Date : 27/01/2011

Laboratory
Laboratoire de Physique Statistique de l'ENS UMR CNRS 8550
Ecole Normale Superieure, 24 rue Lhomond 75005 Paris
Director : Mr Eric PEREZ
Main discipline : Biophysics
http://www.lps.ens.fr

PhD Supervisor
Wladimir URBACH
email : Cet e-mail est protégé contre les robots collecteurs de mails, votre navigateur doit accepter le Javascript pour le voir
phone : +33 6 88 58 09 78

Subjects
1.: amyloid peptides
2.: beta-Lactoglobulin
3.: hydration

Tools-Methodologies
1.: ultrasound
2.: density measurments
3.: all atom molecular dynamics

Summary of labs interests

Biomembrane dynamics : adhesion, fusion and protein transport, from the molecular to the cell level, force measuring techniques coupled to optical tools live or biomimetic systems. The techniques we use are micropipet micromanipulation (Biomembrane Force Probe, cell adhesion, vesicle adhesion), Surface Force Apparatus, coupled to optical tools such as FRAPP, TIRF and confocal microscopy. SEE http://www.lps.ens.fr/-Surfaces-moleculaires-organisees-

Summary of the project

The mechanism of protein conversion into amyloid fibrils remains a crucial problem in biology and medicine. In this respect several lines of experimental evidence indicate that a number of proteins unrelated to neurodegenerative deseases, can self-organize into amyloid aggregates, suggesting a property intrinsic to polypeptide chains as short as four residues. Furthermore, functional amyloids can be involved in diverse mechanisms such as storage or infectivity. The fact that this mechanism can be reversed opens the door to interesting disaggregation possibilities. The candidate will focus on the role of hydration in the aggregation and propagation process which seems relatively unexplored, and where hydrophobic amino acid sequences seem to play an important role.

Interdisciplinarity of the project

The candidate will have to - work with proteins and peptides - confront molecular dynamics results with experimental ones, leading to evaluate the volume and the compressibility of a peptide in a given solvent.