Self-Assembly of a Designed Amyloid Peptide Containing the Functional Thienylalanine Unit (Articolo in rivista)

Type
Label
  • Self-Assembly of a Designed Amyloid Peptide Containing the Functional Thienylalanine Unit (Articolo in rivista) (literal)
Anno
  • 2010-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1021/jp105508g (literal)
Alternative label
  • Hamley I. W., Brown G. D., Castelletto V., Cheng G., Venanzi M., Caruso M., Placidi E., Aleman C., Revilla-López G., Zanuy D. (2010)
    Self-Assembly of a Designed Amyloid Peptide Containing the Functional Thienylalanine Unit
    in The journal of physical chemistry. B; American Chemical Society, Washington (Stati Uniti d'America)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Hamley I. W., Brown G. D., Castelletto V., Cheng G., Venanzi M., Caruso M., Placidi E., Aleman C., Revilla-López G., Zanuy D. (literal)
Pagina inizio
  • 10674 (literal)
Pagina fine
  • 10683 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 114 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#note
  • http://dx.doi.org/10.1021/jp105508g (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • School of Chemistry, Food and Pharmacy, University of Reading, Whiteknights, Reading RG6 6AD, U.K., Department of Chemical Sciences and Technologies, CNR, Department of Physics, University of Rome Tor Vergata, Via Ricerca Scientifica 1, Rome, Italy, Departament d’Enginyeria Qiumica, E. T. S. d’Enginyeria Industrial de Barcelona, Universitat Politècnica de Catalunya, Diagonal 647, 08028 Barcelona, Spain, and Center for Research in Nano-Engineering, Universitat Politècnica de Catalunya, Campus Sud, Edifici C’, C/Pasqual i Vila s/n, Barcelona E-08028, Spain (literal)
Titolo
  • Self-Assembly of a Designed Amyloid Peptide Containing the Functional Thienylalanine Unit (literal)
Abstract
  • The self-assembly of a peptide based on a sequence from the amyloid beta peptide but incorporating the non-natural amino acid beta-2-thienylalanine (2-Thi) has been investigated in aqueous and methanol solutions. The peptide AAKLVFF was used as a design motif, replacing the phenylalanine residues (F) with 2-Thi units to yield (2-Thi)(2-Thi)VLKAA. The 2-Thi residues are expected to confer interesting electronic properties due to charge delocalization and pi-stacking. The peptide is shown to form beta-sheet-rich amyloid fibrils with a twisted morphology, in both water and methanol solutions at sufficiently high concentration. The formation of a self-assembling hydrogel is observed at high concentration. Detailed molecular modeling using molecular dynamics methods was performed using NOE constraints provided by 2D-NMR experiments. The conformational and charge properties of 2-Thi were modeled using quantum mechanical methods, and found to be similar to those previously reported for the beta-3-thienylalanine analogue. The molecular dynamics simulations reveal well-defined folded structures (turn-like) in dilute aqueous solution, driven by self-assembly of the hydrophobic aromatic units, with charged lysine groups exposed to water. (literal)
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