Anderson, K.
, Scott, K.
, Karageorgos, I.
, Gallagher, E.
, Tayi, V.
, Butler, M.
and Hudgens, J.
(2021),
Dataset from HDX-MS Studies of IgG1 Glycoforms and Their Interactions with the FcγR1a (CD64) Receptor, Journal of Research (NIST JRES), National Institute of Standards and Technology, Gaithersburg, MD, [online], https://doi.org/10.6028/jres.126.010, https://tsapps.nist.gov/publication/get_pdf.cfm?pub_id=931995
(Accessed April 18, 2024)
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Dataset from HDX-MS Studies of IgG1 Glycoforms and Their Interactions with the FcγR1a (CD64) Receptor
Published
Author(s)
, Kerry Scott, , Elyssia Gallagher, Venkata Tayi, Michael Butler,
Abstract
This database gives hydrogen-deuterium exchange mass spectrometry (HDX-MS) data from measurements of three purified IgG1 glycoform samples, predominantly G0F, G2F, and SAF, in isolation and in complexation with the high-affinity receptor, FcγR1a (CD64). The IgG1 antibody used in this study, aIL8hFc, is a murine-human chimeric IgG1, which inhibits IL-8 binding to human neutrophils. The working datasets comprise 17,750 deuterium uptake measurements in peptides from the receptor and the light and heavy chains of aIL8hFc obtained during 7 experiments, each comprising three runs of six exchange times. The data illuminate on the hydrogen exchange dynamics in isolated receptor, isolated IgG1 glycoforms, and receptor-IgG1 complexes.Citation
Journal of Research (NIST JRES) -
Volume
126
NIST Pub Series
Pub Type
NIST Pubs
Download Paper
Keywords
antibody-receptor interaction, chromatography, hydrogen-deuterium exchange, glycosylation, mass spectrometry, monoclonal antibody, precision, peptide, protein, proteolysis, proteomics, receptor.
Citation
Created June 17, 2021, Updated November 29, 2022