Fig. 6: Morphological differentiation induced by co-aggregating sequence-dependent variants of the VQIVYK aggregation prone peptide. | Nature Communications

Fig. 6: Morphological differentiation induced by co-aggregating sequence-dependent variants of the VQIVYK aggregation prone peptide.

From: Mapping the sequence specificity of heterotypic amyloid interactions enables the identification of aggregation modifiers

Fig. 6

a Electron micrographs indicate that co-aggregating sequences modify the morphology of amyloid fibrils formed compared to the VQIVYK-alone fibrils. b, c Normalised binding spectra of b pFTAA and c curcumin amplified from fibrils derived from mix, peptide modifier-alone or VQIVYK-alone samples. Data points are shown as mean values ± SD. d, e PCA of the derived d pFTAA and e curcumin spectra highlighted the distribution of heterogenic conformers that cluster in the defined eigen space. For each sample, six individual preparations were split in five independent aliquots and combined in thirty data points (n = 30) per sample in order to represent the intrinsic variability in the fluorescence measurements. Source data are provided as a Source Data file.

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