Key result
Cationic isotachophoresis separates and concentrates cTnI from serum albumin in ~10 minutes.
Why the study?
Effective separation and concentration of cardiac troponin I from high-abundance serum contaminants like albumin is needed for improved biomarker analysis.
Cationic isotachophoresis can be used as a rapid, on-chip technique to isolate the biomarker cardiac troponin I from high-abundance serum contaminants like albumin.
Answers are grounded in this paper and cite their sources.
May enable rapid microfluidic troponin assays; hypothesis-generating with clinical validation required before diagnostic use.
Cationic ITP was used to separate and concentrate fluorescently tagged cardiac troponin I (cTnI) from two proteins with similar isoelectric properties in a PMMA straight-channel microfluidic chip. In an initial set of experiments, cTnI was effectively separated from R-Phycoerythrin using cationic ITP in a pH 8 buffer system. Then, a second set of experiments was conducted in which cTnI was separated from a serum contaminant, albumin. Each experiment took ∼10 min or less at low electric field strengths (34 V/cm) and demonstrated that cationic ITP could be used as an on-chip removal technique to isolate cTnI from albumin. In addition to the experimental work, a 1D numerical simulation of our cationic ITP experiments has been included to qualitatively validate experimental observations.
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Jacroux et al. (2014) studied this question. Cationic isotachophoresis (ITP) was evaluated on Separation of fluorescently tagged cardiac troponin I (cTnI) from albumin. Cationic isotachophoresis effectively separated and concentrated fluorescently tagged cardiac troponin I from serum albumin in a microfluidic chip in approximately 10 minutes or less.
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