Differential glycosylation does not modulate the conformational heterogeneity of a humanised IgGk NIST monoclonal antibody-Reference-Cited by-同舟云学术

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Differential glycosylation does not modulate the conformational heterogeneity of a humanised IgGk NIST monoclonal antibody

Published:2024 Issue: Volume: Page:
ISSN:1359-7345
Container-title:Chemical Communications
language:en
Short-container-title:Chem. Commun.

Author:

Liu Fanny C.¹^ORCID,Lee Jusung¹^ORCID,Pedrete Thais¹^ORCID,Panczyk Erin M.²^ORCID,Pengelley Stuart³^ORCID,Bleiholder Christian¹⁴^ORCID

Affiliation:

1. Department of Chemistry and Biochemistry, Florida State University, 102 Varsity Way, Tallahassee, Florida, 32306, USA

2. Bruker Daltonics, 40 Manning Road, Billerica, MA 01821, USA

3. Bruker Daltonics GmbH&Co, Fahrenheitstrasse 4, Bremen, 28359, Germany

4. Institute of Molecular Biophysics, Florida State University, 91 Chieftan Way, Tallahassee, Florida, 32306, USA

Abstract

Tandem ion mobility spectrometry reveals that glycosylation does not alter the conformational heterogeneity of a monoclonal antibody.

Funder

National Institute of General Medical Sciences

Division of Chemistry

Publisher

Royal Society of Chemistry (RSC)

Link

http://pubs.rsc.org/en/content/articlepdf/2024/CC/D4CC02125H

Reference30 articles.

1. Ensembles in solution as a new paradigm for antibody structure prediction and design

2. CDR-H3 loop ensemble in solution – conformational selection upon antibody binding

3. A broad range of Fab stabilities within a host of therapeutic IgGs

4. NMR of glycoproteins: profiling, structure, conformation and interactions

5. Evidence for Macromolecular Protein Rings in the Absence of Bulk Water

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