How to Characterize Protein Self-Association

Bovine serum albumin (BSA) is a non-glycosylated globular protein found in bovines. Since it is inexpensive and readily accessible, it is widely used in clinical chemistry, immunodiagnostic procedures, and drug delivery.1,2

Image credit: Shutterstock/Raimundo79

Image credit: Shutterstock/Raimundo79

An understanding of the behavior of BSA in solution under various conditions is essential to assess the stability of such systems.

Small Angle X-Ray Scattering (SAXS) data was gathered over a wide range of concentrations on a laboratory instrument to fully understand BSA self-association. The ratio of monomer to dimer in solution was then estimated by fitting SAXS curves to its monomer and dimer crystal structures.

SAXS provides the opportunity to characterize closely related molecules, such as monomer-dimer equilibrium in solution, that are not amenable to most other biophysical characterization techniques.

This application note provides detailed insight into the analysis of SAXS data combined with scattering modeling curve fitting providing valuable insights into the solution state behavior of BSA.

Click here to gain access to the complete application note

References

  1. Rombouts, Ine, Bert Lagrain, Katharina A. Scherf, Marlies A. Lambrecht, Peter Koehler, and Jan 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, no. 1 (2015): 1–12
  2. Karimi, Mahdi, Sajad Bahrami, Soodeh Baghaee Ravari, Parham Sahandi Zangabad, Hamed Mirshekari, Mahnaz Bozorgomid, Somayeh Shahreza, Masume Sori, and Michael R. Hamblin. “Albumin nanostructures as advanced drug delivery systems.” Expert opinion on drug delivery 13, no. 11 (2016): 1609-1623

logo

This information has been sourced, reviewed and adapted from materials provided by Xenocs.

For more information on this source, please visit Xenocs.

Citations

Please use one of the following formats to cite this article in your essay, paper or report:

  • APA

    Xenocs. (2023, March 29). How to Characterize Protein Self-Association. AZoNano. Retrieved on March 03, 2024 from https://www.azonano.com/article.aspx?ArticleID=6286.

  • MLA

    Xenocs. "How to Characterize Protein Self-Association". AZoNano. 03 March 2024. <https://www.azonano.com/article.aspx?ArticleID=6286>.

  • Chicago

    Xenocs. "How to Characterize Protein Self-Association". AZoNano. https://www.azonano.com/article.aspx?ArticleID=6286. (accessed March 03, 2024).

  • Harvard

    Xenocs. 2023. How to Characterize Protein Self-Association. AZoNano, viewed 03 March 2024, https://www.azonano.com/article.aspx?ArticleID=6286.

Ask A Question

Do you have a question you'd like to ask regarding this article?

Leave your feedback
Your comment type
Submit
Azthena logo

AZoM.com powered by Azthena AI

Your AI Assistant finding answers from trusted AZoM content

Your AI Powered Scientific Assistant

Hi, I'm Azthena, you can trust me to find commercial scientific answers from AZoNetwork.com.

A few things you need to know before we start. Please read and accept to continue.

  • Use of “Azthena” is subject to the terms and conditions of use as set out by OpenAI.
  • Content provided on any AZoNetwork sites are subject to the site Terms & Conditions and Privacy Policy.
  • Large Language Models can make mistakes. Consider checking important information.

Great. Ask your question.

While we only use edited and approved content for Azthena answers, it may on occasions provide incorrect responses. Please confirm any data provided with the related suppliers or authors. We do not provide medical advice, if you search for medical information you must always consult a medical professional before acting on any information provided.

Your questions, but not your email details will be shared with OpenAI and retained for 30 days in accordance with their privacy principles.

Please do not ask questions that use sensitive or confidential information.

Read the full Terms & Conditions.