The Internal Structure of Helical Pores Self-Assembled from Dendritic Dipeptides is Stereochemically Programmed and Allosterically Regulated

摘要

Pore-forming proteins,peptides,and their remodeled structures perform diverse biological and biologically inspired functions.These include the formation of viral helical coats and transmembrane channels,mediation of protein folding,reversible encapsulation,stochastic sensing,as well as pathogenic and antibacterial activity.Synthetic strategies to obtain porous or tubular supramolecular assemblies have been elaborated.However,only several synthetic supramolecular pore structures are stable in solution and in solid state.