Research groups

Research

Membrane insertion of proteins and antibiotic peptides

Crystal structure of membrane inserting peptides

The insertion of polypeptides into membranes underlies many biological processes, including the assembly of membrane proteins, and the action of natural polypeptide toxins and some peptide antibiotics. Depending on specific circumstances, adoption of hydrophobic or amphipathic helical structure on binding to the membrane surface may be followed by membrane insertion, resulting in transmembrane helical intermediates in a membrane protein folding pathway, the formation of stable or transient membrane ion channels or, in the case of some polypeptide toxins and antibiotics, the generation of a lytic pore. We are using molecular biological and spectroscopic methods to characterize these processes in native, cell-free and model systems.

Group

Alan Dodd.

Recent publications

Dempsey CE, Mason PE. (2006) Insight into indole interactions from alkali metal chloride effects on a tryptophan zipper beta-hairpin peptide. J Am Chem Soc. 128, 2762-2763.

Dempsey CE, Dive C, Fletcher DJ, Barnes FA, Lobo A, Bingle CD, Whyte MK, Renshaw SA. (2005) Expression of pro-apoptotic Bfk isoforms reduces during malignant transformation in the human gastrointestinal tract. FEBS Lett. 579, 3646-3650.

Dempsey CE, Piggot TJ, Mason PE. (2005) Dissecting contributions to the denaturant sensitivities of proteins. Biochemistry 44, 775-781.

Dempsey CE, Ueno S, and Avison MB. (2005) Enhanced membrane permeabilization and antibacterial activity of a disulphide-dimerised magainin analogue. Biochemistry 42, 402-409.