Abstract
Membrane protein engineering has progressed significantly in recent decades, enabling the design and redesign of nanopores for specific applications in Biotechnology. More recently, alpha-helical nanopores have received much interest due to their structural versatility and tunable selectivity. For example, chemically synthesized peptides can be excellent building blocks to construct alpha-helical transmembrane structures. Notably, solid-phase peptide synthesis provides a possibility to construct alpha-helical pores composed of unnatural D-amino acids that provide unique structural and functional properties.
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