Cyclodextrin — A Paradigmatic Model
Since Emil Fischer’s postulate of the ‘lock and key’ specificity of enzymes with respect to substrates one tries to understand this specificity in terms of stereochemistry, interaction of specific groups, weak interactions, hydrophobic binding or rates of reactions. Even with the knowledge of the complete three-dimensional structure of many enzymes, their extremely high specificity in most cases is hard to understand. In this situation cyclodextrins have served as extremely useful models for enzyme like interactions even in an early stage of cyclodextrin research. They form stereospecific complexes. They can be used in order to separate enantiomers. They show hydrophobic interactions. They provide an inner surface with dielectric properties different from the outside solution. They show off- and on-rates in complex formation similar to those of enzymes. They can accelerate certain chemical transfer reactions to a considerable extent. Therefore during the past 30 years they have served as models for enzyme specificity, enzymatic catalysis, weak interactions, cavities in solution. They offer an ideal set of models and therefore in themselves they are models for models: paradigmatic models.
KeywordsStarch Pyrophosphate Enol Transferase Congo
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