Interaction of the CLPFFD peptide with gold nanospheres. A Raman, surface enhanced Raman scattering and theoretical study
Author
dc.contributor.author
Vera, A. M.
Author
dc.contributor.author
Cárcamo, J. J.
Author
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Aliaga, A. E.
Author
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Gómez Jeria, Juan
Author
dc.contributor.author
Kogan Bocian, Marcelo
Author
dc.contributor.author
Campos Vallette, Marcelo
Admission date
dc.date.accessioned
2015-07-09T20:14:53Z
Available date
dc.date.available
2015-07-09T20:14:53Z
Publication date
dc.date.issued
2015
Cita de ítem
dc.identifier.citation
Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy 134 (2015) 251–256
en_US
Identifier
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Doi.org/10.1016/j.saa.2014.06.116
Identifier
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https://repositorio.uchile.cl/handle/2250/131912
General note
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Artículo de publicación ISI
en_US
Abstract
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In a previous work we demonstrated that toxic aggregates of the protein b-amyloid (ATAb) involved in
the Alzheimer’s disease (AD) can be destabilized upon electromagnetic irradiation of the peptide Cys-
Leu-Pro-Phe-Phe-Asp (CLPFFD) adsorbed on gold nanospheres (AuNSs). For a selective recognition of
the therapeutic target (i.e. ATAb) of AD by the conjugates peptide-nanoparticle it is relevant to understand
how the interaction between attached ligands and nanoparticles occurs. In this work a surface
enhanced Raman scattering spectroscopy (SERS) study of the interactions of CLPFFD with AuNSs of
10 nm average diameter was carried out. The SERS data suggest that phenylalanine displays its aromatic
ring coplanar to the surface which is supported by theoretical data obtained from molecular mechanics
(MM) and Extended Hückel Theory (EHT) calculations.
en_US
Patrocinador
dc.description.sponsorship
FONDECYT-Chile
projects 1130425 and 1110106, and FONDAP-Chile 15130011.
AMV acknowledges a doctoral fellowship from CONICYT for
financial support. JJC acknowledges projects MECESUP UTA-0801,
MECESUP UCH-0811 and Convenio de Desempeño HCSA Universidad
de Tarapacá-MINEDUC.