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Introduced more than fifty years ago, dynamic light scattering is routinelyused to determine the size distribution of colloidal suspensions, as well as ofmacromolecules in solution, such as proteins, nucleic acids, and theircomplexes. More recently, differential dynamic microscopy has been proposed asa way to perform dynamic light scattering experiments with a microscope, withmuch less stringent constraints in terms of cleanliness of the opticalsurfaces, but a potentially lower sensitivity due to the use of camera-baseddetectors. In this work, we push bright-field differential dynamic microscopybeyond known limits and show it to be sufficiently sensitive to size smallmacromolecules in diluted solutions. By considering solutions of threedifferent proteins (Bovine Serum Albumin, Lysozyme, and Pepsin), we accuratelydetermine the diffusion coefficient and hydrodynamic radius of both singleproteins and small protein aggregates down to concentrations of a fewmilligrams per milliliter. In addition, we present preliminary results showingunexplored potential for the determination of virial coefficients. Our resultsare in excellent agreement with the ones obtained in parallel with astate-of-the-art commercial dynamic light scattering setup, showing thatdifferential dynamic microscopy represents a valuable alternative for rapid,label-free protein sizing with an optical microscope.

Protein sizing with Differential Dynamic Microscopy