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. 2024 Dec 28;14:101879. doi: 10.1016/j.toxrep.2024.101879

Table 3.

The binding energy profile of the homodimers of the wild type (WT) and mutant Aβ42. The interacting amino acid residues of each chain are shown.

Dimer BFE
(kcal/mol)
Interacting residues
No. of H-bonds BIE (kcal/mol) Type of AD Special Characteristics
Chain A Chain B
WT −10.2 Arg5 Ala21, Glu22 13 −74.6006 sAD
His6 Phe19
Glu11 Gln15
His13 His13, Gln15
Gln15 Glu11
Phe19 His6
Glu22 Arg5
A2V mutant −10.5 Arg5 Glu22 11 −78.1829 fAD autosomal recessive mutation
His6 Val18
Glu11 Gln15
His13 His13
Lys16 His6
Leu17 His6
Gln22 Arg5
E22del mutant −8.2 Gln15 His13 12 −69.601 fAD (Osaka Variant) no senile plaque formation
Lys16 Tyr10, Glu11
Val18 His13, Gln15
Phe19 Asp1
Asn26 Glu3
Gly36 Phe19
Gly37 Phe19
Val38 Ala21, Phe20
A2T mutant −7.3 Ser8 Arg5 6 −70.4468 NA cured of AD
Tyr10 His6
Glu11 Phe4
His14 His13
Lys16 Glu11
Phe19 Lys16