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Measurement of Secondary Structure Changes in Poly-L-lysine and Lysozyme during Acoustically Levitated Single Droplet
Julian F A Perlitz1,2, Lukas Gentner1, Phillipp A B Braeuer1,2
1Lehrstuhl für Technische Thermodynamik (LTT), Friedrich-Alexander-Universität Erlangen-Nürnberg (FAU), D-91058 Erlangen, Germany.
Sensors (Basel, Switzerland)
|February 15, 2022
Summary
Investigating protein drying, this study developed a novel Raman spectroscopy method to monitor structural changes in single levitated droplets. The findings reveal temperature-dependent alterations in protein secondary structures during drying, crucial for pharmaceutical applications.
Area of Science:
- Biophysical Chemistry
- Spectroscopy
- Pharmaceutical Technology
Background:
- Drying processes like spray drying can denature proteins, reducing drug efficacy.
- In situ monitoring of protein structural changes during drying is challenging due to process conditions.
Purpose of the Study:
- To develop and demonstrate an in situ method for investigating protein secondary structure changes during single droplet drying.
- To quantify structural alterations in model proteins (poly-L-lysine and lysozyme) during drying.
Main Methods:
- Utilized an acoustic levitator to suspend single solution droplets.
- Employed time-resolved Raman spectroscopy with a custom NIR-Raman sensor for in situ measurements.
- Applied mathematical spectral reconstruction (multiple Voigt functions) to quantify secondary structure changes.
Main Results:
- Successfully detected and quantified relative secondary structure changes during single droplet drying.
- Observed an increase in β-sheet structure and a decrease in α-helix and random coil structures.
- Demonstrated that higher temperatures exacerbate protein structural changes during drying.
Conclusions:
- The developed Raman spectroscopy approach enables real-time monitoring of protein structural dynamics during drying.
- Understanding these drying-induced structural changes is vital for preserving protein activity in pharmaceutical formulations.
- Temperature is a critical factor influencing protein structural stability during drying.
