Electrochemiluminescent immunoassay for rat skeletal troponin I (Tnni2) in serum

Sun, Deqin; Hamlin, D. M.; Butterfield, Anthony; Watson, David E.; Smith, Holly W.

doi:10.1016/j.vascn.2009.09.002

Cited by 10 publications

(6 citation statements)

References 20 publications

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“…There are no clear treatment-related effects on serum creatine phosphokinase levels at doses where histopathology is initially noted. The sponsor demonstrates a significant treatmentrelated rise in serum skeletal troponin I using a recently developed assay [30] on the same samples retained from interim and final necropsy bleeds during the 1-month rat study and at the high dose of the dog study. Since serum skeletal troponin responses have been reported in clinical instances of muscle injury previously [31,32], the sponsor proceeds into Phase I studies, future science group Review Sistare & DeGeorge incorporating longitudinal measurements of skeletal troponin I along with the conventional creatine phosphokinase measurements to maintain investment in the lead compound and to understand the promise of pharmacologic engagement of this novel target.…”

Section: Hypothetical Example 7: the Use Of Tsbs To Investigate Concementioning

confidence: 99%

Promise of New Translational Safety Biomarkers in Drug Development and Challenges to Regulatory Qualification

Sistare

DeGeorge

2011

Biomarkers Med.

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One promise of new translational safety biomarkers (TSBs) is their ability to demonstrate that toxicities in animal studies are monitorable at an early stage, such that human relevance of potential adverse effects of drugs can be safely and definitively evaluated in clinical trials. Another is that they would provide an earlier, more definitive and deeper insight to patient prognosis compared with conventional biomarkers. Recent experience with regulatory authorities indicates that resource demands for new TSB qualifications under the current framework are daunting and the rate of their expansion will be slow, particularly in light of mounting financial pressures on the pharmaceutical industry. Sponsors face a dilemma over engaging in safety biomarker qualification consortia. While it is clear new TSBs could be considered catalysts to drug development and that patient health, business and scientific benefits, described here using examples, should outweigh qualification costs, concerns exist that early ambiguities in biomarker interpretations at the introduction of such new TSBs might hinder drug development.

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Section: Hypothetical Example 7: the Use Of Tsbs To Investigate Concementioning

confidence: 99%

Promise of New Translational Safety Biomarkers in Drug Development and Challenges to Regulatory Qualification

Sistare

DeGeorge

2011

Biomarkers Med.

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“…For example, two ECL immunosensors were reported by Cui et al for human cTnI detection using luminol and N--(aminobutyl)-N-(ethylisoluminol)-functionalized gold nanoparticles (AuNPs) as signals [11,12]. An ECL immunoassay was developed by Smith for the detection of rat TnI in serum [13]. Ruan reported an ECL immunosensor for the detection of cTnI by using self-enhanced ECL luminophore [14].…”

Section: Introductionmentioning

confidence: 99%

Electrogenerated chemiluminescence peptide-based biosensing method for cardiac troponin I using peptide-integrating Ru(bpy)3 2+-functionalized gold nanoparticles as nanoprobe

Dong

et al. 2015

Gold Bull

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A sensitive electrogenerated chemiluminescence peptide-based (ECL-PB) biosensing method for the determination of protein was developed by employing peptideintegrating Ru(bpy) 3 2+ (bpy=2,2′-bipyridine)-functionalized gold nanoparticles (Ru(bpy) 3 2+-AuNPs-peptide) as nanoprobe. Cardiac troponin I (cTnI), a reliable clinical biomarker for the detection of cardiac injury, was chosen as target protein, while a specific binding peptide (CFYSHSFHENWPS) was used as molecular recognition element. AuNPs were firstly functionalized with Ru(bpy) 3 2+ through electrostatic interactions between citrate-capped AuNPs and Ru(bpy) 3 2+ to form Ru(bpy) 3 2+-AuNPs aggregates and then functionalized with peptide through Au-S bounds to form Ru(bpy) 3 2+-AuNPs-peptide nanoprobe. AuNPs not only can capture numerous signalgenerating molecules, resulting in high ECL intensity but also can capture a significant amount of the peptide, providing poly binding motif. The specific capture peptide was self-assembled on the surface of a gold electrode and then incubated with the target cTnI and Ru(bpy) 3 2+ -AuNPs-peptide successively. A sandwich-type peptide/cTnI/Ru(bpy) 3 2+ -AuNPs-peptide conjugate was formed on the surface of the electrode and an ECL signal was obtained in the presence of tri-n-propylamine. The novel biosensing method facilitates the sensitive detection of cTnI in the range from 3.0 × 10 −12 g mL −1 to 7.0 × 10 −11 g mL −1 with a low detection limit of 0.5 pg mL. This work provides a promising strategy for the determination of proteins with simplicity, high sensitivity, and selectivity.

