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Figure 2 | BMC Neuroscience

Figure 2

From: Requirement of aggregation propensity of Alzheimer amyloid peptides for neuronal cell surface binding

Figure 2

Comparison of aggregation propensities of different TMR-labelled Aβ. (A) Dynamic light scattering analysis indicated that very small particles (likely to be monomers) were present in the mutant peptide solution, two distributions of oligomers were present for Aβ40, and larger oligomers were present for Aβ42. (B) Aggregation marked by thioflavin-T fluorescence at pH 6 and pH 5 illustrated weak fluorescence for the mutant peptide (Mut), moderate aggregation for Aβ40, and the highest aggregation for Aβ42. The thioflavin-T alone sample represents the total emission peak area for a control sample not containing any Aβ. The data from these techniques indicates that the rank order of aggregation propensity is Aβ42 > Aβ40 > mutant.

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