期刊
JOURNAL OF THE AMERICAN SOCIETY FOR MASS SPECTROMETRY
卷 30, 期 7, 页码 1325-1329出版社
SPRINGER
DOI: 10.1007/s13361-019-02199-2
关键词
Amyloid-; Isomerization; MALDI; Immunoprecipitation
资金
- Russian Science Foundation [16-14-00181, 19-74-30007]
- Russian Science Foundation [19-14-11022, 19-74-30007] Funding Source: Russian Science Foundation
Immunoprecipitation (IP) combined with MALDI-TOF mass spectrometry is a powerful instrument for peptide and protein identification in biological samples. In this study, the analytical capabilities of MALDI-TOF/TOF mass spectrometry for relative quantitation of isoAsp7 in A(1-42) and A(1-16) were investigated. The possibility of quantitative determination of isoAsp7 in A(1-42) with the detection limit as low as 2pmol has been demonstrated. The same approach was applied for a shorter peptide A(1-16) and resulted in enhanced accuracy (3.2%), and lower detection limit (50fmol). Pilot experiments with artificial cerebrospinal fluid and mouse brain tissue were performed and showed that the proposed IP-MALDI-TOF/TOF approach could be applied for measuring isoA content in biological fluids and tissues. Additionally, it was shown that 6E10 anti-amyloid antibodies might affect the accuracy of the amyloid- quantitation in the presence of the isomerized peptide.
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