Ion Mobility-Mass Spectrometry and Collision-Induced Unfolding Rapidly Characterize the Structural Polydispersity and Stability of an Fc-Fusion Protein-Reference-Cited by-同舟云学术

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Ion Mobility-Mass Spectrometry and Collision-Induced Unfolding Rapidly Characterize the Structural Polydispersity and Stability of an Fc-Fusion Protein

Published:2024-06-10 Issue:24 Volume:96 Page:10003-10012
ISSN:0003-2700
Container-title:Analytical Chemistry
language:en
Short-container-title:Anal. Chem.

Author:

Villafuerte-Vega Rosendo C.¹,Li Henry W.¹,Bergman Addison E.¹,Slaney Thomas R.²^ORCID,Chennamsetty Naresh²,Chen Guodong²,Tao Li²^ORCID,Ruotolo Brandon T.¹^ORCID

Affiliation:

1. Department of Chemistry, University of Michigan, Ann Arbor, Michigan 48109, United States

2. Analytical Development and Attribute Sciences, Biologics Development, Global Product Development and Supply, Bristol Myers Squibb, New Brunswick, New Jersey 08903, United States

Funder

University of Michigan

Division of Molecular and Cellular Biosciences

Bristol-Myers Squibb

National Science Foundation

Publisher

American Chemical Society (ACS)

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.analchem.4c01408

Reference74 articles.

1. Rilonacept

2. Luspatercept in Patients with Lower-Risk Myelodysplastic Syndromes

3. Fusion proteins for treatment of retinal diseases: aflibercept, ziv-aflibercept, and conbercept

4. Fc‐fusion proteins: new developments and future perspectives

5. Engineering protein-based therapeutics through structural and chemical design

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