Abstract
We investigate the binding of native β-cyclodextrin (β-CD) and eight novel β-CD derivatives with two different
guest compounds, using isothermal calorimetry (ITC) and 2D NOESY NMR. In all cases, the stoichiometry is 1:1
and binding is exothermic. Overall, modifications at the 3’ position of β-CD, which is at the secondary face, weaken
binding by several kJ/mol relative to native β-CD, while modifications at the 6’ position (primary face) maintain or
somewhat reduce the binding affinity. The variations in binding enthalpy are larger than the variations in binding
free energy, so entropy-enthalpy compensation is observed. Characterization of the bound conformations with
NOESY NMR shows that the polar groups of the guests may be situated at either face, depending on the host
molecule, and, in some cases, both orientations are populated. The present results were used in the SAMPL7 blinded
prediction challenge whose results are detailed in the same special issue of JCAMD.
Supplementary materials
Title
SAMPL7 Kellett Gilson NMR-trans-methyl-cyclohexanol
Description
Actions
Title
SAMPL7 Kellett Gilson ITC complexes
Description
Actions
Title
SAMPL7 Kellett Gilson Hosts SMILES
Description
Actions
Title
SAMPL7 Kellett Gilson NMR-R-Rimantidine
Description
Actions
Title
SAMPL7 Kellett Gilson enthalpograms
Description
Actions