SAXS was used to study the effect of pH and protein concentration on the self-interaction process of a BSA system in solution
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 I. Rombouts, B. Lagrain, K.-A. Scherf, M.-A.Lambrecht, P. Koehler, and J.-A. Delcour. 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, 12210. (2015) DOI: 10.1038/srep12210.
2 M. Karimi, S. Bahrami, S.-B.Ravari, P.-S. Zangabad, H. Mirshekari, M. Bozorgomid, S. Shahreza, M. Soriand, M-R. Hamblin. Albumin nanostructures as advanced drug delivery systems. Expert opinion on drug delivery 13. (2016) DOI: 10.1080/17425247.2016.1193149
