Conformational study of glycal-type neuraminidase inhibitors

G. Surpateanu (1) , Jean-François Soulé (1) , J. M. Beau (1, 2) , S. Norsikian (1) , Bogdan I. Iorga (1)

1 ICSN - Institut de Chimie des Substances Naturelles
2 ICMMO - Institut de Chimie Moléculaire et des Matériaux d'Orsay

Conformational study of glycal-type neuraminidase inhibitors The conformational flexibility of two glycal-type neuraminidase inhibitors has been studied, using several molecular modeling techniques. In agreement with the experimental data available, an intramolecular hydrogen bond, representing a key structural feature that controls the conformer distribution in solution, has been identified. The contribution of each substituent on the overall equilibrium was evaluated using simplified derivatives. Additionally, four methods for estimating NMR coupling constants from dihedral angles were evaluated and the Haasnoot method was found to be appropriate for this class of sugars. These results should allow a better understanding of the structural parameters governing physico-chemical properties of glycal-like compounds.

Mots clés: molecular modeling; quantum chemistry; molecular dynamics; conformational analysis; neuraminidase inhibitors

Domaines: Chimie organique; Chimie théorique et/ou physique

G. Surpateanu, Jean-François Soulé, J. M. Beau, S. Norsikian, Bogdan I. Iorga. Conformational study of glycal-type neuraminidase inhibitors. Journal of Carbohydrate Chemistry, 2012, 31 (2), pp.114-129. ⟨10.1080/07328303.2011.636161⟩. ⟨hal-00678507⟩