Show simple item record

dc.contributor.authorCosta, Rui R.
dc.contributor.authorGonzález Pérez, Miguel 
dc.contributor.authorHerrero Gutiérrez, Marcos 
dc.contributor.authorPires, Ricardo A.
dc.contributor.authorAlonso Rodrigo, Matilde 
dc.contributor.authorRodríguez Cabello, José Carlos 
dc.contributor.authorReis, Rui Luís
dc.contributor.authorPashkuleva, Iva
dc.date.accessioned2019-04-04T09:54:19Z
dc.date.issued2018
dc.identifier.citationBiomacromolecules, 2018, Vol. 19, n. 8. p. 3401-3411es
dc.identifier.issn1525-7797es
dc.identifier.urihttp://uvadoc.uva.es/handle/10324/35331
dc.descriptionProducción Científicaes
dc.description.abstractWe introduce elastin-like recombinamers (ELRs) as polypeptides with precise amino acid positioning to generate polypeptide coatings with tunable rigidity. Two ELRs are used: V84- ELR, a hydrophobic monoblock, and EI-ELR, an amphiphilic diblock. Both were modified with the amine-reactive tetrakis (hydroxymethyl) phosphonium chloride compound. We evaluated the affinity, the conformation, and the dissipative behavior of ELRs assembled on alkanethiol selfassembled coatings by quartz crystal microbalance with dissipation monitoring, multi-parametric surface plasmon resonance, and atomic force microscopy. The thickness of the polypeptide coatings showcase the preferential affinity of ELRs to NH2 and CH3 terminated surfaces. We demonstrate that V84-ELR strongly bonded to the substrate and reorganizes into an extended and more hydrated layer as the adsorbed amount increases, whereas EI-ELR has a less dissipative behavior. The results suggest that ELR adsorption depends on the amino acid sequence and the substrate chemistry, ultimately influencing the stiffness of the polypeptide coatings.es
dc.format.mimetypeapplication/pdfes
dc.language.isoenges
dc.publisherACS Publicationses
dc.rights.accessRightsinfo:eu-repo/semantics/openAccesses
dc.subject.classificationModificación de superficiees
dc.subject.classificationSurface modificationes
dc.subject.classificationPolipéptidoses
dc.subject.classificationPolypeptideses
dc.titleTuning the stiffness of surfaces by assembling genetically engineered polypeptides with tailored amino acid sequencees
dc.typeinfo:eu-repo/semantics/articlees
dc.rights.holder© 2019 American Chemical Societyes
dc.identifier.doi10.1021/acs.biomac.8b00723es
dc.relation.publisherversionhttps://pubs.acs.org/doi/10.1021/acs.biomac.8b00723es
dc.peerreviewedSIes
dc.description.embargo2019-07-03es
dc.description.lift2019-07-03
dc.description.projectFundação para a Ciência e Tecnologia (grants SFRH/BPD/95446/2013 to R.R.C. and IF/00032/2013 to I.P.)es
dc.description.projectComisión Europea: H2020 programme-projects ELASTISLET (NMP-2014-646075), CHEM2NATURE (TWINN-2015-692333), FORECAST (WIDESPREAD-2014-2-668983), THE DISCOVERIES CTR (WIDESPREAD-01-2016-2017739572)es
dc.description.projectMinisterio de Economía, Industria y Competitividad (Project MAT2015-68901-R, MAT2016-78903-R)es
dc.description.projectJunta de Castilla y León (programa de apoyo a proyectos de investigación - Ref. VA015U16)es
dc.description.projectMinisterio de Educación, Cultura y Deporte (Proyect FPU15-00448)es


Files in this item

Thumbnail

This item appears in the following Collection(s)

Show simple item record