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Article Dans Une Revue Physical Chemistry Chemical Physics Année : 2022

How change in chirality prevents β-amyloid type interaction in a protonated cyclic dipeptide dimer

Résumé

The protonated dimers of the diketopiperazine dipeptide cyclo (LPhe-LHis) and cyclo (LPhe-DHis) are studied by laser spectroscopy combined with mass spectrometry to shed light on the influence of stereochemistry on the clustering propensity of cyclic dipeptides. The marked spectroscopic differences experimentally observed in the hydride stretch region are well accounted for by the results of DFT calculations. Both diastereomeric protonated dimers involve a strong ionic hydrogen bond from the protonated imidazole ring of one monomer to the neutral imidazole nitrogen of the other. While this strong interaction is accompanied by a single NHÁ Á ÁO hydrogen bond between the amide functions of the two moieties for the protonated dimer of cyclo (LPhe-DHis), that of cyclo (LPhe-LHis) involves two NHÁ Á ÁO interactions, forming the motif of an antiparallel b sheet. Therefore, a change in chirality of the residue prevents the formation of the b sheet pattern observed in the amyloid type aggregation. These results emphasize the peculiar role of the histidine residue in peptide structure and interaction.
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Dates et versions

hal-03788936 , version 1 (27-09-2022)

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Katia Le Barbu-Debus, Ariel Pérez-Mellor, Valéria Lepère, Anne Zehnacker. How change in chirality prevents β-amyloid type interaction in a protonated cyclic dipeptide dimer. Physical Chemistry Chemical Physics, 2022, 24, pp.19783 - 19791. ⟨10.1039/d2cp03110h⟩. ⟨hal-03788936⟩
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