Monoclonal antibodies (mAb) are a rapidly growing group of biopharmaceuticals. Due to their intrinsic flexibility, intact mAbs provide a challenge with regards to higher order structure characterization. Intact mAbs and their fragments are explored here using the DT-IM-MS and were found to be far more dynamic in the gas-phase than proteins of comparable size. This is rationalised with MD simulations, which revealed dynamics between linked folded domains of mAbs.
Signature dynamics of intact immunoglobulin G revealed by drift-tube ion-mobility mass spectrometry and molecular modeling
Kamila J. Pacholarz, Massimiliano Porrini, Rachel A. Garlish, Richard J. Taylor, Alistair J. Henry, and Perdita E. Barran