Proteomics

Dataset Information

0

O-Glycoproteomic Analysis of Engineered Heavily-Glycosylated Fusion Proteins using NanoHILIC-MS


ABSTRACT: In this study, we identified and quantified the relative glycan distribution on UTI-Fc using nanoHILIC-MS for comprehensive mapping O-glycopeptides in UTI-Fc fusion protein. We quantified O-glycosylated peptides in the Fab domain and describe in detail for the first-time unexpected O-glycosylation at the linker and Fc region in UTI-Fc. These results highlight the improved performance of nanoHILIC-MS for characterization of biotherapeutic protein glycosylation in comparison to RP nanoLC-MS methods.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Gustavo Cavallero  

LAB HEAD: Gustavo Cavallero

PROVIDER: PXD033645 | Pride | 2023-03-11

REPOSITORIES: pride

Dataset's files

Source:
Action DRS
Bikunin0.mzML Mzml
Bikunin0.raw Raw
bikunin02.mzML Mzml
bikunin02.raw Raw
oglcopeptidos_at_Bikunin0__1_1.analysis.db Other
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Publications

O-Glycoproteomic analysis of engineered heavily glycosylated fusion proteins using nanoHILIC-MS.

Cavallero Gustavo J GJ   Wang Yan Y   Nwosu Charles C   Gu Sheng S   Meiyappan Muthuraman M   Zaia Joseph J  

Analytical and bioanalytical chemistry 20220922 27


Recombinant protein engineering design affects therapeutic properties including protein efficacy, safety, and immunogenicity. Importantly, glycosylation modulates glycoprotein therapeutic pharmacokinetics, pharmacodynamics, and effector functions. Furthermore, the development of fusion proteins requires in-depth characterization of the protein integrity and its glycosylation to evaluate their critical quality attributes. Fc-fusion proteins can be modified by complex glycosylation on the active p  ...[more]

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