Open AccessInteractions between gold nanoparticles and amyloid β 25–35 peptide
Author(s) -
Peng Jian,
Weng Jian,
Ren Lei,
Sun LiPing
Publication year - 2014
Publication title -
iet nanobiotechnology
Language(s) - English
Resource type - Journals
ISSN - 1751-875X
DOI - 10.1049/iet-nbt.2013.0071
Subject(s) - thioflavin , circular dichroism , oligomer , monomer , chemistry , peptide , colloidal gold , transmission electron microscopy , nanoparticle , fluorescence , fibril , amyloid (mycology) , biophysics , crystallography , nuclear chemistry , nanotechnology , polymer , materials science , alzheimer's disease , biochemistry , organic chemistry , inorganic chemistry , disease , medicine , physics , pathology , quantum mechanics , biology
Amyloid β 25–35 ( Aβ 25–35 ) peptide is a peculiar peptide for its rapid aggregation properties and high neurotoxicity in Alzheimer's disease. Here, the interactions between gold nanoparticles (GNPs) and Aβ 25–35 monomers, oligomers and fibrils are explored under different molar ratio, temperature and pH by ultraviolet–visible and circular dichroism spectra, thioflavin T fluorescence assay and transmission electron microscope. It is concluded that Aβ 25–35 can induce the aggregation of GNPs at certain concentration of Aβ 25–35 monomer or oligomer. But at higher concentration of Aβ 25–35 , GNPs aggregates dissociate again. Furthermore, the aggregation rate increases at higher temperature or for lower pH. These results might provide the basis of a simple diagnostic tool for detecting Alzheimer's disease.