Conformational polymorphism of the PrP106-126 peptide in different environments: A molecular dynamics study

Villa, A., Mark, A. E., Saracino, G. A. A., Cosentino, U., Pitea, D., Moro, G and Salmona, M. (2006) Conformational polymorphism of the PrP106-126 peptide in different environments: A molecular dynamics study. Journal of Physical Chemistry B, 110 3: 1423-1428. doi:10.1021/jp052722o


Author Villa, A.
Mark, A. E.
Saracino, G. A. A.
Cosentino, U.
Pitea, D.
Moro, G
Salmona, M.
Title Conformational polymorphism of the PrP106-126 peptide in different environments: A molecular dynamics study
Journal name Journal of Physical Chemistry B   Check publisher's open access policy
ISSN 1520-6106
Publication date 2006-01-01
Sub-type Article (original research)
DOI 10.1021/jp052722o
Volume 110
Issue 3
Start page 1423
End page 1428
Total pages 6
Place of publication Washington
Publisher American Chemical Society
Language eng
Abstract Extensive molecular dynamic simulations (similar to 240 ns) have been used to investigate the conformational behavior of PrP106-126 prion peptide in four different environments (water, dimethyl sulfoxide, hexane, and trifluoroethanol) and under both neutral and acidic conditions. The conformational polymorphism of PrP106-126 in solution observed in the simulations supports the role of this fragment in the structural transition of the native to the abnormal form of prion protein in response to changes in the local environmental conditions. The peptide in solution is primarily unstructured. The simulations show an increased presence of helical structure in an apolar solvent, in agreement with the results from circular dichroism spectroscopy. In water solution, beta-sheet elements were observed between residues 108-112 and either residues 115-121 or 121-126. An alpha-beta transition was observed under neutral conditions. In DMSO, the peptide adopted an extended conformation, in agreement with nuclear magnetic resonance experiments.
Keyword Chemistry, Physical
Prion Protein-fragment
Secondary Structure
Circular-dichroism
Scrapie Prion
Simulations
Transition
Residues
Neurotoxicity
Mechanism
Features
Q-Index Code C1

Document type: Journal Article
Sub-type: Article (original research)
Collections: Excellence in Research Australia (ERA) - Collection
School of Chemistry and Molecular Biosciences
 
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Created: Thu, 20 Sep 2007, 04:38:35 EST