Using A Fiber Optic Particle Plasmon Resonance Biosensor To Determine Kinetic Constants of Antigen-Antibody Binding Reaction

被引:48
作者
Chang, Ting-Chou [1 ,3 ]
Wu, Chao-Ching [1 ,3 ]
Wang, Shau-Chun [1 ,3 ]
Chau, Lai-Kwan [1 ,3 ]
Hsieh, Wen-Hsin [2 ,3 ]
机构
[1] Natl Chung Cheng Univ, Dept Chem & Biochem, Chiayi 621, Taiwan
[2] Natl Chung Cheng Univ, Dept Mech Engn, Chiayi 621, Taiwan
[3] Natl Chung Cheng Univ, Ctr Nano Biodetect, Chiayi 621, Taiwan
关键词
MASS-TRANSPORT; PROTEIN INTERACTIONS; REAL-TIME; SURFACE; SENSOR; MATRIX; RANGE;
D O I
10.1021/ac302590n
中图分类号
O65 [分析化学];
学科分类号
070302 ; 081704 ;
摘要
In this paper, one simple and label-free biosensing method has been developed for determining the binding kinetic constants of antiovalbumin antibody (anti-OVA) and anti-mouse IgG antibody using the fiber optic particle plasmon resonance (FOPPR) biosensor. The FOPPR sensor is based on gold-nanoparticle-modified optical fiber, where the gold nanoparticle surface has been modified by a mixed self-assembled monolayer for conjugation of a molecular probe reporter (ovalbumin or mouse IgG) to dock with the corresponding analyte species such as anti-OVA or anti-mouse IgG. The binding process, occurring when an analyte reacts with a probe molecule immobilized on the optical fiber, can be monitored in real-time. In addition, by assuming a Langmuir-type adsorption isotherm to measure the initial binding rate, the quantitative determination of binding kinetic constants, the association and dissociation rate constants, yields k(a) of (7.21 +/- 0.4) x 10(3) M-1 s(-1) and k(d) of (2.97 +/- 0.1) x 10(-3) s(-1) for OVA/anti-OVA and k(a) of (1.45 +/- 0.2) x 10(6) M-1 s(-1) and k(d) of (2.97 +/- 0.6) x 10(-2) s(-1) for mouse IgG/anti-mouse IgG. We demonstrate that the FOPPR biosensor can study real-time biomolecular interactions.
引用
收藏
页码:245 / 250
页数:6
相关论文
共 35 条
[21]   Nanosphere lithography: Effect of the external dielectric medium on the surface plasmon resonance spectrum of a periodic array of sliver nanoparticles [J].
Jensen, TR ;
Duval, ML ;
Kelly, KL ;
Lazarides, AA ;
Schatz, GC ;
Van Duyne, RP .
JOURNAL OF PHYSICAL CHEMISTRY B, 1999, 103 (45) :9846-9853
[22]   THE EFFECT OF TEMPERATURE ON THE BINDING-KINETICS AND EQUILIBRIUM-CONSTANTS OF MONOCLONAL-ANTIBODIES TO CELL-SURFACE ANTIGENS [J].
JOHNSTONE, RW ;
ANDREW, SM ;
HOGARTH, MP ;
PIETERSZ, GA ;
MCKENZIE, IFC .
MOLECULAR IMMUNOLOGY, 1990, 27 (04) :327-333
[23]   Monoclonal antibody-based enzyme-linked immunosorbent assay for the insecticide imidacloprid [J].
Kim, HJ ;
Shelver, WL ;
Li, QX .
ANALYTICA CHIMICA ACTA, 2004, 509 (01) :111-118
[24]   Extending the range of rate constants available from BIACORE: Interpreting mass transport-influenced binding data [J].
Myszka, DG ;
He, X ;
Dembo, M ;
Morton, TA ;
Goldstein, B .
BIOPHYSICAL JOURNAL, 1998, 75 (02) :583-594
[25]   A colorimetric gold nanoparticle sensor to interrogate biomolecular interactions in real time on a surface [J].
Nath, N ;
Chilkoti, A .
ANALYTICAL CHEMISTRY, 2002, 74 (03) :504-509
[26]   Regional and segmental flexibility of antibodies in interaction with antigens of different size [J].
Oda, M ;
Uchiyama, S ;
Robinson, CV ;
Fukui, K ;
Kobayashi, Y ;
Azuma, T .
FEBS JOURNAL, 2006, 273 (07) :1476-1487
[27]   Kinetic measurements of DNA hybridisation an an oligonucleotide-immobilized 27-MHz quartz crystal microbalance [J].
Okahata, Y ;
Kawase, M ;
Niikura, K ;
Ohtake, F ;
Furusawa, H ;
Ebara, Y .
ANALYTICAL CHEMISTRY, 1998, 70 (07) :1288-1296
[28]   Biomolecular recognition based on single gold nanoparticle light scattering [J].
Raschke, G ;
Kowarik, S ;
Franzl, T ;
Sonnichsen, C ;
Klar, TA ;
Feldmann, J ;
Nichtl, A ;
Kürzinger, K .
NANO LETTERS, 2003, 3 (07) :935-938
[29]   Surface plasmon resonance analysis of staphylococcal enterotoxin B in food [J].
Rasooly, A .
JOURNAL OF FOOD PROTECTION, 2001, 64 (01) :37-43
[30]   Kinetics of ligand binding to receptor immobilized in a polymer matrix, as detected with an evanescent wave biosensor .1. A computer simulation of the influence of mass transport [J].
Schuck, P .
BIOPHYSICAL JOURNAL, 1996, 70 (03) :1230-1249