Using A2 and kD to assess protein interactions in formulations

Two different proteins [Immunoglobulin G IgG and human serum albumin HSA] are measured using a series of static (SLS) and dynamic (DLS) light scattering measurements. The molecular weight, 'true' hydrodynamic diameter, second virial coefficient, and DLS interaction parameter are measured.The results show that both SLS and DLS measurements can be used to study interactions between proteins, as well as simply their molecular weight and hydrodynamic size.  The values of A2 and kD can be seen to change in response to a change in buffer pH.


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