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@ARTICLE{Pattky:276452,
author = {Pattky, Martin and Nicolardi, Simone and Santiago-Schübel,
Beatrix and Sydes, Daniel and van der Burgt, Yuri E. M. and
Klein, Antonia N. and Jiang, Nan and Mohrlüder, Jeannine
and Hänel, Karen and Kutzsche, Janine and Funke, S. A. and
Willbold, D. and Willbold, S. and Huhn, C.},
title = {{S}tructure characterization of unexpected covalent
{O}-sulfonation and ion-pairing on an extremely hydrophilic
peptide with {CE}-{MS} and {FT}-{ICR}-{MS}},
journal = {Analytical and bioanalytical chemistry},
volume = {407},
number = {22},
issn = {0016-1152},
address = {Berlin},
publisher = {Springer},
reportid = {FZJ-2015-06891},
pages = {6637 - 6655},
year = {2015},
abstract = {In this study, we characterized unexpected side-products in
a commercially synthesized peptide with the sequence
RPRTRLHTHRNR. This so-called peptide D3 was selected by
mirror phage display against low molecular weight
amyloid-β-peptide (Aβ) associated with Alzheimer’s
disease. Capillary electrophoresis (CE) was the method of
choice for structure analysis because the extreme
hydrophilicity of the peptide did not allow reversed-phase
liquid chromatography (RPLC) and hydrophilic interaction
stationary phases (HILIC). CE-MS analysis, applying a
strongly acidic background electrolyte and different
statically adsorbed capillary coatings, provided fast and
efficient analysis and revealed that D3 unexpectedly showed
strong ion-pairing with sulfuric acid. Moreover, covalent
O-sulfonation at one or two threonine residues was
identified as a result of a side reaction during peptide
synthesis, and deamidation was found at either the
asparagine residue or at the C-terminus. In total, more than
10 different species with different m/z values were
observed. Tandem-MS analysis with collision induced
dissociation (CID) using a CE-quadrupole-time-of-flight
(QTOF) setup predominantly resulted in sulfate losses and
did not yield any further characteristic fragment ions at
high collision energies. Therefore, direct infusion Fourier
transform ion cyclotron resonance (FT-ICR) MS was employed
to identify the covalent modification and discriminate
O-sulfonation from possible O-phosphorylation by using an
accurate mass analysis. Electron transfer dissociation (ETD)
was used for the identification of the threonine O-sulfation
sites. In this work, it is shown that the combination of
CE-MS and FT-ICR-MS with ETD fragmentation was essential for
the full characterization of this extremely basic peptide
with labile modifications.},
cin = {ICS-6},
ddc = {540},
cid = {I:(DE-Juel1)ICS-6-20110106},
pnm = {551 - Functional Macromolecules and Complexes (POF3-551)},
pid = {G:(DE-HGF)POF3-551},
typ = {PUB:(DE-HGF)16},
UT = {WOS:000360220800009},
pubmed = {pmid:26123437},
doi = {10.1007/s00216-015-8826-8},
url = {https://juser.fz-juelich.de/record/276452},
}