Messaging Across Membranes Through Synthetic Alpha Helical Pore Assemblies

Abstract

Engineered membrane protein pores have demonstrated applications in biotechnology and synthetic biology. For example, engineering pores to conduct selectively specific ions or small molecules could lead to new biosensors. However, the formation of the large synthetic transmembrane peptide pores has not been shown previously as the target peptides form a complex reaction mixture in the membrane environment. Here, we assembled a transmembrane peptide pore from 40 amino acid α-helical synthetic peptides based on the membrane protein of the bacterium, Corynebacterium jeikeium.