https://doi.org/10.1051/epjconf/202430904022
Side-scattering spectroscopy of biological aggregates
1 Center for Life Nano- and Neuro-Science, Istituto Italiano di Tecnologia, Viale Regina Elena 291, 00161, Rome, Italy
2 D-TAILS srl, Via di Torre Rossa, 66, 00165, Rome, Italy
3 Department of Biochemical Sciences “Alessandro Rossi Fanelli”, Sapienza University of Rome, P.le A. Moro 5, 00185 Rome, Italy
4 Department of Physics, Sapienza University of Rome, Piazzale Aldo Moro, 5, 00185, Rome, Italy
5 Institute of Nanotechnology of the National Research Council of Italy, CNR-NANOTEC, Rome Unit, Piazzale A. Moro 5, I-00185, Rome, Italy
* Corresponding author: zita.salajkova@iit.it
Published online: 31 October 2024
In this study, we introduce a novel optical setup tailored for measuring scattering spectra of small biological aggregates with minimal sample volumes. Calibration was achieved using Polystyrene beads (PS beads) based on Mie scattering principles, enabling accurate measurements of scattering intensities. Bovine serum albumin (BSA) served as a model for studying protein aggregation due to its predictable aggregation behaviour at elevated temperatures. Analysis of non-aggregated and aggregated BSA solutions revealed significant differences in particle size, underscoring the setup's capability to detect variations in aggregation states. Key findings demonstrate the system's efficacy in monitoring protein aggregation processes, which is critical for biochemical and pharmaceutical research. The precise calibration method and the use of BSA as a validation tool highlight the setup's sensitivity and accuracy in quantifying changes in particle concentration and size due to aggregation. This study provides a framework for analysing protein aggregation and offers insights into the aggregation's impact on scattering properties.
© The Authors, published by EDP Sciences, 2024
This is an Open Access article distributed under the terms of the Creative Commons Attribution License 4.0, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
