Disulfide Analysis

Dr. Anne Zeck
Group Leader Bioanalytics

+49 7121 51530-811

E-Mail

anzeigen

Identification and relative quantification of di- and trisulfide bridges and cysteine modifications

Disulfide bridges stabilize the 3D structure of proteins and covalently link protein subunits. Proper folding and assembly of protein subunits are essential for the secretion of functional proteins from cells, as opposed to misfolding, accelerated degradation or inactivity. We offer determination and localization of disulfide pairings, covalent cysteine modifications and free cysteines.

Our services

• Localisation of the disulfide linkage
• Identification and relative quantification of free sulfhydryl groups
• Identification of trisulfide linkages, glutathionylation, cysteinylation and homocysteinylation

Methods

• LC
• MS
• Peptide Mapping
• ES-MS
• ES-MS/MS

Publications

• Seibel R, Maier S, Schnellbaecher A, Bohl S, Wehsling M, Zeck A, Zimmer A. Impact of S-sulfocysteine on fragments and trisulfide bond linkages in monoclonal antibodies. MAbs. 2017 Aug/Sep;9(6):889-897. doi: 10.1080/19420862.2017.1333212. Epub 2017 Jun 5. PMID: 28581887; PMCID: PMC5540110.
• Prade E, Zeck A, Stiefel F, Unsoeld A, Mentrup D, Arango Gutierrez E, Gorr IH. Cysteine in cell culture media induces acidic IgG1 species by disrupting the disulfide bond network. Biotechnol Bioeng. 2021 Mar;118(3):1091-1104. doi: 10.1002/bit.27628. Epub 2020 Dec 16. PMID: 33200817; PMCID: PMC7986432.