Interaction of the CLPFFD peptide with gold nanospheres. A Raman, surface enhanced Raman scattering and theoretical study
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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.
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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.
Quote ItemSpectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy 134 (2015) 251–256
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