Antibodies under pressure: A Small-Angle X-ray Scattering study of Immunoglobulin G under high hydrostatic pressure

• Published in: Biophysical chemistry Vol. 231; pp. 45 - 49
• Main Authors: König, Nico, Paulus, Michael, Julius, Karin, Schulze, Julian, Voetz, Matthias, Tolan, Metin
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.12.2017
• Subjects: High hydrostatic pressure (HHP); Immunoglobulin G (IgG) antibody; Small-Angle X-ray Scattering (SAXS); Solution conformation; Stability; High hydrostatic pressure (HHP); Immunoglobulin G (IgG) antibody; Stability; Small-Angle X-ray Scattering (SAXS); Solution conformation
• ISSN: 0301-4622; 1873-4200
• DOI: 10.1016/j.bpc.2017.05.016

In the present work two subclasses of the human antibody Immunoglobulin G (IgG) have been investigated by Small-Angle X-ray Scattering under high hydrostatic pressures up to 5kbar. It is shown that IgG adopts a symmetric T-shape in solution which differs significantly from available crystal structures. Moreover, high-pressure experiments verify the high stability of the IgG molecule. It is not unfolded by hydrostatic pressures of up to 5kbar but a slight increase of the radius of gyration was observed at elevated pressures. [Display omitted] •IgG solution structure differs considerably from available crystal structures.•It withstands pressures of up to 5kbar for at least several seconds.•A symmetrical T-shape is maintained at up to 4kbar.•Experimental data can be reproduced computationally by a single IgG conformation.