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

Spectrochim Acta A Mol Biomol Spectrosc. 2015 Jan 5:134:251-6. doi: 10.1016/j.saa.2014.06.116. Epub 2014 Jun 27.

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.

Keywords: CLPFFD peptide; Extended Hückel Theory calculations; Peptide anti-aggregation of β-amyloid; SERS.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amyloid beta-Peptides / metabolism*
  • Aspartic Acid / chemistry
  • Cysteine / chemistry
  • Gold / chemistry*
  • Hydrogen-Ion Concentration
  • Hydrophobic and Hydrophilic Interactions
  • Metal Nanoparticles / chemistry
  • Models, Molecular
  • Nanospheres / chemistry*
  • Peptides / chemistry*
  • Peptides / pharmacology
  • Phenylalanine / chemistry
  • Protein Conformation
  • Spectrophotometry, Ultraviolet
  • Spectrum Analysis, Raman / methods

Substances

  • Amyloid beta-Peptides
  • Peptides
  • Aspartic Acid
  • Phenylalanine
  • Gold
  • Cysteine