Order from the disorder
ZOOM link:https://us02web.zoom.us/j/89236785442
Order from the disorder
Roy Beck
Tel Aviv University, Tel Aviv, Israel
The concept that a given amino-acid sequence will not form a 3D folded structure but still have biological functionality has developed only in the last ~15 years. The discovery rate and characterization of intrinsically disordered proteins have been increasing continually, becoming one of the fastest-growing areas of proteomics. It is now estimated that over 50% of eukaryotic proteins contain large intrinsically disordered regions involved in a wide range of cellular functions, including transcription, translation, signaling, and regulation of protein assembly. Structural flexibility and plasticity originating from the lack of an ordered structures suggest a significant functional advantage for these proteins, enabling them to interact with a broad range of binding partners.
In this colloquium, I will review the recent trends where statistical mechanics ideas transform our understanding of molecular biology. I will also present new peptide amphiphiles composed of an intrinsically disordered peptide conjugated to variants of hydrophobic domains. These molecules, termed intrinsically disordered peptide amphiphiles, exhibit a sharp pH-induced micellar phase transition from low-dispersity spheres to extremely elongated worm-like micelles. I will present various experimental characterizations of the transition and propose a theoretical model to describe the pH response, routed on the weak interactions between disordered proteins. I will also show the potential of the shape transition to serve as a mechanism for the design of a cargo hold-and-release application. Such amphiphilic systems demonstrate the power of tailoring the interactions between disordered peptides for various stimuli-responsive biomedical applications.
Last Updated Date : 29/12/2021
