Correlation between the osmotic second virial coefficient and solubility for equine serum albumin and ovalbumin.
Abstract: The Haas - Drenth - Wilson (HDW) (Haas et al., 1999) theoretical model was used to correlate osmotic second virial coefficient (B) values with solubility (S) values for equine serum albumin (ESA) and ovalbumin for corresponding solution conditions. The best fit from the theoretical model was compared to experimental S versus B data. B values were experimentally measured using static light scattering. Solubilities of ESA were estimated using a sitting drop method. When the experimental data for S versus B were plotted, an excellent fit for ESA was obtained according to the HDW model. The results showed that the coordination number (z) in the crystal lattice was 6, and the adjustable parameter (A) was 0.072. For ovalbumin, previously reported solubility data in aqueous ammonium sulfate solutions were utilized. The solubility data for ovalbumin were correlated with the measured B values obtained in our laboratory. The resulting best fit from the HDW model showed that z = 6 and A = 0.084.
Publication Date: 2002-09-26 PubMed ID: 12351858DOI: 10.1107/s0907444902014385Google Scholar: Lookup
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- Journal Article
Summary
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The research paper is a detailed examination of the correlation between the osmotic second virial coefficient and solubility for two proteins, equine serum albumin and ovalbumin, using the Haas – Drenth – Wilson theoretical model.
Overview of the Research
- The study involved the application of the Haas – Drenth – Wilson (HDW) model – a renowned theoretical model developed in 1999. This model was used to investigate the correlation between the osmotic second virial coefficient (commonly denoted as B) and solubility values for two proteins: equine serum albumin (ESA) and ovalbumin.
- The researchers conducted experiments to measure B values using static light scattering, a technique that involves scattering pattern of laser light to collect relevant data.
- The solubility of ESA was estimated using a sitting drop method. This is a commonly used method in protein crystallization that employs a tiny drop of protein in a sitting position on a glass cover slip.
Results and Interpretation
- The results of this study were drawn by plotting the experimental data for solubility (S) versus B. The researchers noted that the best fit derived from the HDW model displayed an excellent match with the experimental data for ESA.
- The coordination number (z) in the crystal lattice was found to be 6, and the adjustable parameter (A) equaled 0.072. In crystallography, the coordination number is the number of immediate neighbours a central particle has. In the context of this research, it helps to understand the molecular bonding and structure as this value indicates how many other atoms a particle can bond with.
- For ovalbumin, the researchers made use of previously reported solubility data in aqueous ammonium sulfate solutions. The researchers correlated the solubility data of ovalbumin with the measured B values obtained in their laboratory. Similar to ESA, the best fit from the HDW model for ovalbumin showed z equal to 6 and A as 0.084.
By delivering these results, the research demonstrated a significant correlation between the osmotic second virial coefficient and solubility for both proteins. This could enhance understanding of protein behaviour in different solution conditions and potentially aid in proteins’ practical application, such as drug development.
Cite This Article
APA
Demoruelle K, Guo B, Kao S, McDonald HM, Nikic DB, Holman SC, Wilson WW.
(2002).
Correlation between the osmotic second virial coefficient and solubility for equine serum albumin and ovalbumin.
Acta Crystallogr D Biol Crystallogr, 58(Pt 10 Pt 1), 1544-1548.
https://doi.org/10.1107/s0907444902014385 Publication
Researcher Affiliations
- Department of Chemistry, Mississippi State University, Box 9573, Mississippi State, MS 39762, USA.
MeSH Terms
- Ammonium Sulfate
- Animals
- Anisotropy
- Crystallization
- Horses
- Light
- Models, Chemical
- Molecular Weight
- Osmosis
- Ovalbumin / chemistry
- Scattering, Radiation
- Serum Albumin / chemistry
- Solubility
Citations
This article has been cited 8 times.- Yadav S, Liu J, Scherer TM, Gokarn Y, Demeule B, Kanai S, Andya JD, Shire SJ. Assessment and significance of protein-protein interactions during development of protein biopharmaceuticals.. Biophys Rev 2013 Jun;5(2):121-136.
- Pande A, Mokhor N, Pande J. Deamidation of Human γS-Crystallin Increases Attractive Protein Interactions: Implications for Cataract.. Biochemistry 2015 Aug 11;54(31):4890-9.
- Johnson DH, Wilson WW, DeLucas LJ. Protein solubilization: a novel approach.. J Chromatogr B Analyt Technol Biomed Life Sci 2014 Nov 15;971:99-106.
- Wilson WW, Delucas LJ. Applications of the second virial coefficient: protein crystallization and solubility.. Acta Crystallogr F Struct Biol Commun 2014 May;70(Pt 5):543-54.
- Salinas BA, Sathish HA, Bishop SM, Harn N, Carpenter JF, Randolph TW. Understanding and modulating opalescence and viscosity in a monoclonal antibody formulation.. J Pharm Sci 2010 Jan;99(1):82-93.
- Johnson DH, Parupudi A, Wilson WW, DeLucas LJ. High-throughput self-interaction chromatography: applications in protein formulation prediction.. Pharm Res 2009 Feb;26(2):296-305.
- Dumetz AC, Chockla AM, Kaler EW, Lenhoff AM. Protein phase behavior in aqueous solutions: crystallization, liquid-liquid phase separation, gels, and aggregates.. Biophys J 2008 Jan 15;94(2):570-83.
- Saluja A, Badkar AV, Zeng DL, Nema S, Kalonia DS. Ultrasonic storage modulus as a novel parameter for analyzing protein-protein interactions in high protein concentration solutions: correlation with static and dynamic light scattering measurements.. Biophys J 2007 Jan 1;92(1):234-44.
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