Immunodetection of pentamer and modified C-reactive protein using surface plasmon resonance biosensing

被引:65
作者
Hu, WP
Hsu, HY [1 ]
Chiou, A
Tseng, KY
Lin, HY
Chang, GL
Chen, SJ
机构
[1] Natl Yang Ming Univ, Inst Biotechnol Med, Taipei 112, Taiwan
[2] Natl Cheng Kung Univ, Inst Biomed Engn, Tainan 701, Taiwan
[3] Natl Yang Ming Univ, Inst Biophoton Engn, Taipei 112, Taiwan
[4] Natl Chen Kung Univ, Dept Engn Sci, Tainan 701, Taiwan
关键词
C-reactive protein; surface plasmon resonance biosensor; optical biosensing; cardiovascular disease; antibody-antigen;
D O I
10.1016/j.bios.2005.11.001
中图分类号
Q6 [生物物理学];
学科分类号
071011 ;
摘要
In clinical practices, the examination of pentamer C-reactive protein (pCRP) is commonly used as a prognostic indicator of the risk of a patient developing cardiovascular disease (CVD). Structural modification of pCRP produces a modified CRP (mCRP) which exhibits different biological activities in the body. In recent years, mCRP has come to be regarded as a more powerful inducer than pCRP, and hence mCRP measurement has emerged as an important indicator for assessing the risk of developing CVD. The surface plasmon resonance (SPR) biosensing technique can be employed to increase the detection accuracy and real-time response when sensing pCRP or mCRP. In this study, three monoclonal antibodies (Mabs), C8. 8D8. and 9C9. are immobilized on a protein G layer for subsequent CRP detection. The experimental results reveal that the Mab C8 reacts with both pCRP and mCRP, the Mab 8D8 with pCRP, and the Mab 9C9 with mCRP. No false signals caused by non-specific binding are observed. When detecting pCRP using Mab C8, the SPR bioassay provides sufficient sensitivity to evaluate whether or not a patient is at risk of developing CVD. SPR biosensing provides a viable and accurate approach for the real-time evaluation of pCRP and mCRP levels, and is therefore of considerable benefit in clinical examinations of CPR. (c) 2005 Elsevier B.V. All rights reserved.
引用
收藏
页码:1631 / 1637
页数:7
相关论文
共 38 条
[1]   Plasma leptin concentration in patients with Type 2 diabetes: relationship to cardiovascular disease risk factors and insulin resistance [J].
Abdella, NA ;
Mojiminiyi, OA ;
Moussa, MA ;
Zaki, M ;
Al Mohammedi, H ;
Al Ozairi, ESS ;
Al Jebely, S .
DIABETIC MEDICINE, 2005, 22 (03) :278-285
[2]   Study on orientation of immunogrlobulin G on protein G layer [J].
Bae, YM ;
Oh, BK ;
Lee, W ;
Lee, WH ;
Choi, JW .
BIOSENSORS & BIOELECTRONICS, 2005, 21 (01) :103-110
[3]   BACTERIAL FC-RECEPTORS [J].
BOYLE, MDP ;
REIS, KJ .
BIO-TECHNOLOGY, 1987, 5 (07) :697-703
[4]   Partially purified fraction (PPF) antigen from adult Fasciola gigantica for the serodiagnosis of human fascioliasis using Dot-ELISA technique [J].
Dalimi, A ;
Hadighi, R ;
Madani, R .
ANNALS OF SAUDI MEDICINE, 2004, 24 (01) :18-20
[5]   Mechanisms of disease: Acute-phase proteins and other systemic responses to inflammation [J].
Gabay, C ;
Kushner, I .
NEW ENGLAND JOURNAL OF MEDICINE, 1999, 340 (06) :448-454
[6]  
GAEDE W, 2002, BIOCHEMICA, V3, P4
[7]   C-reactive protein binds to apoptotic cells, protects the cells from assembly of the terminal complement components, and sustains an antiinflammatory innate immune response: Implications for systemic autoimmunity [J].
Gershov, D ;
Kim, S ;
Brot, N ;
Elkon, KB .
JOURNAL OF EXPERIMENTAL MEDICINE, 2000, 192 (09) :1353-1363
[8]   C-reactive protein and complement are important mediators of tissue damage in acute myocardial infarction [J].
Griselli, M ;
Herbert, J ;
Hutchinson, WL ;
Taylor, KM ;
Sohail, M ;
Krausz, T ;
Pepys, MB .
JOURNAL OF EXPERIMENTAL MEDICINE, 1999, 190 (12) :1733-1739
[9]   C-REACTIVE PROTEIN - CURRENT STATUS AND FUTURE PERSPECTIVES [J].
HOKAMA, Y ;
NAKAMURA, RM .
JOURNAL OF CLINICAL LABORATORY ANALYSIS, 1987, 1 (01) :15-27
[10]   Surface plasmon resonance sensors: review [J].
Homola, J ;
Yee, SS ;
Gauglitz, G .
SENSORS AND ACTUATORS B-CHEMICAL, 1999, 54 (1-2) :3-15