Conformational polymorphism of the PrP106-126 peptide in different environments

A molecular dynamics study

Alessandra Villa, Alan E. Mark, Gloria A A Saracino, Ugo Cosentino, Demetrio Pitea, Giorgio Moro, Mario Salmona

Research output: Contribution to journalArticle

31 Citations (Scopus)

Abstract

Extensive molecular dynamic simulations (∼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, β-sheet elements were observed between residues 108-112 and either residues 115-121 or 121-126. An α-β transition was observed under neutral conditions. In DMSO, the peptide adopted an extended conformation, in agreement with nuclear magnetic resonance experiments.

Original languageEnglish
Pages (from-to)1423-1428
Number of pages6
JournalJournal of Physical Chemistry B
Volume110
Issue number3
DOIs
Publication statusPublished - Feb 26 2006

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polymorphism
Polymorphism
Peptides
peptides
Molecular dynamics
molecular dynamics
Dimethyl Sulfoxide
Trifluoroethanol
Circular dichroism spectroscopy
Dimethyl sulfoxide
Water
simulation
Prions
Hexanes
Hexane
water
dichroism
Conformations
Nuclear magnetic resonance
fragments

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry

Cite this

Conformational polymorphism of the PrP106-126 peptide in different environments : A molecular dynamics study. / Villa, Alessandra; Mark, Alan E.; Saracino, Gloria A A; Cosentino, Ugo; Pitea, Demetrio; Moro, Giorgio; Salmona, Mario.

In: Journal of Physical Chemistry B, Vol. 110, No. 3, 26.02.2006, p. 1423-1428.

Research output: Contribution to journalArticle

Villa, Alessandra ; Mark, Alan E. ; Saracino, Gloria A A ; Cosentino, Ugo ; Pitea, Demetrio ; Moro, Giorgio ; Salmona, Mario. / Conformational polymorphism of the PrP106-126 peptide in different environments : A molecular dynamics study. In: Journal of Physical Chemistry B. 2006 ; Vol. 110, No. 3. pp. 1423-1428.
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