IgG Antibody 3D Structures and Dynamics

Jay, Jacob; Bray, Brinkley; Qi, Yaozhi; Igbinigie, Eseosaserea; Wu, Hao; Li, Jinping; Ren, Gang

doi:10.3390/antib7020018

IgG Antibody 3D Structures and Dynamics

Journal Article · Thu Apr 19 00:00:00 EDT 2018 · Antibodies

DOI:https://doi.org/10.3390/antib7020018· OSTI ID:1629230

Jay, Jacob ^[1]; Bray, Brinkley ^[2]; Qi, Yaozhi ^[3]; Igbinigie, Eseosaserea ^[2]; Wu, Hao ^[4]; Li, Jinping ^[2]; ^[5]

Mercer University School of Medicine, Savannah, GA (United States). Dept. of Biomedical Sciences; DOE/OSTI
Mercer University School of Medicine, Savannah, GA (United States). Dept. of Biomedical Sciences
Mercer University School of Medicine, Savannah, GA (United States). Dept. of Biomedical Sciences; Department of Clinical Laboratory, Lianyungang Maternal and Child Health Hospital, Lianyungang, China
College of Information Science and Technology, Beijing Normal University, Beijing, China
Lawrence Berkeley National Lab (LBNL), Berkeley, CA (United States). The Molecular Foundry

Antibodies are vital for human health because of their ability to function as nature’s drugs by protecting the body from infection. In recent decades, antibodies have been used as pharmaceutics for targeted therapy in patients with cancer, autoimmune diseases, and cardiovascular diseases. Capturing the dynamic structure of antibodies and characterizing antibody fluctuation is critical for gaining a deeper understanding of their structural characteristics and for improving drug development. Current techniques for studying three-dimensional (3D) structural heterogeneity and variability of proteins have limitations in ascertaining the dynamic structural behavior of antibodies and antibody-antigen complexes. Here, we review current techniques used to study antibody structures with a focus on the recently developed individual-particle electron tomography (IPET) technique. IPET, as a particle-by-particle methodology for 3D structural characterization, has shown advantages in studying structural variety and conformational changes of antibodies, providing direct imaging data for biomolecular engineering to improve development and clinical application of synthetic antibodies.

View Accepted Manuscript (DOE)

Research Organization:: Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States)

Sponsoring Organization:: National Institutes of Health (NIH), National Heart, Lung and Blood Institute; USDOE/Office of Science (SC), Office of Basic Energy Sciences (BES)

Grant/Contract Number:: AC02-05CH11231

OSTI ID:: 1629230

Journal Information:: Antibodies, Journal Name: Antibodies Journal Issue: 2 Vol. 7; ISSN 2073-4468; ISSN ANTICA

Country of Publication:: United States

Language:: English

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