Differential recruitment efficacy of patient-derived amyloidogenic and myeloma light chain proteins by synthetic fibrils—A metric for predicting amyloid propensity
Fig 5
Thermodynamic folding stability of AL- and MM-associated LC does not correlate with fibril recruitment efficacy.
(A) Estimates of the thermodynamic folding stability expressed as the apparent melting midpoint at a scan rate of 0.5°C/min (Tmapp). Numbers indicate the Tmapp of individual LCs. Correlation analyses of (B), Tmapp and rVλ6Wil fibril recruitment efficacy at 24 h of incubation (% bound) and of (C), Tmapp and the calculated recruitment rate. Black and gray symbols in B and C represent the MM- and AL-associated LC, respectively. Correlation coefficients in B and C were not significant (p = 0.68).