Elucidation of the Reversible Self-Association Interface of a Diabody–Interleukin Fusion Protein Using Hydrogen-Exchange Mass Spectrometry and In Silico Modeling-Reference-Cited by-同舟云学术

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Elucidation of the Reversible Self-Association Interface of a Diabody–Interleukin Fusion Protein Using Hydrogen-Exchange Mass Spectrometry and In Silico Modeling

Published:2024-06-26 Issue:9 Volume:21 Page:4285-4296
ISSN:1543-8384
Container-title:Molecular Pharmaceutics
language:en
Short-container-title:Mol. Pharmaceutics

Author:

Eisinger Martin¹,Rahn Harri¹^ORCID,Chen Yong²,Fernandes Melissa³,Lin Zhiyi³,Hentze Nikolai¹,Tavella Davide⁴,Moussa Ehab M.³^ORCID

Affiliation:

1. Biologics Analytical Research and Development, AbbVie Deutschland GmbH & Co. KG, Ludwigshafen 67061, Germany

2. Biologics Analytical Research and Development, AbbVie Inc., North Chicago, Illinois 60061, United States

3. Biologics Drug Product Development, AbbVie Inc., North Chicago, Illinois 60061, United States

4. Biotherapeutics and Genetic Medicine, AbbVie Inc., Worcester, Massachusetts 01604, United States

Funder

AbbVie

Publisher

American Chemical Society (ACS)

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.molpharmaceut.4c00169

Reference73 articles.

1. Therapeutic antibodies: successes, limitations and hopes for the future

2. Antibody fragments

3. Role of tumor-host interactions in interstitial diffusion of macromolecules: Cranial vs. subcutaneous tumors

4. Engineered antibody fragments and the rise of single domains

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