Messaging Across Membranes Through Synthetic Alpha Helical Pore Assemblies

Engineered membrane protein pores have demonstrated applications in biotechnology and synthetic biology. For example, engineering to conduct selectively specific ions or small molecules could lead new biosensors. However, the formation of large transmembrane peptide has not been shown previously as target peptides form a complex reaction mixture environment. Here, we assembled pore from 40 amino acid α-helical based on bacterium, Corynebacterium jeikeium. By chemical biophysical techniques, defined structural composition elucidated its assembly mechanism membrane. The is ion-selective, functional capable conducting binding blockers. Furthermore, investigated translocation differently charged cationic through this quantified peptide-binding kinetics at single-molecule resolution. significance work that no one stable steady large-conductance state tunable ion selectivity. Often when these experiments are tried, many conformational states formed, making it difficult engineer such systems for specificity distinct functions. highly original system great interest, due unique architecture, pores, their potential nanobiotechnology. Additionally, our findings shed light action antimicrobial bacterial membranes.