OFFER DEADLINE01/09/2018 13:30 - Europe/Brussels
EU RESEARCH FRAMEWORK PROGRAMMEH2020 / Marie Skłodowska-Curie Actions
ORGANISATION/COMPANYInternational Project Office
DEPARTMENTPromotion & Advisory Unit
Professor Irene Luque-Fernández, from the Department of Physical Chemistry at the University of Granada, welcomes postdoctoral candidates interested in applying for a Marie Skłodowska-Curie Individual Fellowships (MSCA-IF) in this university. Applicants must comply with the Mobility Rule (more information in the participant guide: http://sl.ugr.es/097k).
The host group is the Biophysics and Biotechnology group in the Department of Physical Chemistry at the Faculty of Sciences of the University of Granada. This group has vast experience in Molecular Biology and Biophysics. The team leaded by Prof. Luque is formed by experts in biophysical techniques such as calorimetry (DSC, ITC), spectroscopy (fluorescence, circular dichroism, FT-IR, NMR), protein engineering (cloning and mutagenesis), stopped-flow techniques, protein expression and purification, and structure determination techniques. The team members have an extensive experience in the application of these techniques to the analysis of folding, structure and interactions of modular domains, protein fragments and small globular proteins. The group pioneered the use of differential scanning calorimetry to analyse the thermodynamics of protein stability and denaturation. It is also a well-known and recognised group with a deep expertise in isothermal titration calorimetry. Furthermore, the group is now shifting towards high-throughput screening methods, including phage display, thermofluor and alpha-screening. Research is conducted in a laboratory perfectly equipped with all necessary instrumentation and infrastructure for protein engineering, expression and purification, and all the biophysical techniques. In addition, a settled collaboration with the research institute Medina, also placed in Granada, provides the required instrumentation for the high-throughput techniques thermofluor and alpha-screening.
Viral diseases are a leading cause of death, resulting in enormous social and economic costs worldwide. No effective vaccines or treatments are available against most known viruses, including encapsulated RNA viruses, such as Ebola or Marburg, causing deadly hemorrhagic fevers. The need for effective tools for rapid intervention against these and other emerging diseases is patent. Our long-term goal is to set the basis for the development of broad-spectrum antivirals targeting budding mechanisms common to many viruses. studying the interactions betweeen viral Late domains and their cellular targets, Nedd4-WW3, Tsg101-UEV and Alix-V, exploring the druggability of their binding interfaces, probing the achievable level of binding affinity and selectivity, and evaluating the toxicity and impact on the normal cellular functioning of budding inhibitors. A multidisciplinary platform, including biochemical, biophysical, proteomic and computational techniques, will be used to: a) Perform detailed biophysical studies of Late domain interactions to provide a strong foundation for the experimental and computational search for effective inhibitors; b) Identify high affinity peptide ligands for Tsg101-UEV and Alix-V domains using phage display techniques, to assess the molecular determinants of high binding affinity; c) Explore the druggability of the Late domain binding interfaces in Nedd4-WW3, Tsg101-UEV and Alix-V, searching for non peptidic inhibitors with high affinity and good specificity profiles by the High Throughput Screening (HTS) of libraries of pure compounds and microbial extracts; d) Evaluate to which extent specificity can be achieved for these domains in a proteome-wide context, assessing binding specificity against all WW and UEV domains in the human proteome.
- Chemistry (CHE)
- Life Sciences (LIF)
For a correct evaluation of your candidature, please send the documents below to Professor (firstname.lastname@example.org):
- Letter of recommendation (optional)