Determination of the short-time self-diffusion of antibodies approaching an arrested state
We submit this proposal to college 9 due to the fundamental soft-matter nature of our approach. We replied in the text to the comments from the previous round. An important part of the immune response of mammals relies on proteins, immunoglobulins (Igs), serving as antibodies. Igs are also used at high doses, and sometimes formulated at high concentrations to treat immunodeficiencies, autoimmune diseases and other conditions. At high concentrations, however, the viscosity of Igs increases significantly, posing a challenge to clinical administration. Modifying protein-protein interactions, influencing the viscosity, may also render the solution unstable at low storage temperatures and cause aggregation and liquid-liquid phase-separation (LLPS). We propose to profit from the unique capability of IN16B to record inelastic fixed window scans to perform a real-time study of the dynamics of Igs in aqueous solution with polyethylene glycol (PEG), the presence of which modifies protein-protein interactions and can lead to an arrested LLPS state upon cooling to common storage temperatures. We will combine the neutron spectroscopy data with complementary small-angle scattering data.
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MATSARSKAIA Olga; BAEUERLE Famke; BECK Christian; DA VELA Stefano; GIRELLI Anita; GRIMALDO Marco; ROOSEN RUNGE Felix; Frank Schreiber; SEYDEL Tilo and ZHANG Fajun. (2020). Determination of the short-time self-diffusion of antibodies approaching an arrested state. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.9-13-829
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