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Fig. 2 | Molecular Neurodegeneration

Fig. 2

From: Biophysical mapping of TREM2-ligand interactions reveals shared surfaces for engagement of multiple Alzheimer’s disease ligands

Fig. 2

Mutations to TREM2 hydrophobic site ablate binding to apoE4. Immobilized TREM2 WT and variants were probed for binding to apoE4 (0.012–50 µM). (A) Scheme of experiment. (B) Summary of steady-state binding for TREM2 WT and variants from our previous publication [9]. (C-J) BLI sensorgrams for TREM2 (C) R46A/R47A, (D) L69D/L71D, (E) W44D/L69D/L71D, (F) D87N, (G) R76D, (H) R77D, (I) R122D/K123D binding to apoE4 (0.012–50 µM). Double-reference subtracted data shown in black. (J) Steady state analysis and non-linear fits to derive KD from data shown in (C-I). The derived KDs are listed in Table 1

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Molecular Neurodegeneration

ISSN: 1750-1326