Dynamics, Intermolecular Interactions, and Organization of Transmembrane β-Peptides

Abstract

Cellular membranes contain a vast variety of proteins, which are practically required for every vital mechanism, such as selective transportation of ions and organic molecules, cell-cell recognition and signal transduction. [1] Nowadays, the major concern in life science is to gather an overview about the thermodynamics and kinetics that govern the native folding and aggregational behavior of these proteins. Artificially folded polymers, or foldamers, have attracted the interest of many research groups since they showed the potential for considerable versatilityin biological functions akin to natural proteins. [2] Thus, the prudent preorganization and refinement of such molecules can shed light on the molecular forces that control the structural features of membrane proteins and thereby, explore the correlation between their conformational stability and biological activity.In particular, β-peptides have recently been used as very promising peptide mimics with interesting conformational and functional propensities. These non-biological polymers are stable towards enzymatic degradation and they can fold into compact multihelical structures including the 14-and the 12-helix. [3] Generally, introducing non-covalent interactions, such as hydrogen bonds and Vander Waals forces via interhelical side chains can enhance the threedimensional stability of proteins. In this regard, β-peptides have been largely utilized as suitable folding patterns to provide information about self-assembly processes.