On the impossibility of determination of stepwise binding constants for the 1 ∶ 2 complex of (+)-camphor with α-cyclodextrin

Literature Information

Publication Date 2003-01-13
DOI 10.1039/B209272G
Impact Factor 3.876
Authors

Helena Dodziuk, Krzysztof S. Nowinski, Wiktor Kozminski, Grigory Dolgonos


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Abstract

Knowledge of stepwise binding constants for complexes with higher than 1 ∶ 1 stoichiometry would allow one to study the cooperativity of their formation. However, a detailed analysis of partitioning of the overall binding constant β12 determined by NMR titrations for the 1 ∶ 2 complex of (+)-camphor with α-cyclodextrin into the stepwise ones K1 and K2 carried out analogously to published procedures revealed that the partitioning cannot be carried out unequivocally for K1 << K2. The programs for partitioning cannot be used as a black box and a satisfactory reproduction of the experimental dependence of relative shifts as a function of relative CD concentration should not be the only criterion of the reliability of the stepwise binding constants obtained using such programs.

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Organic & Biomolecular Chemistry
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