| Functionalization of gold nanoparticles with amino acid, beta-amyloid peptides and fragment. | |
| | |
MedLine Citation:
|
PMID: 20674288 Owner: NLM Status: In-Process |
Abstract/OtherAbstract:
|
Gold nanoparticles (Au NPs) were functionalized by cysteine (Cys), beta-amyloid peptides (Cys(0)Abeta(1-28), Cys(0)Abeta(1-40), Abeta(1-42)) and a pentapeptide fragment (Leu-Pro-Phe-Phe-Asp-OH (LPFFD-OH)). Optical absorption spectra of these systems were recorded and the plasmon resonance maximum values (lambda(max)) of the UV-vis spectra together with the transmission electron microscopy (TEM) images were also analysed. Both TEM images and the appearance of a new absorption band between approximately 720 and 750 nm in the visible spectra of the Au-cysteine and Au-LPFFD-OH systems most probably indicate that upon addition of these molecules to Au NPs-containing aqueous dispersions formation of aggregates is occurred. The wavelength shift between the two observed absorption bands in cysteine- and pentapeptide-modified Au NPs systems are Deltalambda=185 and 193 nm, respectively. These results suggest that the monodisperse spherical gold nanoparticles were arranged to chained structure due to the effect of these molecules. For confirmation of the binding of citrate and cysteine onto the plasmonic metal surface (1)H NMR measurements were also performed. (1)H NMR results may suggest that the citrate layer on the metal surface is replaced by cysteine leading to a formation of organic double layer structure. In the presence of beta-amyloid peptides the aggregation was not observed, especially in the Au-Cys(0)Abeta(1-40) and Au-Abeta(1-42) systems, however compared to the cysteine or LPFFD-OH-containing gold dispersion with Cys(0)Abeta(1-28) measurable less aggregation were occurred. The spectral parameters clearly suggest that Abeta(1-42) can attach or bind to the surface of gold nanoparticles via both the apolar and the N-donors containing side-chains of amino acids and no aggregation in the colloidal gold dispersion was observed. |
| | |
Authors:
|
A Majzik; L Fülöp; E Csapó; F Bogár; T Martinek; B Penke; G Bíró; I Dékány |
Related Documents
:
|
9057828 - Specific modulation of the fusogenic properties of the alzheimer beta-amyloid peptide b... 12070348 - The aspartate-257 of presenilin 1 is indispensable for mouse development and production... 8248178 - Beta-amyloid-(1-42) is a major component of cerebrovascular amyloid deposits: implicati... 18690708 - Biophysical analysis of progressive c-terminal truncations of human apolipoprotein e4: ... 6916768 - The aminoacyl-trna population of human reticulocytes. 17010618 - Discovery of novel, highly potent and selective beta-hairpin mimetic cxcr4 inhibitors w... |
Publication Detail:
|
Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2010-07-13 |
Journal Detail:
|
Title: Colloids and surfaces. B, Biointerfaces Volume: 81 ISSN: 1873-4367 ISO Abbreviation: Colloids Surf B Biointerfaces Publication Date: 2010 Nov |
Date Detail:
|
Created Date: 2010-08-24 Completed Date: - Revised Date: - |
Medline Journal Info:
|
Nlm Unique ID: 9315133 Medline TA: Colloids Surf B Biointerfaces Country: Netherlands |
Other Details:
|
Languages: eng Pagination: 235-41 Citation Subset: IM |
Copyright Information:
|
Copyright (c) 2010 Elsevier B.V. All rights reserved. |
Affiliation:
|
Supramolecular and Nanostructured Materials Research Group of the Hungarian Academy of Sciences, University of Szeged, 6720 Szeged Aradi vt 1, Hungary. |
Export Citation:
|
APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
|
|
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
Previous Document: Biocompatible novel starch/polyaniline composites: characterization, anti-cytotoxicity and antioxida...
Next Document: Nanomicelle with long-term circulation and enhanced stability of camptothecin based on mPEGylated al...