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

被引：10
作者：
Koenig, Nico [1 ,2 ,3 ,4 ]
Paulus, Michael [1 ]
Julius, Karin [1 ]
Schulze, Julian [1 ]
Voetz, Matthias [2 ]
Tolan, Metin [1 ]
机构：
[1] TU Dortmund, Falc Phys, DELTA, D-44221 Dortmund, Germany
[2] Bayer AG, D-51368 Leverkusen, Germany
[3] Forschungszentrum Julich, JCNS, D-52425 Julich, Germany
[4] Forschungszentrum Julich, ICS, D-52425 Julich, Germany
来源：
BIOPHYSICAL CHEMISTRY | 2017年 / 231卷
关键词：
Small-Angle X-ray Scattering (SAXS); High hydrostatic pressure (HHP); Immunoglobulin G (IgG) antibody; Stability; Solution conformation; PROTEIN CRYSTALLIZATION; MONOCLONAL-ANTIBODIES; IGG SUBCLASSES; CRYSTAL; MACROMOLECULES; SAXS;
D O I：
10.1016/j.bpc.2017.05.016
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
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 5 kbar. 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 5 kbar but a slight increase of the radius of gyration was observed at elevated pressures.
引用
收藏
页码：45 / 49
页数：5
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