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dc.contributor.authorZanuy Gomara, David
dc.contributor.authorRevilla López, Guillermo
dc.contributor.authorHamley, I. W.
dc.contributor.authorBrown, Gordon D.A.
dc.contributor.authorCastelletto, V.
dc.contributor.authorCheng, G.
dc.contributor.authorVenanzi, M.
dc.contributor.authorCaruso, M.
dc.contributor.authorPlacidi, E.
dc.contributor.authorAlemán Llansó, Carlos
dc.contributor.otherUniversitat Politècnica de Catalunya. Departament d'Enginyeria Química
dc.date.accessioned2010-11-09T17:50:33Z
dc.date.available2010-11-09T17:50:33Z
dc.date.created2010-08-19
dc.date.issued2010-08-19
dc.identifier.citationHamley, . [et al.]. Self-Assembly of a Designed Amyloid Peptide Containing the Functional Thienylalanine Unit. "Journal of physical chemistry B", 19 Agost 2010, vol. 114, núm. 32, p. 10674-10683.
dc.identifier.issn1520-6106
dc.identifier.urihttp://hdl.handle.net/2117/10229
dc.description.abstractThe self-assembly of a peptide based on a sequence from the amyloid peptide but incorporating the nonnatural amino acid -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 π-stacking. The peptide is shown to form -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 -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.
dc.format.extent10 p.
dc.language.isoeng
dc.rightsAttribution-NonCommercial-NoDerivs 3.0 Spain
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/3.0/es/
dc.subjectÀrees temàtiques de la UPC::Enginyeria química
dc.subjectÀrees temàtiques de la UPC::Energies
dc.subject.lcshChemical engineering
dc.titleSelf-Assembly of a Designed Amyloid Peptide Containing the Functional Thienylalanine Unit
dc.typeArticle
dc.subject.lemacBioquímica
dc.contributor.groupUniversitat Politècnica de Catalunya. IMEM - Innovació, Modelització i Enginyeria en (BIO) Materials
dc.identifier.doi10.1021/jp105508g
dc.description.peerreviewedPeer Reviewed
dc.relation.publisherversionhttp://www.ncbi.nlm.nih.gov/pubmed/20662537
dc.rights.accessRestricted access - publisher's policy
local.identifier.drac2747451
dc.description.versionPostprint (published version)
local.citation.authorHamley, .; Brown, G.; Castelletto, V.; Cheng, G.; Venanzi, M.; Caruso, M.; Placidi, E.; Alemán, C.; Revilla-López, G.; Zanuy, D.
local.citation.publicationNameJournal of physical chemistry B
local.citation.volume114
local.citation.number32
local.citation.startingPage10674
local.citation.endingPage10683


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