Figure 5: Formation and properties of A108I and V30M heterotetramers. | Scientific Reports

Figure 5: Formation and properties of A108I and V30M heterotetramers.

From: Cavity filling mutations at the thyroxine-binding site dramatically increase transthyretin stability and prevent its aggregation

Figure 5

Panel A shows a scheme of the protocol used to produce hybrid tetramers. Panel B shows Trp spectra emission of the mixture obtained at different moments of the assay, in which spectral shifts indicate the state of folding. The black continuous, black discontinuous and grey lines correspond to the spectra before application of HPP, after application of maximum HPP and upon refolding, respectively. Panel C shows the oligomeric state of the sample probed by SEC. The main peak on the chromatogram corresponds to the tetramer. Panel D shows the HHP titration assay. Trp fluorescence emission was used to report on the stability of the samples against increasing pressure. The results of an acidic induced aggregation assay for an equimolar mixture of non treated TTR A108V and TTR V30M and the hetroterameric mixture are shown in the inset.

Back to article page