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Comparative effects of pH and ionic strength on protein–protein interactions, unfolding, and aggregation for IgG1 antibodies

✍ Scribed by Erinc Sahin; Adeola O. Grillo; Melissa D. Perkins; Christopher J. Roberts

Publisher
John Wiley and Sons
Year
2010
Tongue
English
Weight
418 KB
Volume
99
Category
Article
ISSN
0022-3549

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✦ Synopsis

Changes in protein-protein interactions, protein unfolding, and nonnative aggregation were assessed for a series of human IgG1 antibodies as a function of pH and solution ionic strength (I). Unfolding transitions were characterized with differential scanning calorimetry. Protein-protein interactions were characterized with the apparent second virial coefficient (A 2 ) from light scattering. Aggregation pathways were assessed using size-exclusion chromatography and multi-angle laser light scattering, aggregation kinetics, and structural changes monitored by circular dichroism spectroscopy and thioflavine T (ThT) binding. Ionic strength had relatively minor qualitative effects on unfolding, while pH had large effects for all four antibodies. A 2 was sensitive to both pH and I, and indicated that electrostatic interactions and nonuniform surface-charge distributions were important near neutral pH. Depending on solution pH and I, distinct aggregation pathways were found for each antibody, and these shared similar patterns versus pH, I, and A 2 . Main differences observed across different antibodies included thermal unfolding transitions in DSC and the effects of pH and I on aggregation kinetics and pathways. These correlated strongly with whether aggregates of a given antibody bound ThT, suggesting possible differences with respect to conformational changes and/or regions of the proteins that are structurally involved in stabilizing the aggregates.

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