Protein seeding of gold nanoparticles and mechanism of glycation sensing

Abstract The plasmon resonance of gold nanoparticles (GNPs) synthesized on a protein template senses formation of advanced glycosylated end products (AGEs). A graded alteration of plasmon resonance (both the peak and intensity are affected) is observed as the glycation progresses. Transmission elect...

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Bibliographic Details
Published in:Nanomedicine 2007-09, Vol.3 (3), p.208-214
Main Authors: GhoshMoulick, Ranjita, PhD, Bhattacharya, Jaydeep, MS, Mitra, Chanchal K., PhD, Basak, Soumen, PhD, Dasgupta, Anjan Kr., PhD
Format: Article
Language:English
Subjects:
Biosensing Techniques - methods
Coated Materials, Biocompatible - chemistry
Glycation
Glycation End Products, Advanced - analysis
Glycation End Products, Advanced - chemistry
Gold - chemistry
Gold nanoparticle
Hemoglobins - chemistry
Hemoglobins - ultrastructure
Internal Medicine
Materials Testing
Nanoparticles - chemistry
Nanoparticles - ultrastructure
Nanotechnology - methods
Plasmon resonance
Surface Plasmon Resonance - methods
Surface Properties
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Summary:Abstract The plasmon resonance of gold nanoparticles (GNPs) synthesized on a protein template senses formation of advanced glycosylated end products (AGEs). A graded alteration of plasmon resonance (both the peak and intensity are affected) is observed as the glycation progresses. Transmission electron microscopy shows significant shift of the size distribution of GNPs in presence of glycation. The higher plasmon resonance is thus caused by increased formation of GNPs, which in turn is attributed to a larger number of smaller particles. To study the binding of the protein with the GNP, infrared (IR) spectroscopy and circular dichroism (CD) studies were undertaken. Whereas the CD studies confirmed the emergence of β-structure and loss of α-helix, the IR data indicated glycation-induced alterations in the amide I region. The proposed sensor for formation of AGEs thus apparently operates by direct or indirect conjugation with amino groups. Incidentally, glycation and AGE formation are responsible for a number of diabetes-related clinical conditions, and the present approach could be adopted for use for a simple colorimetric assay for the AGEs.
ISSN:1549-9634
1549-9642
DOI:10.1016/j.nano.2007.04.002