Skip to main content
. Author manuscript; available in PMC: 2018 Aug 1.
Published in final edited form as: Bioorg Med Chem Lett. 2017 May 26;27(15):3441–3449. doi: 10.1016/j.bmcl.2017.05.080

Figure 2.

Figure 2

Summary of the structure-activity relationships (data derived) from a trio of previous libraries designed to screen the three substructures of a typical small molecule TTR amyloidosis inhibitor (i.e., Aryl-X, Linker-Y, and Aryl-Z).46–48 Substructures are quantitatively ranked according to the average experimental efficacy scores (EES) as determined using Equation 1, which evaluates the ability of a substructure to afford potent aggregation inhibitors in vitro that bind selectively to TTR in human blood plasma ex vivo.