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Updated: May 22, 2025

Purification and Aggregation of the Amyloid Precursor Protein Intracellular Domain
Published on: August 28, 2012
IgG4 and IgG1 undergo common acid-induced compaction into an alternatively folded state
Hiroshi Imamura1, Shinya Honda2
1Department of Biological Data Science, Nagahama Institute of Bio-Science and Technology, Japan.
Abstract:
Immunoglobulin G1 (IgG1) antibodies undergo denaturation in acidic conditions, resulting in an alternatively folded state (AFS). The AFS structure is more compact than the native state. However, the prevalence of AFS in other subclasses remains largely unexplored. This study provides evidence that humanized IgG4 can also adopt the AFS structure, as demonstrated through size-exclusion chromatography coupled with small-angle X-ray scattering (SEC-SAXS) analysis. These findings suggest that the anomalous compaction of immunoglobulins G (IgGs) is resilient to variations in sequence and structure among subclasses.
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