How the Physical Sciences can Enhance Life Science Research
2 pm-5.30pm, February 15 2012, Lindisfarne Centre
Programme:
14.00 Welcome
14.10 Timothy Cross (Florida State University): Part of the British Biophysical Society 2012 Lecture
Tour: The native conformation of the influenza A M2 proton channel: A proven but recently
mutated drug target
14:50 Martin Warren (Kent): Title to be confirmed
15.30 Poster session and refreshments
16.10 Rachel McKendry (UCL): Superbugs and superdrugs: microbiology meets nanotechnology
16:50 Frank Gunn-Moore (St Andrews): Lighting the way for biologists
17:30 Closing remarks
Deadline for submission of abstracts for posters: Friday 3rd January 2012
Poster abstracts should be submitted to admin.bsi@durham.ac.uk
More information about the event can be found on the event pages at:
www.dur.ac.uk/bsi/.
Abstracts:
The native conformation of the influenza A M2 proton channel: a proven but recently mutated drug target.
Professor Timothy A. Cross, National High Magnetic Field Lab, Department of Chemistry and Biochemistry and Institute of Molecular Biophysics, Florida State University.
Abstract: Anfinsen’s thermodynamic hypothesis states “that the native conformation (of a protein) is determined by the totality of inter-atomic interactions and hence by the amino acid sequence in a given environment.” As in most Biochemistry textbooks, too often these last four words are ignored. For membrane proteins the complex and heterogeneous membrane environment can have a profound impact on protein structure and dynamics as well as
on our understanding of protein function. I will discuss a new structure of the M2 proton channel from Influenza A virus obtained from liquid crystalline lipid bilayer preparations. With solid state NMR we have characterized the
conductance domain (residues 22-62) that has very similar electrophysiology to that of the full length protein. In addition we have considerable data of the full length protein that in addition to the conductance domain binds the
M1 protein and plays a critical role in viral budding. Additional structures of M2 constructs have been achieved by X-ray crystallography as well as solution NMR, both with and without the antiviral drug, amantadine. Recently, resistance to the antiviral drugs amantadine and rimantadine has dominated the flu seasons and the recent swine flu pandemic. The implications for characterizing a-helical membrane protein structures in various membrane mimetic environments will be discussed along with the elucidated proton conductance mechanism.
Lighting the way for biologists.
Professor Frank Gunn-Moore, Professor of Molecular Neurobiology, St Andrews University.
Abstract: The plasma membrane of a eukaryotic cell is impermeable to most hydrophilic substances, yet the insertion of these materials into cells is an extremely important and universal requirement for the cell biologist. To address
this need, many transfection techniques have been developed including viral, lipoplex, polyplex, capillary microinjection, gene gun and electroporation. The current discussion explores a procedure called optical injection
or photoporation, where a laser field transiently increases the membrane permeability to allow species to be internalized. If the internalized substance is a nucleic acid, such as DNA, RNA or small interfering RNA (siRNA), then
the process is called optical transfection. This contactless, aseptic, cell transfection method provides a key nanosurgical tool to the microscopist—the intracellular delivery of reagents and single nanoscopic objects. The
experimental possibilities enabled by this technology are only beginning to be realized. In this presentation will be discussed our new and novel optical transfection technology which is being developed for the end-user in mind.