Analytical Chemistry Laboratory - FTICR-MS
August 2010
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Recent Results and Publications
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Autoproteolytic fragments are intermediates in the oligomerization/aggregation of the Parkinson's disease protein alpha-synuclein as revealed by ion mobility mass spectrometry.
(Vlad C et al., ChemBioChem 2011
12(18) 2740-2744
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Toward Bioinspired Galectin Mimetics: Identification of Ligand-Contacting Peptides by Proteolytic-Excision Mass Spectrometry.
(Moise A et al.,
2011
J. Am. Chem. Soc.
133(38) 14844-14847)
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An online biosensor-electrospray-mass spectroemtry interface has been developed for the direct structural identification and
affinity quantification of biomolecular ligand interactions, such as polypeptide-antigen- antibody. The interface, described here for an SAW-biosensor, is equally
feasble with other biosensors, such as QCM or SPR.
On-line bioaffinity-electrospray mass spectrometry for simultaneous detection,
identification, and quantification of protein-ligand interactions.
(Dragusanu M. et al., J. Am. Soc. Mass Spectrom. 2010
21 1643-1648
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Structural characterization of beta-amyloid oligomer-aggregates by
ion mobility mass spectrometry and electron spin resonance spectroscopy.
(Iurascu MI et al.,
Anal. Bioanal. Chem. 2010
395, 2509-2519)
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Functional ubiquitin conjugates with lysine-epsilon-amino-specific linkage
by thioether ligation of cysteinyl-ubiquitin peptide building blocks.
(Jung JE et al., Bioconj. Chem. 2009
20 1152-1162
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"Unknown genome" proteomics: a new NADP-dependent epimerase/dehydratase revealed by
N-terminal sequencing, inverted PCR, and high resolution mass spectrometry.
(Simeonova DD, Susnea I et al.,
Mol Cell Proteomics 2009
8(1), 122-131)
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Elucidation of O-Glycosylation Structures of the Aß-Amyloid Precursor
Protein by Liquid Chromatography-Mass Spectrometry Using
Electron Transfer Dissociation and Collision Induced Dissociation
(Perdivara I. et al., J. Proteome Res
8 (2) 631-642
Three specific O-glycosylation sites of the secreted APP695 (sAPP695)
produced in CHO cells have been identified using a combination of high-performance liquid
chromatography and electrospray-tandem mass spectrometry,
with electron transfer
dissociation and collision induced dissociation (ETD and CID).
The glycosylations comprise multiple short glycans, containing N-acetyl galactosamine (GalNAc),
Gal-GalNAc and sialic acid terminated structures.
The combination of the CID and ETD techniques in LC-MS is shown as a powerful
tool for de novo identification of O-glycosylations at unknown modification
sites in proteins.
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Binding Epitopes and Interaction Structure of the Neuroprotective Protease Inhibitor Cystatin
C with ß-Amyloid Revealed by Proteolytic Excision Mass Spectrometry and Molecular Docking
Simulation
(Juszczyk P. et al.,
J. Med. Chem. 2009
52, 2420–2428)
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"Peptidbody" Design:
Functional single-chain peptide anti-lysozyme antibody,
revealed by high-resolution affinity - mass spectrometry
(A. Marquardt et al., Chemistry 2006 12(7): 1915-1923
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Proteolytic specificity
of serine protease HtrA1 & implications for amyloid
precursor protein (APP) processing revealed by
FTICR-MS
(S. Grau et
al., Proc Natl Acad Sci USA 2005,
102(17),
6021) |
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Elucidation of a
plaque-specific epitope β-amyloid (4-10) provides
Alzheimer-vaccine lead structure
(J. McLaurin et al., Nature Med 2002, 8, 1263;
M.
Manea
et
al., Biopolymers 2004, 76,
503) |
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