2007 NSTI Nanotechnology Conference and Trade Show - Nanotech 2007 - 10th Annual

Transport of _-helical peptides through _-hemolysin and aerolysin pores

R. Stefureac, Y. Long, H-B. Kraatz, P. Howard and J.S. Lee
University of Saskatchewan, CA

alpha-helical peptides, nanopore, alpha-hemolysin, aerolysin, current blockade

A series of negatively-charged -helical peptides of the general formula Fmoc-DxAyKz were synthesized where x and z were 1, 2 or 3 and y was 10, 14, 18 or 22. The translocation of the peptides through single pores, which were self-assembled into lipid membranes, was analyzed by measuring the current blockade and duration. The pores were either -hemolysin or aerolysin, a novel pore from the bacterium Aeromonas hydrophyla. Many thousands of events were measured for each peptide with each pore and they could be assigned to two types; bumping events (type I) and translocation events (type II). For type II events the current blockade and duration increase with the length of the peptides on both pores tested. The dipole moment and the net charge of each peptide have a major effect on the transport characteristics. The ratio of type II/type I events increases as the dipole moment increases and uncharged peptides gave mostly type I events. This type of analysis may prove useful for the study of the conformational changes in proteins present in amyloidogenic diseases and find important diagnostic applications.

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