(365d) Interaction Forces between Random Coil Proteins

The coiled-coil interaction system represents one of the most studied protein complex due to its important role in numerous biological processes such as gene transcription or intra-cellular trafficking. The unique double helix structure of this complex has inspired the design of de novo peptides exhibiting the ability to spontaneously assemble with a cognate partner specifically. Such peptides are now finding their place in many biotechnological applications such as drug development, tissue engineering, biomedical devices etc.

Besides their promising future in the biomedical field, our fundamental understanding regarding the intimate process of interaction between a coiled coil pair is still limited.

In the present presentation, we will give an overview of some recent fundamental advances in our comprehension of the interaction mechanisms taking place in the coiled system. Using delicate forces measurement techniques such as the surface forces apparatus, we were able to dissect certain key aspect of the double helix formation and rupture. Our results show that the distribution of the association energy along the double helix complex is non uniform with a maximum at its core. Our results also showed that the complex formation can be initiated at any site or heptade along the peptides, ruling out the existence of a preferential triggering domain for the association.

Practical applications of the coiled coils adhesive system, especially in the drug delivery system area will be described as well. We will show that this adhesive system can be used to design affinity based delivery systems for the long term release of nanoparticles transporting active proteins.