Binding Kinetics of Biomolecule Interaction at Ultralow Concentrations Based on Gold Nanoparticle Enhancement

Please use this identifier to cite or link to this item: http://ir.lib.ncu.edu.tw/handle/987654321/51015

Title:	Binding Kinetics of Biomolecule Interaction at Ultralow Concentrations Based on Gold Nanoparticle Enhancement
Authors:	Su,LC;Chang,YF;Chou,C;Ho,JAA;Li,YC;Chou,LD;Lee,CC
Contributors:	光電科學與工程學系
Keywords:	FLUORESCENCE FIBEROPTIC BIOSENSOR;SURFACE-PLASMON RESONANCE;PROSTATE-SPECIFIC ANTIGEN;MASS-TRANSPORT;MOLECULAR RECOGNITION;IMMUNOGLOBULIN-G;HUMAN PROTEOME;AFFINITY;HETEROGENEITY;ANTIBODIES
Date:	2011
Issue Date:	2012-03-27 18:15:35 (UTC+8)
Publisher:	國立中央大學
Abstract:	Measuring the kinetic constants of protein-protein interactions at ultralow concentrations becomes critical in characterizing biospecific affinity, and exploring the feasibility of clinical diagnosis with respect to detection sensitivity, efficiency and accuracy. In this study, we propose a method that can calculate the binding constants of protein-protein interactions in sandwich assays at ultralow concentrations at the pg/mL level, using a localized surface plasmon coupled fluorescence fiber-optic biosensor (LSPCF-FOB). We discuss a two-compartment model to achieve reaction-limited kinetics under the stagnant conditions of the reaction chamber. The association rate constant, dissociation rate constant, and the equilibrium dissociation constant, that is, k(a), k(d), K(D), respectively, of the kinetics of binding between total prostate specific antigen (t-PSA) and anti-t-PSA at concentrations from 0.1 pg/mL to 1 ng/mL, were measured either in PBS or in human serum. This is the first time that k(a), k(d), and K(D) have been measured at such a low concentration range in a complex sample such as human serum.
Relation:	ANALYTICAL CHEMISTRY
Appears in Collections:	[Department of Optics and Photonics] journal & Dissertation

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