• Level of Education

    5 years of post-secondary education

  • ECTS

    2 credits

  • Training Structure

    College of Sciences

Description

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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Objectives

The course is designed to be inclusive and will focus primarily on understanding the molecular basis of the cascades that enable the transition from gene to protein, as well as on manipulating and utilizing these reactions for applications in the life sciences.

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Class Hours

  • Chemobiology (67% ENSCM) - LectureLecture3:00 p.m.
  • Chemobiology (67% ENSCM) - TutorialTutorials5 hours

Mandatory Prerequisites

Organic Chemistry (Master's Level 1)

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Knowledge Assessment

2-hour final written exam

Authorized documents: yes

Non-graphical calculators allowed: yes

Internet access allowed: No

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Course Outline

Class: 15 hours

 

  1. Fundamentals

Topics covered: from gene to protein, sequencing, phenotypes, transcriptomes, post-translational modifications, the immune system, and the function and chemistry of cellular compartments.

 

  1. The Tools of Chemical Biology.

Concepts covered: bioorthogonal reactions, biodegradable linkers, chemical probes, directed self-assembly, self-immolating probes, vectorization, vector viruses, chromophores, biosynthetic libraries, phages, protein expression systems, monoclonal antibodies, stem cells, model organisms for in vivo testing.

 

  1. Manipulating DNA and RNA

Topics covered: DNA-targeting drugs, SELEX, and functional nucleic acids (aptamers, DNAzymes, RNAzymes); DNA-encoded chemistry; DNA-based nanobiotechnology; and the extension of the genetic code beyond 20 amino acids.

  1. Manipulating proteins and peptides

Concepts covered: protein-targeting probes, protein (e.g., enzymes, antibodies) engineering and synthesis (native ligation), mutations. Secondary structure of proteins: domains and folds that confer function; supramolecular assemblies (e.g., zinc fingers, peptide/RNA interactions, self-assembling peptides).

 

TD: 5H

The concepts presented in a lecture-style format will be reinforced through classroom discussions of articles from scholarly journals, which will be presented and discussed by students.

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Additional Information

Teaching Staff :

 

Michael.smietana@umontpellier.fr

gilles.subra @ umontpellier.fr

lubomir.vezenkov @ enscm.fr

 

 

Administrative contact(s):

Master's in Chemistry Office

https://master-chimie.edu.umontpellier.fr/

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