کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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1193314 | 1492273 | 2013 | 6 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Fluorophore-assisted laser desorption/ionization-mass spectrometry (FALDI-MS) Fluorophore-assisted laser desorption/ionization-mass spectrometry (FALDI-MS)](/preview/png/1193314.png)
• Direct analysis of fluorescently labeled peptides by LDI-MS is demonstrated for the first time.
• Peptides labeled on their N-termini with rhodamine B were analyzed by FALDI MS and MS/MS without the addition of a matrix.
• MS/MS spectra of fluorescently labeled peptides show exclusively a and b ion series enabling easier peptide sequencing.
• FALDI-MS allows for selective ionization of the fluorescently labeled peptides in peptide mixtures.
The direct analysis of fluorescently labeled peptides by laser desorption/ionization-mass spectrometry (LDI-MS) is demonstrated for the first time. Peptides labeled on their N-termini with rhodamine B were analyzed by MS and tandem MS (MS/MS) using a recently developed visible-wavelength LDI-MS instrument. Labeling with a fluorescent dye leads to soft LDI of peptides in the absence of a matrix. The MS/MS spectra were simplified because only a and b rhodamine B-containing peptide fragment ions were observed, which allowed for easy spectral interpretation and de novo sequencing of peptides. In mixtures, the rhodamine B labeled peptides demonstrated a greater ionization efficiency, and therefore selectivity, compared to ionization of the unlabeled peptides. Additionally, FALDI-MS was used to directly analyze beta-amyloid peptides that were N-terminally labeled with the fluorophore HiLyte Fluor™ 555. The described FALDI-MS methodology provides a novel way to ionize and structurally characterize specifically labeled peptides.
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Journal: International Journal of Mass Spectrometry - Volume 353, 1 November 2013, Pages 54–59