The early stages of insulin fibrillogenesis explored with mass spectrometry and molecular modelling
- Event time: 1:00pm
- Event date: 5th March 2012
- Speaker: Massimiliano Porrini (Formerly School of Physics & Astronomy, University of Edinburgh)
- Location: Room 2511, James Clerk Maxwell Building (JCMB) James Clerk Maxwell Building Peter Guthrie Tait Road Edinburgh EH9 3FD GB
A prevalent type of protein misfolding causes the formation of β-sheet-rich structures known as amyloid fibrils. Research into the mechanisms of fibril formation has ramifications for both disease prevention and nanoscale templating technologies. This investigation into the aggregation of insulin utilises ion mobility mass spectrometry coupled with molecular modelling to identify and characterise oligomers formed during the 'lag' phase that precedes fibril growth. We show that insulin oligomerises and adopts multiple distinct conformations, the most dominant of which are compact species. Modelling suggests that these are enriched in β-sheet secondary structure and dominated by hydrophobic interactions.
This is a weekly series of informal talks given primarily by members of the soft condensed matter and statistical mechanics groups, but is also open to members of other groups and external visitors. The aim of the series is to promote discussion and learning of various topics at a level suitable to the broad background of the group. Everyone is welcome to attend..