Peptide ion channels: Design and creation of function

✍ Scribed by Shiroh Futaki

• Publisher: Wiley (John Wiley & Sons)
• Year: 1998
• Tongue: English
• Weight: 140 KB
• Volume: 47
• Category: Article
• ISSN: 0006-3525
• DOI: 10.1002/(sici)1097-0282(1998)47:1<75::aid-bip8>3.0.co;2-u

✦ Synopsis

To create ion channel function by synthetic peptides is a challenge in the de novo design of artificial membrane proteins. Amphiphilic a-helical motifs of Ç 20 amino acid residues to span lipid bilayers are most often used for the creation of peptide ion channels. Template molecules to tether helical peptides have been employed to obtain more organized pore structures. Approaches to form molecular assembly of peptides in the membranes by hydrogen bonding have been also investigated. We have developed approaches to assemble helices with individual amino acid sequences to construct artificial helical proteins. Using one of these approaches, four helices corresponding to the voltage sensor segments (S4 in repeat I-IV) of the sodium channel were assembled on a peptide template to give a protein having ion channel activity with rectification.