title: Interaction of the CLPFFD peptide with gold nanospheres. A Raman, surface enhanced Raman scattering and theoretical study.
abstract: In a previous work we demonstrated that toxic aggregates of the protein β-amyloid (ATAβ) 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. ATAβ) 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 10nm 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.
authors.affiliation: Depto de Química, Facultad de Ciencias, Universidad de Chile, Las Palmeras 3425, Ñuñoa, Santiago, Chile; Depto de Química, Facultad de Ciencias Químicas y Farmacéuticas, Universidad de Chile, Sergio Livingstone 1007, Independencia, Santiago, Chile.
authors.forename: A M
authors.initials: AM
authors.lastname: Vera
authors.affiliation: Depto de Antropología, Universidad de Tarapacá, Casilla 6D, Arica, Chile.
authors.forename: J J
authors.initials: JJ
authors.lastname: Cárcamo
authors.affiliation: Depto de Química, Facultad de Ciencias, Universidad de Chile, Las Palmeras 3425, Ñuñoa, Santiago, Chile.
authors.forename: A E
authors.initials: AE
authors.lastname: Aliaga
authors.affiliation: Depto de Química, Facultad de Ciencias, Universidad de Chile, Las Palmeras 3425, Ñuñoa, Santiago, Chile.
authors.forename: J S
authors.initials: JS
authors.lastname: Gómez-Jeria
authors.affiliation: Depto de Química, Facultad de Ciencias Químicas y Farmacéuticas, Universidad de Chile, Sergio Livingstone 1007, Independencia, Santiago, Chile; Advanced Center for Chronic Diseases (ACCDiS), Chile. Electronic address: mkogan@ciq.uchile.cl.
authors.forename: M J
authors.initials: MJ
authors.lastname: Kogan
authors.affiliation: Depto de Química, Facultad de Ciencias, Universidad de Chile, Las Palmeras 3425, Ñuñoa, Santiago, Chile. Electronic address: facien05@uchile.cl.
authors.forename: M M
authors.initials: MM
authors.lastname: Campos-Vallette
mesh_terms: D016229:Amyloid beta-Peptides / Q000378:metabolism*; D001224:Aspartic Acid / Q000737:chemistry; D003545:Cysteine / Q000737:chemistry; D006046:Gold / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D057927:Hydrophobic and Hydrophilic Interactions; D053768:Metal Nanoparticles / Q000737:chemistry; D008958:Models, Molecular; D054118:Nanospheres / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry* / Q000494:pharmacology; D010649:Phenylalanine / Q000737:chemistry; D011487:Protein Conformation; D013056:Spectrophotometry, Ultraviolet; D013059:Spectrum Analysis, Raman / Q000379:methods
chemical_list: D016229:Amyloid beta-Peptides; D010455:Peptides; D001224:Aspartic Acid; D010649:Phenylalanine; D006046:Gold; D003545:Cysteine
keywords: CLPFFD peptide; Extended Hückel Theory calculations; Peptide anti-aggregation of β-amyloid; SERS