Abstract
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.
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