Dynamic Peptide Library for the Discovery of Charge Transfer Hydrogels
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Otros documentos de la autoría: Berdugo Gumbau, Cristina; Nalluri, Siva Krishna Mohan; Javid, Nadeem; Escuder, Beatriu; Miravet, Juan; Ulijn, R. V.
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http://dx.doi.org/10.1021/acsami.5b08968 |
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Título
Dynamic Peptide Library for the Discovery of Charge Transfer HydrogelsAutoría
Fecha de publicación
2015Editor
ACS PublicationsCita bibliográfica
BERDUGO GUMBAU, Cristina; NALLURI, Siva Krishna Mohan; JAVID, Nadeem; ESCUDER GIL, Beatriu; MIRAVET CELADES, Juan Felipe; ULIJN, R. V. Dynamic Peptide Library for the Discovery of Charge Transfer Hydrogels. ACS Applied Materials & Interfaces (2015), v. 7, n. 46, pp. 25946-25954Tipo de documento
info:eu-repo/semantics/articleVersión de la editorial
http://pubs.acs.org/doi/abs/10.1021/acsami.5b08968Palabras clave / Materias
Resumen
Coupling of peptide self-assembly to dynamic sequence exchange provides a useful approach for the discovery of self-assembling materials. In here, we demonstrate the discovery and optimization of aqueous, gel-phase ... [+]
Coupling of peptide self-assembly to dynamic sequence exchange provides a useful approach for the discovery of self-assembling materials. In here, we demonstrate the discovery and optimization of aqueous, gel-phase nanostructures based on dynamically exchanging peptide sequences that self-select to maximize charge transfer of n-type semiconducting naphthalenediimide (NDI)-dipeptide bioconjugates with various π-electron-rich donors (dialkoxy/hydroxy/amino-naphthalene or pyrene derivatives). These gel-phase peptide libraries are characterized by spectroscopy (UV–vis and fluorescence), microscopy (TEM), HPLC, and oscillatory rheology and it is found that, of the various peptide sequences explored (tyrosine Y-NDI with tyrosine Y, phenylalanine F, leucine L, valine V, alanine A or glycine G-NH2), the optimum sequence is tyrosine-phenylalanine in each case; however, both its absolute and relative yield amplification is dictated by the properties of the donor component, indicating cooperativity of peptide sequence and donor/acceptor pairs in assembly. The methodology provides an in situ discovery tool for nanostructures that enable dynamic interfacing of supramolecular electronics with aqueous (biological) systems. [-]
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ACS Applied Materials & Interfaces (2015), v. 7, n. 46Derechos de acceso
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info:eu-repo/semantics/restrictedAccess
info:eu-repo/semantics/restrictedAccess
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