(-)-Epigallocatechin-3-gallate (EGCG) has been proved effective in preventing the aggregation of amyloid �-peptide 42 (A�42), and the thermodynamic interactions between them were studied in our previous work. To further probe the interactions between different regions of A�42 and EGCG, three A�42 fragments (A�1-16, A�1-30, and A�31-42) were synthesized and the interactions between each of the fragments and EGCG were investigated by isothermal titration calorimetry. It is found that though hydrogen bonding and hydrophobic interaction are both involved in the interactions between A�42 and EGCG, hydrogen bonding mainly happens in A�1-16 while hydrophobic interaction mainly happens in A�17-42. When A�42 and its fragments are saturated by EGCG, the thermodynamic parameters for them have linear relationships. It suggests that there are not specific interactions and binding sites in the A�42 and EGCG binding. Moreover, there is significant enthalpy-entropy compensation in the binding of EGCG to A�42 and its fragments.

Thermodynamics of the molecular interactions between amyloid β-peptide fragments and (-)-epigallocatechin-3-gallate

243rd National Meeting (2012)

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