Guidance 2

The purpose of this course is to highlight biological processes at the cellular level or even in living organisms. Various molecular imaging approaches will be covered (fluorescent probes, radiolabeling).

Hourly Volumes*:

            CM: 9:00 a.m.

           Land: 11 H

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The principles of green chemistry provide a foundation for the evaluation and design of new chemical products and processes that minimize negative impacts on human health and the environment. In this course, offered to M2 students in the Master’s program in Biomolecular Chemistry (BM), Track 2 (O2), we will cover the basic principles and concepts of green chemistry, as well as their applications in the field of unconventional activation methods and the use of alternative solvents in organic synthesis.

Hourly Volumes*:

CM: 9:00 a.m.

Field: 11 h

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This course unit will cover techniques for the extraction of biomolecules (protein precipitation, SPE), as well as techniques for the separation of biomolecules (chromatography, electrophoresis).

Hourly volumes*:

            CM: 9 a.m.

            Field: 11 h

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Peptides and proteins consist of chains of amino acid residues that confer specific properties upon them. Their functionality depends on their sequence—and thus on the chemical functions they possess—and is also greatly influenced by their structure. In addition to conventional peptide synthesis, advanced options for functional modification, structural changes, and property adjustments—which can significantly alter or enhance the properties of the resulting peptide—will be explored. Significant biotechnological developments in both the chemical and biological fields will be discussed, leading to a wide range of applications in which peptides and proteins are successfully utilized.

Hourly Volumes*:

CM: 15

TD: 5

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In chemistry, solid-phase synthesis is a method in which molecules are covalently bonded to a solid support and synthesized step by step using selective protective groups. The purpose of this applied course is to provide a comprehensive understanding of this field and to examine supported strategies for the practical preparation of polypeptides and oligonucleotides.

Hourly Volumes*:

CM: 9:00 a.m. 

Land: 11 H

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Discusses the structure and function of nucleic acids. Reviews methods used to synthesize DNA- and RNA-based oligonucleotides, as well as chemical reactions that lead to modifications of nucleic acids for therapeutic and diagnostic applications. Additional topics include: nucleic acid molecular beacons, antisense and siRNA oligonucleotides, and DNA arrays.

Hourly Volumes*:

            CM: 3:00 p.m.  

            TD: 5 hours

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This course covers the various molecular and supramolecular tools used for the vectorization and delivery of active ingredients based on the type of cells or intracellular organelles being targeted. Ligand-receptor interactions will be discussed, as will methods for preparing and activating conjugates. Examples of drugs will be presented.

Hourly Volumes*:

CM: 3:00 p.m.

TD: 5 H

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The course will focus on organic chemistry and the post-functionalization of biomolecules—specifically peptides, proteins, and nucleic acids (DNA and RNA)—with applications in gene therapy, biosensing, and the design of probes for biological studies.

Hourly Volumes*:

CM: 3:00 p.m. 

TD: 5 hours

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 In-depth study of ^1H, ^13C, ^19F, ^29Si, and ^31PNMR, as well as two-dimensional methods. The basics of EPR will also be covered (principles and applications).

Hourly Volumes*:

CM: 3:00 p.m.

TD: 5 H

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This course aims to describe the synthetic tools applied to complex and polyfunctional molecules. Retrosynthetic and stereocontrolled approaches will be covered, as well as the judicious use of protective groups.

Hourly Volumes*:

CM: 9:00 a.m.

Land: 11 H

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Bioconjugation reactions are of major interest in the biomedical sciences and enable chemists to modify biomolecules to impart new functions or properties to them. This course will cover strategies for bioconjugation and the labeling of biomolecules, which allow for the exploration of complex biological systems. The lab sessions will illustrate these concepts through examples of bioconjugation using osidic and nucleotide platforms.

Hourly Volumes*:

CM: 9:00 a.m. 

Land: 11 H

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Knowledge of the latest mass spectrometry techniques for the detection, identification, and structural characterization of organic molecules and biomolecules.

Applications in chemistry (pharmaceutical industry) and biology (omics approaches).

1) Structural elucidation (Ion characterization technologies):

• LC/MS/MS and exact mass measurements 
• Isotope Labeling, H/D Exchange
• Ionic Mobility

2) Surface analysis and imaging (molecular mapping)

3) Applications in chemistry and biology: characterization of small organic molecules and biomolecules.

Hourly Volumes*:

CM: 3:00 p.m.

TD: 5 hours

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The following topics will be covered:

- Triglycerides

- Phospholipids and sphingolipids

- Glycolipids

- Fat-soluble vitamins

- Steroid hormones

- Bile salts

- Structure and Synthesis of Prostaglandins and Leukotrienes

Hourly Volumes*:

CM: 15

TD: 5

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The following topics will be covered:

- General Mechanism of Glycosylation

- Synthesis of glycosyl donors

- Methods for Activating Glycosyl Donors

- Stereoselective synthesis of several natural oligosaccharides

Hourly Volumes*:

CM: 15

TD: 5

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A 5- to 6-month internship must be completed in a research or research and development laboratory specializing in organic chemistry, biomolecular chemistry, biochemistry, analytical instrumentation, or analytical testing and development. Students will thus have the opportunity to complete this end-of-program internship in academic or private research laboratories. Subject to prior approval by the faculty (the internship topic must be related to the master’s program curriculum, and the environment and resources must be adequate), students may seek a host team in an academic setting at the institutes of the Chemistry Cluster at the University of Montpellier (IBMM, ICGM, IEM…), in academic laboratories outside the University of Montpellier (in France or abroad), or in the private sector (chemical, pharmaceutical, agri-food, and cosmetics industries; biotechnology laboratories; etc.), as well as in research facilities such as proteomics, metabolomics, and fluxomics platforms.

The research project assigned to students must be related to the skills and expertise they have acquired during previous semesters and in the courses they have taken, particularly in Semester 9, depending on their chosen track.

This 5- to 6-month internship may begin in mid-January after the exam period and may not exceed 6 months, with one semester included during the period of valid university enrollment. The faculty of the Master’s program in Biomolecular Chemistry will advise students on finding an internship that matches their aspirations and abilities.

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Scientific Information: This course aims to familiarize students with scientific research and information management. As part of this, recent bibliographic search tools will be explained and used during lectures and tutorials (Electronic resources: SciFinder / ISIS / Beilstein). Training on the features of Zotero and the use of the electronic lab notebook will also be provided. The writing and analysis of scientific publications will be covered.

Bibliographic Project: Tools for researching scientific information will be applied to a real-world scenario. The teaching team will assign each student a bibliographic topic related to the specialization they have chosen. If necessary, this bibliographic topic may be defined in consultation with the host organization where the internship will take place.

For this personal project, the student will have access to all the bibliographic resources available at the university or the host company. The bibliographic research may be combined with the English course to prepare for an oral presentation similar to one given at an international conference.

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