Publication | Closed Access
Molecular Recognition of C<sub>60</sub> with γ‐Cyclodextrin
248
Citations
17
References
1994
Year
Molecular CharacterizationC60 Derivatives InhibitHiv-1 ProteaseEngineeringBiochemistryProtein AssemblyProtein FoldingNatural SciencesCyclodextrin ProductionMolecular BiologyActive SiteBiochemical InteractionBiomolecular InteractionAnalytical UltracentrifugationMolecular RecognitionMolecular ModelingHost-guest Chemistry
Charge-transfer interactions stabilize the 1:2 complex between C60 and γ-cyclodextrin (schematic representation shown on the right). Since it is known that C60 derivatives inhibit, for instance, the HIV-1 protease, this result is also important for the understanding of the molecular recognition of C60 by the hydrophobic pocket of the active site of enzymes.
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