Characterization of protein intermolecular interactions

Bovine serum albumin (BSA) is a non-glycosylated globular protein found in bovines. It is widely used in drug delivery, immunodiagnostic procedures  and in clinical chemistry due to its low cost and readily availability. ^[1,2]

Understanding the behavior of BSA in solution under varying conditions is crucial for assessing the stability of such systems.

To characterize the protein self-interactions, SAXS data were collected for BSA in various pH solutions over a wide range of concentrations on a laboratory instrument.

SAXS enables detailed analysis of intermolecular attraction and repulsion in dilute and in concentrated solutions in near-physiological environments.

SAXS can also monitor the colloidal stability of therapeutic proteins as a function of pH, ionic strength, protein concentration and excipients, protein-ligand interaction, monomer-dimer equilibrium, oligomerization and aggregation.

References:

¹ Rombouts, I., Lagrain, B., Scherf, K. A., Lambrecht, M. A., Koehler, P., & Delcour, J. A. (2015). Formation and reshuffling of disulfide bonds in bovine serum albumin demonstrated using tandem mass spectrometry with collision-induced and electron-transfer dissociation. Scientific reports, 5(1), 1-12.

² Karimi, M., Bahrami, S., Ravari, S.B., Zangabad, P.S., Mirshekari, H., Bozorgomid, M., Shahreza, S., Sori, M. and Hamblin, M.R. (2016). Albumin nanostructures as advanced drug delivery systems. Expert opinion on drug delivery, 13(11), 1609-1623.