Skip to main content
U.S. flag

An official website of the United States government

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you’ve safely connected to the .gov website. Share sensitive information only on official, secure websites.

Dataset from HDX-MS Studies of IgG1 Glycoforms and Their Interactions with the FcγR1a (CD64) Receptor



Kyle Anderson, Kerry Scott, Ioannis Karageorgos, Elyssia Gallagher, Venkata Tayi, Michael Butler, Jeffrey W. Hudgens


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.
Journal of Research (NIST JRES) -


antibody-receptor interaction, chromatography, hydrogen-deuterium exchange, glycosylation, mass spectrometry, monoclonal antibody, precision, peptide, protein, proteolysis, proteomics, receptor.


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],, (Accessed April 14, 2024)
Created June 17, 2021, Updated November 29, 2022