Interaction of the CLPFFD peptide with gold nanospheres. A Raman, surface enhanced Raman scattering and theoretical studyReport as inadecuate




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In a previous work we demonstrated that toxic aggregates of the protein b-amyloid ATAb involved inthe 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 ofthe therapeutic target i.e. ATAb of AD by the conjugates peptide-nanoparticle it is relevant to understandhow the interaction between attached ligands and nanoparticles occurs. In this work a surfaceenhanced Raman scattering spectroscopy SERS study of the interactions of CLPFFD with AuNSs of10 nm average diameter was carried out. The SERS data suggest that phenylalanine displays its aromaticring coplanar to the surface which is supported by theoretical data obtained from molecular mechanicsMM and Extended Hückel Theory EHT calculations.Nota general

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Author: Vera, A. M.; - Cárcamo, J. J.; - Aliaga, A. E.; - Gómez Jeria, Juan; - Kogan, Marcelo; - Campos Vallette, Marcelo; -

Source: http://repositorio.uchile.cl/



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