Quantifying Species-Specific Binding Affinities of Transthyretin Aggregation Inhibitors

F-NMR aggregation data for designed peptide inhibitors. The results show that concatenating two capping peptides increases their binding affinity to both TTR tetramers and monomeric intermediates by about two-fold, relative to the same peptides mixed separately at equal concentrations. Our method enables direct, quantitative comparison of species-dependent inhibitor binding, providing mechanistic insights useful for designing and optimizing TTR aggregation inhibitors.