4.8 Article

Dynamics of Intact Immunoglobulin G Explored by Drift-Tube Ion-Mobility Mass Spectrometry and Molecular Modeling

Journal

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume 53, Issue 30, Pages 7765-7769

Publisher

WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201402863

Keywords

conformation analysis; immunoglobulin G; mass spectrometry; molecular dynamics; protein structures

Funding

  1. MRC Industrial Case Studentship
  2. UCB Pharma
  3. Biotechnology and Biological Sciences Research Council [BB/L002655/1] Funding Source: researchfish
  4. Medical Research Council [1008655] Funding Source: researchfish
  5. BBSRC [BB/L002655/1] Funding Source: UKRI

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Collision cross-sections (CCS) of immunoglobulins G1 and G4 have been determined using linear drift-tube ion-mobility mass spectrometry. Intact antibodies and Fc-hinge fragments present with a larger range of CCS than proteins of comparable size. This is rationalized with MD simulations, which indicate significant in vacuo dynamics between linked folded domains. The IgG4 subclass presents over a wider CCS range than the IgG1 subclass.

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