In 2009, EFMC launched a series of short courses aimed to favour cultural and scientific growth of the medicinal chemistry community and organised with affordable fees for participation.
This intensive course is intended for scientists working in the field, and the presentations will be given by senior scientists from industry and academia. The number of participants will be limited to 35, to favour in depth discussion. Should the number of applications exceed the maximum, preference will be given to applicants from EFMC adhering countries and employees of EFMC corporate members. Upon special request to the organizers (only based on financial conditions and supported by an argued recommendation of the head of the department of the applicant) a limited number (maximum 3) applicants from academia may be admitted at a reduced fee.
The interactions between molecules govern all of the properties that determine whether a compound will be an effective drug or not. This course will present the fundamental considerations determining the thermodynamic and kinetic properties of interactions between molecules.
The first part of the course will begin with an introduction to the types of interactions that are usually considered important for drug-like compounds, including some of the less commonly considered weaker interaction types. The decomposition of these interactions into their thermodynamic components will follow. A description of the experimental and computational methods available to study intermolecular interactions and their strengths and weaknesses will follow.
The second part of the course will focus on applied aspects. This will take two forms: detailed presentations considering most key molecular properties and some hands on tutorial exercises. Both will be structured around real life case studies taken from the literature and the presenters’ own experience. The areas of application will be directly relevant to the properties of a molecule typically modulated by medicinal chemists. Interactions in the solid state and their similarities and differences with interactions in solution determine the solubility of a molecule. The interactions with a range of solvent types determine many partitioning effects. The interactions between small molecules and proteins and between different protein molecules determine the affinity of compounds for their target and antitargets as well as their ability to compete with other compounds present in biological environments. The considerations governing the kinetics of association and dissociation have come into focus in recent years; they provide confounding influences that can lead to surprising in vivo effects and more importantly to better therapeutic index.
The various presentations and tutorials will be taken by experts in the field who will present a broad historical perspective as well as cutting edge research from both academia and industrial settings. The course will take an informal approach and ought to prompt plenty of discussion among participants.
George Keseru, Hungarian Academy of Sciences, Budapest, Hungary
Andrew Leach, John Moores University, Liverpool, United Kingdom
Henk Timmerman, VU University Amsterdam, Amsterdam, The Netherlands