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Binding Studies of L-Tryptophan to Human Serum Albumin with Nanogold-Structured Sensor by Piezoelectric Quartz Crystal Impedance Analysis

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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 nanogoldmodified 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 × 104 (mol l−1)−1 s−1 and 1.13, respectively, and 2.24 × 103 (mol l−1)−1 s−1 and 1.18, respectively for the binding process with competitor.
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Keywords: HAS; L-TRYPTOPHAN; NANOGOLD-MODIFIED SENSOR; UREMIC TOXINS

Document Type: Research Article

Publication date: 01 December 2011

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  • Journal for Nanoscience and Nanotechnology (JNN) is an international and multidisciplinary peer-reviewed journal with a wide-ranging coverage, consolidating research activities in all areas of nanoscience and nanotechnology into a single and unique reference source. JNN is the first cross-disciplinary journal to publish original full research articles, rapid communications of important new scientific and technological findings, timely state-of-the-art reviews with author's photo and short biography, and current research news encompassing the fundamental and applied research in all disciplines of science, engineering and medicine.
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