How changes in the sequence of the peptide CLPFFD-NH(2) can modify the conjugation and stability of gold nanoparticles and their affinity for beta-amyloid fibrils

Olmedo, I; Araya, E.; Sanz, F; Medina, E; Arbiol, J; Toledo, P; Alvarez-Lueje, A; Giralt E.; Kogan, MJ

Abstract

In a previous work, we studied the interaction of β-amyloid fibrils (Aβ) with gold nanoparticles (AuNP) conjugated with the peptide CLPFFD-NH2. Here, we studied the effect of changing the residue sequence of the peptide CLPFFD-NH2 on the efficiency of conjugation to AuNP, the stability of the conjugates, and the affinity of the conjugates to the Aβ fibrils. We conjugated the AuNP with CLPFFD-NH2 isomeric peptides (CDLPFF-NH2 and CLPDFF-NH2) and characterized the resulting conjugates with different techniques including UV-Vis, TEM, EELS, XPS, analysis of amino acids, agarose gel electrophoresis, and CD. In addition, we determined the proportion of AuNP bonded to the Aβ fibrils by ICP-MS. AuNP-CLPFFD-NH2 was the most stable of the conjugates and presented more affinity for Aβ fibrils with respect to the other conjugates and bare AuNP. These findings help to better understand the way peptide sequences affect conjugation and stability of AuNP and their interaction with Aβ fibrils. The peptide sequence, the steric effects, and the charge and disposition of hydrophilic and hydrophobic residues are crucial parameters when considering the design of AuNP peptide conjugates for biomedical applications. © 2008 American Chemical Society.

Más información

Título según WOS: How changes in the sequence of the peptide CLPFFD-NH(2) can modify the conjugation and stability of gold nanoparticles and their affinity for beta-amyloid fibrils
Título según SCOPUS: How changes in the sequence of the peptide CLPFFD-NH2 can modify the conjugation and stability of gold nanoparticles and their affinity for ß-amyloid fibrils
Título de la Revista: BIOCONJUGATE CHEMISTRY
Volumen: 19
Número: 6
Editorial: AMER CHEMICAL SOC
Fecha de publicación: 2008
Página de inicio: 1154
Página final: 1163
Idioma: English
URL: http://pubs.acs.org/doi/abs/10.1021/bc800016y
DOI:

10.1021/bc800016y

Notas: ISI, SCOPUS