Nanopore analysis of tethered peptides (pages 701–708)
Howard Meng, Dielle Detillieux, Christian Baran, Besnik Krasniqi, Christopher Christensen, Claudia Madampage, Radu I. Stefureac and Jeremy S. Lee
Article first published online: 2 SEP 2010 | DOI: 10.1002/psc.1289
Threading the needle. Up to four short peptides were attached to a single benzene ring to produce peptide bundles and their ability to thread through the α-hemolysin pore was assessed. Bundles of one or two strands readily translocated, whereas three- and four-stranded bundles produced many bumping and intercalation events as well as permanent blockages. The results suggest that proteins must completely unfold in order to thread through the pore.