ArticleBiomolecules2025
Observing Picomolar Protein Unfolding Using Resonance Light Scattering.
Article in Biomolecules, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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5 authors.
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Abstract
We here present a novel and sensitive methodology for determining the melting point (MP) of Bovine Serum Albumin (BSA) from micromolar to picomolar concentration levels under label-free conditions. At 1 pM we could model the melting with a sharp Gaussian. However, from the transient state observed during the melting process by using a simple exponential decay model, we determined a time constant of 67 s. We applied this methodology by studying a 3.3 pM sample of a botulinum toxin A (BoNT-A) (stabilized with 2.8 nanomolar denatured Human Serum Albumin (HSA)). We were able to determine the Tm of BoNT-A in the presence of approximately 1000-fold more concentrated HSA. This method enables the detection of protein melting transitions at picomolar concentrations without the use of a fluorescence dye. Its sensitivity and simplicity make it a valuable analytical tool for studying protein stability in diluted pharmaceutical formulations. This method is useful for correlating thermal conformational changes with catalytic function.
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