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. 2021 Feb 23;60(9):678–688. doi: 10.1021/acs.biochem.1c00003

Figure 4.

Figure 4

ProSP-C BRICHOS T187R binding to soluble Aβ42 aggregates of different sizes; analysis of ACCs in FCCS measurements. (A) Normalized temporal ACCs of 100 nM HiLyteFluor488-Aβ42 (a1–a3) and 100 nM proSP-C BRICHOS T187R-Atto655 (aa1–aa3) during Aβ42 aggregation for different initial concentrations of unlabeled Aβ42 [(1) 20 μM, (2) 10 μM, and (3) 5 μM] in the presence of unlabeled 385 nM proSP-C BRICHOS T187R. (B) MEMFCS analysis of ACCs shown in panel A displaying the distribution of diffusion times for 100 nM HiLyteFluor488-Aβ42 (b1–b3) and 100 nM proSP-C BRICHOS T187R-Atto655 (bb1–bb3) during Aβ42 aggregation. The green and red diffusion time distributions reflect the diffusion of monomeric HiLyteFluor488-Aβ42 and proSP-C BRICHOS T187R-Atto655, respectively. (C) Apparent average number of HiLyteFluor488-Aβ42 (c1) and proSP-C BRICHOS T187R-Atto655 (cc1) molecules in the observation volume element during the time course of Aβ42 aggregation. (D) Apparent brightness of HiLyteFluor488-Aβ42 (d1) and proSP-C BRICHOS T187R-Atto655 (dd1) molecules, as reflected by the counts per molecule and second (CPM). (E) Relative amplitude of the second component for HiLyteFluor488-Aβ42 (e1) and proSP-C BRICHOS T187R-Atto655 (ee1) molecules. (F) Diffusion time of the second component of HiLyteFluor488-Aβ42 (f1) and proSP-C BRICHOS T187R-Atto655 (ff1) molecules during the time course of Aβ42 aggregation.