Woolfson group paper featured on the cover of Nature Chemistry
24 April 2017
Congratulations to Dek Woolfson's Group for their research entitled "A monodisperse transmembrane α-helical peptide barrel" which was featured on the cover of Nature Chemistry
Cell membranes are a crucial component of biological systems and they fulfil a variety of essential roles, including the compartmentalization of chemical reactions as well as enabling the formation of concentration gradients. Molecules and ions, acting as chemical signals, must be transported across cell membranes to mediate a range of cellular functions.
The paper reports the formation of a transmembrane pore through the self-assembly of 35 amino acid α-helical peptides. The design of the peptides is based on the C-terminal D4 domain of the Escherichia coli polysaccharide transporter Wza. By using single-channel current recording, they define discrete assembly intermediates and show that the pore is most probably a helix barrel that contains eight D4 peptides arranged in parallel. They also show that the peptide pore is functional and capable of conducting ions and binding blockers. Such α-helix barrels engineered from peptides could find applications in nanopore technologies such as single-molecule sensing and nucleic-acid sequencing.
The cover image shows a synthetic transmembrane pore — formed by the self-assembly of a-helical peptides — developed by a team led by Hagan Bayley and Dek Woolfson