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Research in the Sanderson group focuses on the interactions of proteins and peptides with membranes.

Research Areas:

Recent Publications:

"Lytic Reactions of Drugs with Lipid Membranes", Hannah M. Britt, Clara A. García-Herrero, Paul W. Denny, Jackie A. Mosely and John M. Sanderson, Chem. Sci., 2018, in press.

"The Influence of Cholesterol on Melittin Lipidation in Neutral Membranes", Hannah M. Britt, Jackie A. Mosely and John M. Sanderson, Phys. Chem. Chem. Phys., 2018, in press.

"The Association of Defensin HNP-2 with Negatively Charged Membranes: A Combined Fluorescence and Linear Dichroism Study", Catherine J. Pridmore, Alison Rodger and John M. Sanderson, Biochim. Biophys. Acta - Biomembr., 2016, 1858, 892–903.

Society Membership:

Member of the British Biophysical Society (committee member), Biophysical Society and the Royal Society of Chemistry (FRSC).

News

Chemical Science Article

Image similar to the Chem. Sci. back cover Recent work by Hannah Britt has demonstrated that acyl transfer can occur from membrane lipids to the drug propranolol. This transfer occurs in model liposome systems in vitro and in vivo in Hep G2 cells. In the latter case, incubation of cells with 30 µM propranolol followed by LC-MS analysis led to the identification of 14 different lipidated propranolol species. Other membrane-active drugs did not generate detectable levels of lipidated products, but those that promoted lipid hydrolysis in vitro had lower EC50 values for phospholipidosis. To read the article, click here.

Peptide Lipidation

Lipidated Magainin II Recent work has established that a chemical process, first seen following the addition of the peptide melittin to lipid membranes, is widely applicable to other membrane binding peptides. The process involves acyl transfer from the lipid to the peptide and occurs in the absence of enzyme catalysis. The process leads the development of chemical complexity in peptide-lipid systems. For example, a mixture of melittin with a binary lipid mixture will evolve from a mixture of three components (peptide + two lipids) into a mixture with up to twenty potential lipidated melittin products and eight different lyso lipids. The lipidation process may also help to account for a number of proteins that are found with unusual lipidation patterns in vivo. To learn more, click here.

The Lab

The Sanderson group is located in the Department of Chemistry and the Biophysical Sciences Institute (BSI) at Durham University. To read more about the BSI, click here.

The Sanderson Lab

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