Version 1
: Received: 4 January 2024 / Approved: 5 January 2024 / Online: 5 January 2024 (10:38:20 CET)
How to cite:
Agbelusi, T.; Pancholi, K.; Sampatk Kumar, H.; Kumar, A. Overcoming CD Spectroscopy Sample Preparation Challenges in Protein Structural Analysis for Biosimilars. Preprints2024, 2024010441. https://doi.org/10.20944/preprints202401.0441.v1
Agbelusi, T.; Pancholi, K.; Sampatk Kumar, H.; Kumar, A. Overcoming CD Spectroscopy Sample Preparation Challenges in Protein Structural Analysis for Biosimilars. Preprints 2024, 2024010441. https://doi.org/10.20944/preprints202401.0441.v1
Agbelusi, T.; Pancholi, K.; Sampatk Kumar, H.; Kumar, A. Overcoming CD Spectroscopy Sample Preparation Challenges in Protein Structural Analysis for Biosimilars. Preprints2024, 2024010441. https://doi.org/10.20944/preprints202401.0441.v1
APA Style
Agbelusi, T., Pancholi, K., Sampatk Kumar, H., & Kumar, A. (2024). Overcoming CD Spectroscopy Sample Preparation Challenges in Protein Structural Analysis for Biosimilars. Preprints. https://doi.org/10.20944/preprints202401.0441.v1
Chicago/Turabian Style
Agbelusi, T., Harini Sampatk Kumar and Amit Kumar. 2024 "Overcoming CD Spectroscopy Sample Preparation Challenges in Protein Structural Analysis for Biosimilars" Preprints. https://doi.org/10.20944/preprints202401.0441.v1
Abstract
Circular dichroism (CD) spectroscopy is a valuable tool in the pharmaceutical industry for determining the secondary and tertiary structure, folding, stability, and interactions of proteins in biosimilars. However, protein aggregation due to its interaction with surfactants can introduce variations in CD spectra, leading to false interpretations. To investigate this effect, we prepared aqueous solutions of α-chymotrypsin with the same amount of surfactant but at different solution preparation steps. Interestingly, the CD spectra of these solutions showed slight differences despite having the same surfactant concentration. This suggests that the order of surfactant addition can influence protein conformation. To address this issue, we propose a method for preparing aqueous protein solutions that yields reproducible CD spectra. This method is expected to benefit the pharmaceutical industry by improving the accuracy of CD spectroscopy for protein structural analysis and evaluation of protein functionality.
Copyright:
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
