Unbound MEDLINE

Binding studies of L-tryptophan to human serum albumin with nanogold-structured sensor by piezoelectric quartz crystal impedance analysis.

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.

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  • Publisher Full Text
  • Authors

    Long Y, Yao S, Chen J

    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