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“…Several ECL methods have been developed for the determination of TnI [11][12][13][14][15]. Cui designed ECL immunosensor for the detection of human cardiac troponin I by using luminol [11] and N-(aminobutyl)-N-(ethylisoluminol) [12] -functionalized gold nanoparticles as labels.…”

Section: Introductionmentioning

confidence: 99%

“…Cui designed ECL immunosensor for the detection of human cardiac troponin I by using luminol [11] and N-(aminobutyl)-N-(ethylisoluminol) [12] -functionalized gold nanoparticles as labels. Smith developed an ECL immunoassay for detection of rat TnI in serum [13]. The commonly used ECL immunoassays are normally conducted by employing antibodies as molecular recognition elements.…”

Section: Introductionmentioning

confidence: 99%

Sensitive electrogenerated chemiluminescence peptide-based biosensor for the determination of troponin I with gold nanoparticles amplification

Meng

Qiu

et al. 2013

Gold Bull

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A sensitive electrogenerated chemiluminescence (ECL) peptide-based biosensor was fabricated for the determination of troponin I (TnI) by employing gold nanoparticles as amplification platform. Two specific peptides including peptide1 with a sequence of CFYSHSFHENWPS and peptide2 with a sequence of FYSHSFHENWPSK were employed as capture peptide and report peptide, respectively. The peptide2 was labeled with ruthenium bis(2,2′-bipyridine) (2,2′-bipyridine-4,4′-dicarboxylic acid)-N-hydroxysuccinimide ester (Ru(bpy) 2 (dcbpy)NHS) at NH 2 -containing lysine via acylation reaction and utilized as the ECL probe. Gold nanoparticles were electrodeposited onto gold electrode and used as an amplification platform. The peptide-based biosensor was fabricated by self-assembling peptide1 onto the surface of gold nanoparticles-modified gold electrode through a thiolcontaining cysteine at the end of the peptide1. When the biosensor reacted with target TnI, and then incubated with the ECL probe, a strong ECL response was electrochemically generated. The ECL intensity is directly proportional to the logarithm of the concentration of TnI in the range from 1 to 300 pg/mL. The biosensor employing gold nanoparticles as amplification platform shows high sensitivity for the detection of TnI with a detection limit of 0.4 pg/mL (S/N =3). Moreover, the biosensor is successfully applied to analysis of TnI in human serum sample. This work demonstrates that the combination of a highly binding peptide with nanoparticle amplification is a great promising approach for the design of ECL biosensor.

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Electrochemiluminescent immunoassay for rat skeletal troponin I (Tnni2) in serum

Cited by 10 publications

References 20 publications

Promise of New Translational Safety Biomarkers in Drug Development and Challenges to Regulatory Qualification

Promise of New Translational Safety Biomarkers in Drug Development and Challenges to Regulatory Qualification

Electrogenerated chemiluminescence peptide-based biosensing method for cardiac troponin I using peptide-integrating Ru(bpy)3 2+-functionalized gold nanoparticles as nanoprobe

Sensitive electrogenerated chemiluminescence peptide-based biosensor for the determination of troponin I with gold nanoparticles amplification

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