Complexation Thermodynamics of Cyclodextrins

Rekharsky, Mikhail V.; Inoue, Yoshihisa

doi:10.1021/cr970015o

Cited by 3,055 publications

(2,694 citation statements)

References 248 publications

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“…Figure 3 shows a plot of the frequency of occurrence of complexes with specific values of K a for a-, b-, and g-cyclodextrins. [11,12] This and subsequent frequency plots show the number of equilibrium constants lying within each 0.25 range of pK a unit for the entire range for which data are available. Connors previously reported and discussed individual plots of this nature for a-, b-, and g-cyclodextrins.…”

Section: Cyclodextrinsmentioning

confidence: 99%

“…Distribution of a-, b-, and g-cyclodextrin complexes within a particular range of lg K a values (K a = 10 2.5AE1.1 m À1 , n = number of complexes). [11,12] Figure 4 shows a plot of the DH values versus the DS values measured experimentally for 1121 of the complexes plotted in Figure 3. [11] There is a strong enthalpy/entropy compensation, such that the free energy of complexation remains around À3.5 kcal mol À1 .…”

Section: Cyclodextrinsmentioning

confidence: 99%

“…[11,12] Figure 4 shows a plot of the DH values versus the DS values measured experimentally for 1121 of the complexes plotted in Figure 3. [11] There is a strong enthalpy/entropy compensation, such that the free energy of complexation remains around À3.5 kcal mol À1 . These types of plots were made earlier by Connors for individual classes of cyclodextrins.…”

Section: Cyclodextrinsmentioning

confidence: 99%

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Binding Affinities of Host–Guest, Protein–Ligand, and Protein–Transition‐State Complexes

et al. 2003

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The affinities of hosts—ranging from small synthetic cavitands to large proteins—for organic molecules are well documented. The average association constants for the binding of organic molecules by cyclodextrins, synthetic hosts, and albumins in water, as well as of catalytic antibodies or enzymes for substrates are 103.5±2.5 M−1. Binding affinities are elevated to 108±2 M−1 for the complexation of transition states and biological antigens by antibodies or inhibitors by enzymes, and to 1016±4 M−1 for transition states with enzymes. The origins of the distributions of association constants observed for the broad range of host–guest systems are explored in this Review, and typical approaches to compute and analyze host–guest binding in solution are discussed. In many classes of complexes a rough correlation is found between the binding affinity and the surface area that is buried upon complexation. Enzymes transcend this effect and achieve transition‐state binding much greater than is expected from the surface areas.

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Section: Cyclodextrinsmentioning

confidence: 99%

Section: Cyclodextrinsmentioning

confidence: 99%

Section: Cyclodextrinsmentioning

confidence: 99%

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Binding Affinities of Host–Guest, Protein–Ligand, and Protein–Transition‐State Complexes

et al. 2003

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“…Cyclic host molecules, such as modified cyclodextrins1a,1g and self‐assembled metal–organic cages1f,1h,1i,1l–1n and organic nanocapsules,1c are among the most extensively investigated host molecules. However, owing to their rigid and distinct conformational scaffold, a limited number of guest molecules of complementary size and shape can be entrapped in their cavities.…”

mentioning

confidence: 99%

“Helix‐in‐Helix” Superstructure Formation through Encapsulation of Fullerene‐Bound Helical Peptides within a Helical Poly(methyl methacrylate) Cavity

et al. 2016

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A one‐handed 310‐helical hexapeptide is efficiently encapsulated within the helical cavity of st‐PMMA when a fullerene (C60) derivative is introduced at the C‐terminal end of the peptide. The encapsulation is accompanied by induction of a preferred‐handed helical conformation in the st‐PMMA backbone with the same‐handedness as that of the hexapeptide to form a crystalline st‐PMMA/peptide‐C60 inclusion complex with a unique optically active helix‐in‐helix structure. Although the st‐PMMA is unable to encapsulate the 310‐helical peptide without the terminal C60 unit, the helical hollow space of the st‐PMMA is almost filled by the C60‐bound peptides. This result suggests that the C60 moiety can serve as a versatile molecular carrier of specific molecules and polymers in the helical cavity of the st‐PMMA for the formation of an inclusion complex, thus producing unique supramolecular soft materials that cannot be prepared by other methods.

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“…The exterior of the cavity is hydrophilic and makes the cyclodextrin water-soluble, while the hydrophobic interior enables cyclodextrins to form inclusion (host-guest) complexes with various molecules. The most probable noncovalent binding mode involves the inclusion of the less polar part of the guest molecule into the cavity, while the more polar group of the guest is exposed to the bulk solvent just outside the wider opening of the cavity [7]. As a general rule, the complex is strong when there is size complementarity between the guest and the cavity of the CD [8,9].…”

mentioning

confidence: 99%

On the specificity of cyclodextrin complexes detected by electrospray mass spectrometry

Gabelica

Galić

Pauw

2002

J. Am. Soc. Mass Spectrom.

123

116

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␣-cyclodextrin complexes with linear ␣, -dicarboxylic acids were investigated by electrospray mass spectrometry. These hydrophobic complexes are known to have an equilibrium binding constant that increases with the diacid chain length. However, the electrospray mass spectrometry (ES-MS) spectra showed that the relative intensity of the complex did not vary significantly with chain length. This contradiction is caused by a contribution of nonspecific adducts to the signal of the complex in ES-MS. In order to estimate the contribution of nonspecific adducts to the total intensity of the complexes with ␣-cyclodextrin, the comparison was made between ␣-cyclodextrin and maltohexaose, the latter being incapable of making inclusion complexes in solution. The signal observed for complexes between diacids and maltohexaose can only result from nonspecific electrostatic aggregation, and is found to be more favorable with the shorter diacids. This is also supported by MS/MS experiments. A procedure is described which allows estimation of the contribution of the nonspecific complex in the spectra of the complexes with ␣-cyclodextrin by using the relative intensity of the complex with maltohexaose. The contribution of the specific complex to the total signal intensity is found to increase with the diacid chain length, which is in agreement with solution behavior. (J Am Soc Mass Spectrom 2002, 13, 946 -953)

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Complexation Thermodynamics of Cyclodextrins

Cited by 3,055 publications

References 248 publications

Binding Affinities of Host–Guest, Protein–Ligand, and Protein–Transition‐State Complexes

Binding Affinities of Host–Guest, Protein–Ligand, and Protein–Transition‐State Complexes

“Helix‐in‐Helix” Superstructure Formation through Encapsulation of Fullerene‐Bound Helical Peptides within a Helical Poly(methyl methacrylate) Cavity

On the specificity of cyclodextrin complexes detected by electrospray mass spectrometry

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