BIOL 157 |
| Botulinum neurotoxins (BoNTs) are the most deadly poison known to human being as well as increasingly popular therapeutic agents against some neuromuscular disorders. Both the toxicity and therapeutic effects of BoNTs highly depend on their proteolytic activity, which resides exclusively in their light chain (LC) part. The objective of this study was to investigate the stability of BoNT type A LC (LCA) against proteases. LCA was incubated with proteases at 25oC. Samples were taken every 30 min and subjected to SDS-PAGE and fluorescent spectroscopy. LCA largely retained its proteolytic activity immediately after trypsin was added in spite of significant cleavage by trypsin. Extended exposure of LCA to trypsin resulted in further cleavage and decrease in proteolytic activity. This research is funded by National Institute of Health through New England Regional Centre of Excellence for Biodefense (1-U54AI057159-03) and Department of Defense/US Army (W911NF-06 1-0095). |
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Frontiers in Chemical Biology
5:00 PM-7:00 PM, Wednesday, August 22, 2007 BCEC -- Exhibit Hall - B2, Poster
Division of Biological Chemistry |