| dc.description.abstract | In a previous work, we studied the interaction of -amyloid fibrils (A ) 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 A 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 A fibrils by ICP-MS. AuNP-CLPFFD-NH2 was the most stable of the conjugates and
presented more affinity for A 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
A 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. | |
