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dc.contributor.authorBhak, Ghibom
dc.contributor.authorMéndez Ardoy, Alejandro
dc.contributor.authorEscobedo, Albert
dc.contributor.authorSalvatella, Xavier
dc.contributor.authorMontenegro García, Javier
dc.date.accessioned2021-09-06T17:57:14Z
dc.date.issued2020
dc.identifier.citationBioconjugate Chem. 2020, 31, 12, 2759–2766
dc.identifier.issn1043-1802
dc.identifier.urihttp://hdl.handle.net/10347/26919
dc.description.abstractThe two-dimensional (2D) homogeneous assembly of nanoparticle monolayer arrays onto a broad range of substrates constitutes an important challenge for chemistry, nanotechnology, and material science. α-Synuclein (αS) is an intrinsically disordered protein associated with neuronal protein complexes and has a high degree of structural plasticity and chaperone activity. The C-terminal domain of αS has been linked to the noncovalent interactions of this protein with biological targets and the activity of αS in presynaptic connections. Herein, we have systematically studied peptide fragments of the chaperone-active C-terminal sequence of αS and identified a 17-residue peptide that preserves the versatile binding nature of αS. Attachment of this short peptide to gold nanoparticles afforded colloidally stable nanoparticle suspensions that allowed the homogeneous 2D adhesion of the conjugates onto a wide variety of surfaces, including the formation of crystalline nanoparticle superlattices. The peptide sequence and the strategy reported here describe a new adhesive molecule for the controlled monolayer adhesion of metal nanoparticles and sets a stepping-stone toward the potential application of the adhesive properties of αS
dc.description.sponsorshipThis work was partially supported by the Spanish Agencia Estatal de Investigación (AEI) [BIO2015-70092-R, SAF2017-89890-R], the Xunta de Galicia (ED431C 2017/25, 2016-AD031, AGAUR (2017 SGR 324), and Centro Singular de Investigación de Galicia accreditation 2016–2019, ED431G/09), the ISCIII (COV20/00297), and the European Union (European Regional Development Fund – ERDF). X.S. acknowledges funding from the ERC (CONCERT-648201). IRB Barcelona is the recipient of a Severo Ochoa Award (Government of Spain). J.M. received a Ramón y Cajal (RYC-2013-13784), an ERC Starting Grant (DYNAP-677786), and a Young Investigator Grant from the HFSP (RGY0066/2017)
dc.language.isoeng
dc.publisherAmerican Chemical Society
dc.relationinfo:eu-repo/grantAgreement/EC/H2020/677786
dc.relationinfo:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2017-2020/SAF2017-89890-R/ES/PEPTIDOS HIBRIDOS PARA EL TRANSPORTE SELECTIVO Y ENTREGA DE PROTEINAS TERAPEUTICAS
dc.relationinfo:eu-repo/grantAgreement/MINECO/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/BIO2015-70092-R/ES/EL DOMINIO INTRINSECAMENTE DESORDENADO DE TRANSACTIVACION DEL RECEPTOR DE ANDROGENOS COMO DIANA FARMACOLOGICA
dc.relationinfo:eu-repo/grantAgreement/MINECO/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/RYC-2013-13784/ES
dc.relationinfo:eu-repo/grantAgreement/EC/H2020/648201
dc.rightsCopyright © 2020 American Chemical Society
dc.subjectMetal nanoparticles
dc.subjectPeptides and proteins
dc.subjectSurface interactions
dc.subjectMonomers
dc.subjectConjugate acid-base pairs
dc.titleAn Adhesive Peptide from the C-Terminal Domain of α-Synuclein for Single-Layer Adsorption of Nanoparticles onto Substrates
dc.typeinfo:eu-repo/semantics/article
dc.identifier.DOI10.1021/acs.bioconjchem.0c00544
dc.relation.publisherversionhttps://doi.org/10.1021/acs.bioconjchem.0c00544
dc.description.embargo2021-11-10
dc.type.versioninfo:eu-repo/semantics/acceptedVersion
dc.identifier.e-issn1520-4812
dc.rights.accessrightsinfo:eu-repo/semantics/embargoedAccess
dc.contributor.affiliationUniversidade de Santiago de Compostela. Centro de Investigación en Química Biolóxica e Materiais Moleculares
dc.contributor.affiliationUniversidade de Santiago de Compostela. Departamento de Química Orgánica
dc.description.peerreviewedSI


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