Welcome to the Laboratory of 
Analytical Chemistry and Biopolymer Structure Analysis

Prof. Dr Dr h.c. Michael Przybylski


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Analytical Chemistry Laboratory - FTICR-MS  

August 2010

Anniversary Symposium
„Michael Przybylski's contribution to
mass spectrometry in life sciences“

April 25th - 26th 2014





Recent Results and Publications

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


  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)


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


  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)


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


  "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)


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.

  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)


"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

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)


  Elucidation of a plaque-specific epitope β-amyloid (4-10) provides Alzheimer-vaccine lead structure
(J. McLaurin et al.,
Nature Med 2002, 8, 1263;
et al., Biopolymers 2004, 76, 503)



Postal address
University of Konstanz
Department of Chemistry
Laboratory of Analytical Chemistry and Biopolymer Structure Analysis
Universitaetsstrasse 10
78457 Konstanz, Germany

+49 7531 882497
+49 7531 883097
For information please contact Michael Przybylski or Secretariat.


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Stand: 21 11 2012