Recognition of Aβ oligomer by LilrB2 acceptor: a tetracoordinated zipper mechanism

Identification and characterization of the conformation and size of amyloid-β (42) oligomers targeting the receptor LilrB2

“…S6, ESI†) binding, indicating the hydrophobic residues dominates the SASA interaction in the LDD-D/T complexes, accounting for Cao et al 's observation 14 but not always the F residues for the top contribution residue. 15 Therefore, the truth should be hydrophobic residues rather than a kind of specific one, such as F , to contribute region I binding for these low-MW AβO (LDD-D/T) at the SP1 stage. The assessment can be further confirmed by following AβO–LDD binding at region I in the SP2 stage.…”

“…Taken together, the hydrophobic residues in both β1 ( F19 ) and β2 regions are key to forming the hydrophobic collapse in the pocket of region I of LDD, 14 while charged residues binding at the NR and even the turning region would further stabilize the complex. 15 Moreover, for Aβ42 protofibrils bound to region I of the LDD receptor, their major residues that contribute to the binding energy are mainly hydrophobic V18/F20 in the β1 region and I31/M35/V39/V40 in the β2 region, negatively charged E3/D7/E11 in the hydrophilic region, and hydrophobic I41/A42 at the C-terminus.…”

“…Further study revealed that four hydrophobic residues, including the two phenylalanine residues, are required to stabilize the AbO-LDD complex. 15 In addition, LDD was observed specifically to inhibit the growth of Ab42 protofibrils by binding to the growing end of the protofibril, with unknown accommodation of LDD for protofibril binding. 16 Different sizes and conformations of AbO may be produced through several pathways and have varying toxic effects.…”