Glycosylation characterization of therapeutic mAbs by top- and middle-down mass spectrometry

Bao Quoc Tran; Christopher Barton; Jinhua Feng; Aimee Sandjong; Sung Hwan Yoon; Shivangi Awasthi; Tao Liang; Mohd M. Khan; David P.A. Kilgour; David R. Goodlett; Young Ah Goo

doi:10.1016/j.dib.2015.11.031

Glycosylation characterization of therapeutic mAbs by top- and middle-down mass spectrometry

Bao Quoc Tran, Christopher Barton, Jinhua Feng, Aimee Sandjong, Sung Hwan Yoon, Shivangi Awasthi, Tao Liang, Mohd M. Khan, David P.A. Kilgour, David R. Goodlett, Young Ah Goo

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14 Scopus citations

Abstract

A reference monoclonal antibody IgG1 and a fusion IgG protein were analyzed by top- and middle-down mass spectrometry with multiple fragmentation techniques including electron transfer dissociation (ETD) and matrix-assisted laser desorption ionization in-source decay (MALDI-ISD) to investigate heterogeneity of glycosylated protein species. Specifically, glycan structure, sites, relative abundance levels, and termini structural conformation were investigated by use of Fourier transform ion cyclotron resonance (FT-ICR) or high performance liquid chromatography electrospray ionization (HPLC-ESI) linked to an Orbitrap. Incorporating a limited enzymatic digestion by immunoglobulin G-degrading enzyme Streptococcus pyogenes (IdeS) with MALDI-ISD analysis extended sequence coverage of the internal region of the proteins without pre-fractionation. The data in this article is associated with the research article published in Journal of Proteomics (Tran et al., 2015) [1].

Original language	English
Pages (from-to)	68-76
Number of pages	9
Journal	Data in Brief
Volume	6
DOIs	https://doi.org/10.1016/j.dib.2015.11.031
State	Published - Mar 1 2016

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10.1016/j.dib.2015.11.031

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@article{1e26e4d13e6345ba894e46cd87e02126,

title = "Glycosylation characterization of therapeutic mAbs by top- and middle-down mass spectrometry",

abstract = "A reference monoclonal antibody IgG1 and a fusion IgG protein were analyzed by top- and middle-down mass spectrometry with multiple fragmentation techniques including electron transfer dissociation (ETD) and matrix-assisted laser desorption ionization in-source decay (MALDI-ISD) to investigate heterogeneity of glycosylated protein species. Specifically, glycan structure, sites, relative abundance levels, and termini structural conformation were investigated by use of Fourier transform ion cyclotron resonance (FT-ICR) or high performance liquid chromatography electrospray ionization (HPLC-ESI) linked to an Orbitrap. Incorporating a limited enzymatic digestion by immunoglobulin G-degrading enzyme Streptococcus pyogenes (IdeS) with MALDI-ISD analysis extended sequence coverage of the internal region of the proteins without pre-fractionation. The data in this article is associated with the research article published in Journal of Proteomics (Tran et al., 2015) [1].",

author = "Tran, {Bao Quoc} and Christopher Barton and Jinhua Feng and Aimee Sandjong and Yoon, {Sung Hwan} and Shivangi Awasthi and Tao Liang and Khan, {Mohd M.} and Kilgour, {David P.A.} and Goodlett, {David R.} and Goo, {Young Ah}",

note = "Funding Information: The data collection was supported in part by collaborative grant from MedImmune, LLC ( 2014-2312 RSA ), and University of Maryland, Baltimore, School of Pharmacy Mass Spectrometry Center ( SOP1841-IQB2014 ). Publisher Copyright: {\textcopyright} 2015.",

year = "2016",

month = mar,

day = "1",

doi = "10.1016/j.dib.2015.11.031",

language = "English",

volume = "6",

pages = "68--76",

journal = "Data in Brief",

issn = "2352-3409",

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T1 - Glycosylation characterization of therapeutic mAbs by top- and middle-down mass spectrometry

AU - Tran, Bao Quoc

AU - Barton, Christopher

AU - Feng, Jinhua

AU - Sandjong, Aimee

AU - Yoon, Sung Hwan

AU - Awasthi, Shivangi

AU - Liang, Tao

AU - Khan, Mohd M.

AU - Kilgour, David P.A.

AU - Goodlett, David R.

AU - Goo, Young Ah

N1 - Funding Information: The data collection was supported in part by collaborative grant from MedImmune, LLC ( 2014-2312 RSA ), and University of Maryland, Baltimore, School of Pharmacy Mass Spectrometry Center ( SOP1841-IQB2014 ). Publisher Copyright: © 2015.

PY - 2016/3/1

Y1 - 2016/3/1

N2 - A reference monoclonal antibody IgG1 and a fusion IgG protein were analyzed by top- and middle-down mass spectrometry with multiple fragmentation techniques including electron transfer dissociation (ETD) and matrix-assisted laser desorption ionization in-source decay (MALDI-ISD) to investigate heterogeneity of glycosylated protein species. Specifically, glycan structure, sites, relative abundance levels, and termini structural conformation were investigated by use of Fourier transform ion cyclotron resonance (FT-ICR) or high performance liquid chromatography electrospray ionization (HPLC-ESI) linked to an Orbitrap. Incorporating a limited enzymatic digestion by immunoglobulin G-degrading enzyme Streptococcus pyogenes (IdeS) with MALDI-ISD analysis extended sequence coverage of the internal region of the proteins without pre-fractionation. The data in this article is associated with the research article published in Journal of Proteomics (Tran et al., 2015) [1].

AB - A reference monoclonal antibody IgG1 and a fusion IgG protein were analyzed by top- and middle-down mass spectrometry with multiple fragmentation techniques including electron transfer dissociation (ETD) and matrix-assisted laser desorption ionization in-source decay (MALDI-ISD) to investigate heterogeneity of glycosylated protein species. Specifically, glycan structure, sites, relative abundance levels, and termini structural conformation were investigated by use of Fourier transform ion cyclotron resonance (FT-ICR) or high performance liquid chromatography electrospray ionization (HPLC-ESI) linked to an Orbitrap. Incorporating a limited enzymatic digestion by immunoglobulin G-degrading enzyme Streptococcus pyogenes (IdeS) with MALDI-ISD analysis extended sequence coverage of the internal region of the proteins without pre-fractionation. The data in this article is associated with the research article published in Journal of Proteomics (Tran et al., 2015) [1].

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DO - 10.1016/j.dib.2015.11.031

M3 - Article

AN - SCOPUS:84949009539

SN - 2352-3409

VL - 6

SP - 68

EP - 76

JO - Data in Brief

JF - Data in Brief

ER -

Glycosylation characterization of therapeutic mAbs by top- and middle-down mass spectrometry

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