Abstract

Nanogold-modified sensor was constructed and applied to study the binding of L-tryptophan to human serum albumin (HSA) in situ by piezoelectric quartz crystal impedance (PQCI) analysis. It was interesting that the as-prepared nanogold modified sensor was more sensitive and biocompatible than bare gold electrode. The frequency changes due to protein adsorption on the nanogold-modified sensor might be described as a sum of two exponential functions and detailed explanation was given. Additionally, the kinetics of the binding process was also investigated. The binding constant (K) and the number of binding site (n) for the binding process without competitor are fitted to be 1.07 x 10(4) (mol l(-1))(-1) s(-1) and 1.13, respectively, and 2.24 x 10(3) (mol l-(1))(-1) s(-1) and 1.18, respectively for the binding process with competitor.

Authors

Long Y, Yao S, Chen J

Institution

College of Chemistry, Chemical Engineering and Materials Science, Soochow University, Suzhou 215123, PR China.

Source

Journal of nanoscience and nanotechnology 11:12 2011 Dec pg 11074-8

MeSH

Gold
Humans
Kinetics
Metal Nanoparticles
Protein Binding
Serum Albumin
Tryptophan

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

22409059