Artículo de revista
Interaction of the CLPFFD peptide with gold nanospheres. A Raman, surface enhanced Raman scattering and theoretical study
Fecha
2015Registro en:
Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy 134 (2015) 251–256
Doi.org/10.1016/j.saa.2014.06.116
Autor
Vera, A. M.
Cárcamo, J. J.
Aliaga, A. E.
Gómez Jeria, Juan
Kogan Bocian, Marcelo
Campos Vallette, Marcelo
Institución
Resumen
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.