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Liverpool  
Aggregates of the Prion Peptide, PrP109-122, imaged on mica using Atomic Force Microscopy

Ultimate Goal:

To understand the molecular level structure of peptides associated with diseases.
Techniques Employed: Isotope edited infrared spectroscopy
Atomic Force Microscopy
Solid phase peptide synthesis
Peptides Studied: Residues 109-122 of the Prion peptide, associated with BSE.
Residues 16-22 of the Amyloid Beta peptide, associated with Alzheimer's disease.
Main Findings: Both peptides form b-sheet aggregates, which are shown to have a very specific alignment, which affects the stability and type of aggregates formed.
The kinetics of the alignment process are highly dependent on concentration, providing insites into the alignment mechanism.
Advisor: Prof. Sean Decatur
Last Updated: 07-Jun-2007