Highly sensitive detection of cardiac troponin I in human serum using gold nanoparticle-based enhanced sandwich immunoassay

2015 ◽  
Vol 221 ◽  
pp. 537-543 ◽  
Author(s):  
Wan-Joong Kim ◽  
Hyo Young Cho ◽  
Bong Kyu Kim ◽  
Chul Huh ◽  
Kwang Hyo Chung ◽  
...  
Keyword(s):  
Human Serum ◽  
Gold Nanoparticle ◽  
Cardiac Troponin ◽  
Troponin I ◽  
Cardiac Troponin I ◽  
Sandwich Immunoassay ◽  
Sensitive Detection ◽  
Highly Sensitive ◽  
Highly Sensitive Detection

Hollow gold nanoparticle-enhanced SPR based sandwich immunoassay for human cardiac troponin I

2017 ◽  
Vol 184 (7) ◽  
pp. 2395-2402 ◽  
Author(s):  
Qiong Wu ◽  
Shuo Li ◽  
Ying Sun ◽  
Junnan Wang
Keyword(s):  
Gold Nanoparticle ◽  
Cardiac Troponin ◽  
Troponin I ◽  
Cardiac Troponin I ◽  
Sandwich Immunoassay

scholarly journals A graphene oxide/gold nanoparticle-based amplification method for SERS immunoassay of cardiac troponin I

The Analyst ◽  
2019 ◽  
Vol 144 (5) ◽  
pp. 1582-1589 ◽  
Author(s):  
Xiuli Fu ◽  
Yunqing Wang ◽  
Yongming Liu ◽  
Huitao Liu ◽  
Longwen Fu ◽  
...  
Keyword(s):  
Graphene Oxide ◽  
Gold Nanoparticle ◽  
Cardiac Troponin ◽  
Signal Amplification ◽  
Troponin I ◽  
Cardiac Troponin I ◽  
Sensitive Detection ◽  
Multiple Signal ◽  
Amplification Method

A multiple signal amplification of a SERS biosensor was developed for sensitive detection of cTnI with the aid of GO/AuNP complexes.

scholarly journals Degradation of Cardiac Troponin I in Serum Complicates Comparisons of Cardiac Troponin I Assays

1999 ◽  
Vol 45 (7) ◽  
pp. 1018-1025 ◽  
Author(s):  
Qinwei Shi ◽  
Mingfu Ling ◽  
Xiaochen Zhang ◽  
Minyuan Zhang ◽  
Lilly Kadijevic ◽  
...  
Keyword(s):  
Western Blot ◽  
Human Serum ◽  
Cardiac Troponin ◽  
Troponin I ◽  
Cardiac Troponin I ◽  
Stable Region ◽  
Terminal Portion ◽  
Key Factor ◽  
The Stability ◽  
Serum Cardiac Troponin

Abstract Background: Up to a 20-fold variation in serum cardiac troponin I (cTnI) concentration may be observed for a given patient sample with different analytical methods. Because more limited variation is seen for control materials and for purified cTnI, we explored the possibility that cTnI was present in altered forms in serum. Methods: We used four recombinantly engineered cTnI fragments to study the regions of cTnI recognized by the Stratus®, Opus®, and ACCESS® immunoassays. The stability of these regions in serum was analyzed with Western blot. Results: The measurement of several control materials and different forms of purified cTnI using selected commercial assays demonstrated five- to ninefold variation. Both the Stratus and Opus assays recognized the N-terminal portion (NTP) of cTnI, whereas the ACCESS assay recognized the C-terminal portion (CTP) of cTnI. Incubation of recombinant cTnI in normal human serum produced a marked decrease in cTnI concentration as determined with the ACCESS, but not the Stratus, immunoassay. Western blot analysis of the same samples using cTnI NTP- and CTP-specific antibodies demonstrated preferential degradation of the CTP of cTnI. Conclusions: The availability of serum cTnI epitopes is markedly affected by the extent of ligand degradation. The N-terminal half of the cTnI molecule was found to be the most stable region in human serum. Differential degradation of cTnI is a key factor in assay-to-assay variation.

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