Abstract
Recent studies have shown that N-terminal sulfonation of tryptic peptides by various sulfonating molecules greatly improves their post-source decay processes (e.g., in matrix-assisted laser desorption ionization) or the gas phase fragmentation processes (e.g., in tandem mass spectrometer), enhancing the ability to identify their sequences de novo. In the present work, we have demonstrated that incorporation of water-soluble C60-N,N- dimethylpyrrolidinium iodide selectively precipitates the 4-sulfophenyl isothiocyanate-modified peptide (SPITC-GGYR, SPITC-ASHLGLAR) by forming a noncovalent ion pair to the SO3 - group of the SPITC, and thereby the C60 derivative can be utilized to enrich the modified peptide. Electrospray ionization (ESI) mass analyses show that the cationic SPITC-GGYR and SPITC-ASHLGLAR species are well separated from unmodified peptides and the modified peptides are subsequently detached from the C 60 derivative upon using an acidic solution.
| Original language | English |
|---|---|
| Pages (from-to) | 140-144 |
| Number of pages | 5 |
| Journal | Analytica Chimica Acta |
| Volume | 556 |
| Issue number | 1 |
| DOIs | |
| Publication status | Published - 2006 Jan 18 |
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Keywords
- De novo peptide sequencing
- Liquid chromatography
- N-terminal sulfonation
- Tandem mass spectrometry
- Water-soluble fullerene derivative
ASJC Scopus subject areas
- Biochemistry
- Analytical Chemistry
- Spectroscopy
- Environmental Chemistry
Cite this
Enrichment of N-terminal sulfonated peptides by a water-soluble fullerene derivative and its applications to highly efficient proteomics. / Lee, Yong Ho; Shin, Joong Won; Ryu, Seungwan; Lee, Sang Won; Lee, Chang Hoon; Lee, Kwangyeol.
In: Analytica Chimica Acta, Vol. 556, No. 1, 18.01.2006, p. 140-144.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Enrichment of N-terminal sulfonated peptides by a water-soluble fullerene derivative and its applications to highly efficient proteomics
AU - Lee, Yong Ho
AU - Shin, Joong Won
AU - Ryu, Seungwan
AU - Lee, Sang Won
AU - Lee, Chang Hoon
AU - Lee, Kwangyeol
PY - 2006/1/18
Y1 - 2006/1/18
N2 - Recent studies have shown that N-terminal sulfonation of tryptic peptides by various sulfonating molecules greatly improves their post-source decay processes (e.g., in matrix-assisted laser desorption ionization) or the gas phase fragmentation processes (e.g., in tandem mass spectrometer), enhancing the ability to identify their sequences de novo. In the present work, we have demonstrated that incorporation of water-soluble C60-N,N- dimethylpyrrolidinium iodide selectively precipitates the 4-sulfophenyl isothiocyanate-modified peptide (SPITC-GGYR, SPITC-ASHLGLAR) by forming a noncovalent ion pair to the SO3 - group of the SPITC, and thereby the C60 derivative can be utilized to enrich the modified peptide. Electrospray ionization (ESI) mass analyses show that the cationic SPITC-GGYR and SPITC-ASHLGLAR species are well separated from unmodified peptides and the modified peptides are subsequently detached from the C 60 derivative upon using an acidic solution.
AB - Recent studies have shown that N-terminal sulfonation of tryptic peptides by various sulfonating molecules greatly improves their post-source decay processes (e.g., in matrix-assisted laser desorption ionization) or the gas phase fragmentation processes (e.g., in tandem mass spectrometer), enhancing the ability to identify their sequences de novo. In the present work, we have demonstrated that incorporation of water-soluble C60-N,N- dimethylpyrrolidinium iodide selectively precipitates the 4-sulfophenyl isothiocyanate-modified peptide (SPITC-GGYR, SPITC-ASHLGLAR) by forming a noncovalent ion pair to the SO3 - group of the SPITC, and thereby the C60 derivative can be utilized to enrich the modified peptide. Electrospray ionization (ESI) mass analyses show that the cationic SPITC-GGYR and SPITC-ASHLGLAR species are well separated from unmodified peptides and the modified peptides are subsequently detached from the C 60 derivative upon using an acidic solution.
KW - De novo peptide sequencing
KW - Liquid chromatography
KW - N-terminal sulfonation
KW - Tandem mass spectrometry
KW - Water-soluble fullerene derivative
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UR - http://www.scopus.com/inward/citedby.url?scp=29944443752&partnerID=8YFLogxK
U2 - 10.1016/j.aca.2005.06.060
DO - 10.1016/j.aca.2005.06.060
M3 - Article
C2 - 17723340
AN - SCOPUS:29944443752
VL - 556
SP - 140
EP - 144
JO - Analytica Chimica Acta
JF - Analytica Chimica Acta
SN - 0003-2670
IS - 1
ER -