Correlation between symmetry breaker position and the preferences of conformationally constrained homopeptides: a molecular dynamics investigation (Articolo in rivista)

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Label
  • Correlation between symmetry breaker position and the preferences of conformationally constrained homopeptides: a molecular dynamics investigation (Articolo in rivista) (literal)
Anno
  • 2008-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1002/bip.21031 (literal)
Alternative label
  • Torras J., Zanuy D., Crisma M., Toniolo C., Betran O., Alemán C. (2008)
    Correlation between symmetry breaker position and the preferences of conformationally constrained homopeptides: a molecular dynamics investigation
    in Biopolymers (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Torras J., Zanuy D., Crisma M., Toniolo C., Betran O., Alemán C. (literal)
Pagina inizio
  • 695 (literal)
Pagina fine
  • 706 (literal)
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  • Citazioni WOS: 9 Impact Factor 2008: 2.823 Coautore (literal)
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  • 90 (literal)
Rivista
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Departament d'Enginyeria Quimica, EUETII, Universitat Poliytecnica de Catalunya, Igualada 08700, Spain; Departament d'Enginyeria Quimica, E.T.S. d'Enginyers Industrials de Barcelona, Universitat Poliytecnica de Catalunya, Barcelona E-08028, Spain; Institute of Biomolecular Chemistry, Padova Unit, CNR, Department of Chemistry, University of Padova, 35131 Padova, Italy (literal)
Titolo
  • Correlation between symmetry breaker position and the preferences of conformationally constrained homopeptides: a molecular dynamics investigation (literal)
Abstract
  • The conformational tendencies of C-alpha,C-alpha-diethylglycine (Deg)-based peptides have been studied in solution using all atom molecular dynamics simulations. Specifically, the conformational effects of breaking the symmetry of the host Tfa-(Deg)(5)-OtBu (Tfa, trifluoroacetyl; OtBu, tert-butoxy) pentapeptide with punctual replacements at different sequence positions of one Deg residue by its corresponding guest chiral analogue, L-alpha-aminobutyric acid (L-Abu), have been examined by simulating the following peptides: Tja-(Deg)(5)-OtBu, Tfa-(Deg)(2)-L-Abu(Deg)(2)-OtBu, Tfa-(Deg)(3)-L-Abu-Deg-OtBu, and Tfa(Deg)(4)-L-Abu-OtBu. Simulations show that only the Deg homopeptide is able to stabilize a 2.0(5) helix, even though a kinked arrangement with all the Deg residues adopting a fully-extended conformation was found to be stable when the L-Abu residue is introduced in the middle of the sequence. On the other hand, when the L-Abu residue is closer to the C-end of the sequence, the peptide chain prefers a partially folded 3(10)-helix. Additional simulations on Tfa-(Deg)(3)-L-Abu-(Deg)(3)-OtBu highlighted that, when the size of the Deg segments increases, their tendency to adopt a 2.0(5) helix predominates over the preferred folded conformation of L-Abu. The overall picture extracted after more than 300 ns of molecular dynamics simulation is that breaking the alpha-carbon symmetry of achiral C-alpha-tetrasubstituted amino acids is a promising strategy to build up polypeptides with modulated conformational tendencies. (literal)
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