Paper
18 January 2005 Study on molecular interactions of bovine serum albumin in electrolyte solutions by dynamic light scattering
Junfeng Li, Da Xing, Shaoxin Li
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Abstract
The concentration dependence of the diffusion coefficient of particles suspended in solution depends primarily on the occupied volume fraction and on repulsive and attractive forces. This dependency is expressed by the interaction parameter λ. In the present work we have measured the diffusion coefficient of Bovine Serum Albumin at different ionic strength and determined the interaction parameter. The results indicate: the value of λ is positive at low ionic strength and the interaction between proteins is repulsive; however, with increasing ionic strength the value of λ becomes negative and the interaction is attractive, and when ionic strength is bigger than 0.50M aggregation occurs. The dependence of the interaction on ionic strength is interpreted using DLVO theory for interactions of two hard spheres: with increasing ionic strength, the repulsive electrostatic interaction is screened and Van der Waals forces become dominant. According to the correlation of λ with ionic strength, the protein parameters are regressed: the protein net charge ZP= -9.0e, Hamaker constant HA= 2.8kBT. This work indicates the technique of dynamic light scattering can be used effectively to study protein molecular interactions.
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Junfeng Li, Da Xing, and Shaoxin Li "Study on molecular interactions of bovine serum albumin in electrolyte solutions by dynamic light scattering", Proc. SPIE 5630, Optics in Health Care and Biomedical Optics: Diagnostics and Treatment II, (18 January 2005); https://doi.org/10.1117/12.572820
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KEYWORDS
Proteins

Diffusion

Dynamic light scattering

Particles

Crystals

Light scattering

Molecular interactions

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