Abstract
Design of peptides, using functional properties of natural ion channels, is a goal in development of novel macromolecular devices and therapeutics. A porin-like channel is a self-associated channel in a membrane, composed of short β-sheet peptides. Gramicidin-like channel (GLC) is an ion channel synthesized recently by substitutions of D-alanine for glycines in the sequence of porin-like channel peptide. Existence of D-amino acid residues makes it difficult to determine the exact secondary structure of GLC; however experimental methods such as CD and IR have shown a beta helical dimer for GLC similar to the structure of gramicidin A (GA) ion channel.
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