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On-line aptamer affinity solid-phase extraction capillary electrophoresis-mass spectrometry for the analysis of blood α-synuclein
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In this paper, an on-line aptamer affinity solid-phase extraction capillary electrophoresis-mass spectrometry method is described for the purification, preconcentration, separation, and characterization of α-synuclein (α-syn) in blood at the intact protein level. A single-stranded DNA aptamer is used to bind with high affinity and selectivity α-syn, which is a major component of Lewy bodies, the typical aggregated protein deposits found in Parkinson's disease (PD). Under the conditions optimized with recombinant α-syn, repeatability (2.1 and 5.4% percent relative standard deviation for migration times and peak areas, respectively) and microcartridge lifetime (around 20 analyses/microcartridge) were good, the method was linear between 0.5 and 10 µg·mL-1 and limit of detection was 0.2 µg·mL-1 (100 times lower than by CE-MS, 20 µg·mL-1). The method was subsequently applied to the analysis of endogenous α-syn from red blood cells lysate of healthy controls and PD patients.
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PERÓ GASCÓN, Roger, et al. On-line aptamer affinity solid-phase extraction capillary electrophoresis-mass spectrometry for the analysis of blood α-synuclein. Analytical Chemistry. 2019. Vol. 92, num. 1525-1533. ISSN 0003-2700. [consulted: 17 of August of 2026]. Available at: https://hdl.handle.net/2445/149622