let the peptides warm up to room temperature before opening a vial to avoid water condensation.


    Before solubilizing peptides it is important to evaluate the net charge of your peptide. The simple rules stated below are used to determine if the peptide is basic, acidic or neutral.

    • Assign a value of -1 to each acidic residue (D, E, and C-terminal COOH).
    • Assign a value of +1 to each basic residue (K, R and the N-terminal NH2).
    • Assign a value of +1 to each H residue at pH<6 and zero at pH >6.

    Count the total number of charges of the peptide at pH 7 (all D, E, K, R, C-terminal COOH, and N-terminal NH2). Calculate the overall net charge of the peptide. Some peptides can cause some solubilization problems. Firstly, start with deionized water. If peptide remains insoluble, different additives can be added to water in accordance with the type of peptide and/or your assay :

    • Basic peptides (overall positive net charge): add acetic acid (up to maximum 20-30% for difficult peptides) or TFA (up to 1%)
    • Acidic peptides (overall negative net charge): add ammonia (ammonium hydroxide) (up to 5%)
    • Very hydrophobic or neutral peptides: add acetonitrile (up to 10-20%), isopropanol, DMSO or DMF.

    In all cases, sonication is recommended. When your peptide is fully solubilized, add solvent/buffer in order to reach concentration required.


    Cysteine (C), Methionine (M) or Tryptophan (W) :

    Peptides containing these amino acids are extremely sensitive to oxidation (risk of dimerization, cyclization) and should be solubilized with water or deoxygenated buffer (can be obtained by vacuum filtration or bubbling with helium, argon or nitrogen). Do not use basic solutions or DMSO in any case.

    Glutamine (Q) :

    Peptides containng a glutamic acid in N-terminal can form a pyroglutamate cycle in acidic solution. Solvents like acetonitrile or DMSO should be diluted to a concentration compatible with biological tests (ex cell culture…)

    The net peptide content (NPC) is the real peptidic material fraction of the sample (i.e. the requested peptide and the peptidic impurities), the rest is salt & water. Depending on the aminoacids present in the sequence, the salt quantity is different. All basic residues have counter-ions coming from corresponding acid (TFA, AcOH or HCl). The nitrogen content determined by Elemental Analysis comes only from the peptidic material and therefore is used for quantification of peptide content in the sample. Ex : 10 mg of a peptide 95% purity, NPC=80%, contains 8 mg of the peptide at 95% purity. To have 10 mg of NPC, don’t forget to specify that you want NPC quantity.

    For long-term storage the peptide should be kept in solid form in the freezer at  -15 °C. For short-time storage a refrigerator (+4 °C) will suffice. After removing from the fridge or the freezer, let the peptides warm up to room temperature before opening to avoid water condensation. Peptides should be protected from intense sunlight. Peptides containing fluorophores should be kept in the dark. Depending on the storage condition and the aminoacids contained in the sequence, the shelf stability of peptide may range from few weeks to years.