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A single-residue substitution inhibits fibrillization of Ala-based pentapeptides. A spectroscopic and molecular dynamics investigation
dc.contributor.author | Caruso, M. |
dc.contributor.author | Gatto, Emanuela |
dc.contributor.author | Placidi, E. |
dc.contributor.author | Venanzi, Mariano |
dc.contributor.author | Ballano Ballano, María Gema |
dc.contributor.author | Formaggio, Fernando |
dc.contributor.author | Toniolo, Claudio |
dc.contributor.author | Zanuy Gomara, David |
dc.contributor.author | Alemán Llansó, Carlos |
dc.contributor.other | Universitat Politècnica de Catalunya. Departament d'Enginyeria Química |
dc.date.accessioned | 2014-05-15T10:43:25Z |
dc.date.available | 2014-05-15T10:43:25Z |
dc.date.created | 2014-01-01 |
dc.date.issued | 2014-01-01 |
dc.identifier.citation | Caruso, M. [et al.]. A single-residue substitution inhibits fibrillization of Ala-based pentapeptides. A spectroscopic and molecular dynamics investigation. "Soft matter", 01 Gener 2014, vol. 10, núm. 15, p. 2508-2519. |
dc.identifier.issn | 1744-683X |
dc.identifier.uri | http://hdl.handle.net/2117/22996 |
dc.description.abstract | The aggregation properties of two Ala-based pentapeptides were investigated by spectroscopic techniques and molecular dynamics (MD) simulations. The two peptides, both functionalized at the N-terminus with a pyrenyl group, differ in the insertion of an alpha-aminoisobutyric acid residue at position 4. We showed that this single modification of the homo-peptide sequence inhibits the aggregation of the pentapeptide in aqueous solutions. Atomic force microscopy imaging revealed that the two peptides form mesoscopic aggregates of very different morphologies when deposited on mica. MD experiments showed that the two peptides have a very different propensity to form beta-pleated sheet structures, as confirmed by our spectroscopic measurements. The implications of these findings for our understanding of the mechanism leading to the formation of amyloid structures, primary responsible for numerous neurodegenerative diseases, are also discussed. |
dc.format.extent | 12 p. |
dc.language.iso | eng |
dc.rights | Attribution-NonCommercial-NoDerivs 3.0 Spain |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/3.0/es/ |
dc.subject | Àrees temàtiques de la UPC::Enginyeria química |
dc.subject.lcsh | Peptides |
dc.subject.lcsh | Spectroscopic techniques |
dc.subject.lcsh | Molecular dynamics--Computer simulation |
dc.subject.other | INFRARED CONFORMATIONAL-ANALYSIS |
dc.subject.other | ALPHA-AMINOISOBUTYRIC-ACID |
dc.subject.other | AMYLOID FIBRIL FORMATION |
dc.subject.other | HOMO-L-OLIGOPEPTIDES |
dc.subject.other | LINEAR OLIGOPEPTIDES |
dc.subject.other | SOLID-STATE |
dc.subject.other | PROLINE RESIDUE |
dc.subject.other | THIOPHENE DIMER |
dc.subject.other | BOUND ALANINE |
dc.subject.other | PI-STACKING |
dc.title | A single-residue substitution inhibits fibrillization of Ala-based pentapeptides. A spectroscopic and molecular dynamics investigation |
dc.type | Article |
dc.subject.lemac | Pèptids |
dc.subject.lemac | Anàlisi espectral |
dc.subject.lemac | Dinàmica molecular -- Simulació per ordinador |
dc.contributor.group | Universitat Politècnica de Catalunya. IMEM - Innovació, Modelització i Enginyeria en (BIO) Materials |
dc.identifier.doi | 10.1039/c3sm52831f |
dc.description.peerreviewed | Peer Reviewed |
dc.relation.publisherversion | http://pubs.rsc.org/en/Content/ArticleLanding/2014/SM/c3sm52831f#!divAbstract |
dc.rights.access | Open Access |
local.identifier.drac | 14143399 |
dc.description.version | Postprint (published version) |
local.citation.author | Caruso, M.; Gatto, E.; Placidi, E.; Venanzi, Mariano; Ballano, G.; Formaggio, F.; Toniolo, C.; Zanuy, D.; Aleman, C. |
local.citation.publicationName | Soft matter |
local.citation.volume | 10 |
local.citation.number | 15 |
local.citation.startingPage | 2508 |
local.citation.endingPage | 2519 |
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