Resolving molecular diffusion and aggregation of antibody proteins with megahertz X-ray free-electron laser pulses

Author:

Reiser MarioORCID,Girelli Anita,Ragulskaya Anastasia,Das Sudipta,Berkowicz Sharon,Bin MaddalenaORCID,Ladd-Parada MarjorieORCID,Filianina MariiaORCID,Poggemann Hanna-Friederike,Begam Nafisa,Akhundzadeh Mohammad Sayed,Timmermann SonjaORCID,Randolph LisaORCID,Chushkin Yuriy,Seydel TiloORCID,Boesenberg Ulrike,Hallmann Jörg,Möller Johannes,Rodriguez-Fernandez AngelORCID,Rosca RobertORCID,Schaffer Robert,Scholz MarkusORCID,Shayduk Roman,Zozulya AlexeyORCID,Madsen AndersORCID,Schreiber FrankORCID,Zhang Fajun,Perakis FivosORCID,Gutt ChristianORCID

Abstract

AbstractX-ray free-electron lasers (XFELs) with megahertz repetition rate can provide novel insights into structural dynamics of biological macromolecule solutions. However, very high dose rates can lead to beam-induced dynamics and structural changes due to radiation damage. Here, we probe the dynamics of dense antibody protein (Ig-PEG) solutions using megahertz X-ray photon correlation spectroscopy (MHz-XPCS) at the European XFEL. By varying the total dose and dose rate, we identify a regime for measuring the motion of proteins in their first coordination shell, quantify XFEL-induced effects such as driven motion, and map out the extent of agglomeration dynamics. The results indicate that for average dose rates below 1.06 kGy μs−1 in a time window up to 10 μs, it is possible to capture the protein dynamics before the onset of beam induced aggregation. We refer to this approach as correlation before aggregation and demonstrate that MHz-XPCS bridges an important spatio-temporal gap in measurement techniques for biological samples.

Publisher

Springer Science and Business Media LLC

Subject

General Physics and Astronomy,General Biochemistry, Genetics and Molecular Biology,General Chemistry,Multidisciplinary

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