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. 1996 Oct;71(4):2144–2154. doi: 10.1016/S0006-3495(96)79415-8

Thermodynamics of hydrogen bond and hydrophobic interactions in cyclodextrin complexes.

P D Ross 1, M V Rekharsky 1
PMCID: PMC1233682  PMID: 8889190

Abstract

Values of K, delta G(o), delta H(o), delta S(o) and delta C(po) for the binding reaction of small organic ligands forming 1:1 complexes with either alpha- or beta-cyclodextrin were obtained by titration calorimetry from 15 degrees C to 45 degrees C. A hydrogen bond or hydrophobic interaction was introduced by adding a single functional group to the ligand. The thermodynamics of binding with and without the added group are compared to estimate the contribution of the hydrogen bond or hydrophobic interaction. A change in the environment of a functional group is required to influence the binding thermodynamics, but molecular size-dependent solute-solvent interactions have no effect. For phenolic O-H-O hydrogen bond formation, delta H(o) varies from -2 to -1.4 kcal mol(-1) from 15 degrees C to 45 degrees C, and delta C(p) is increased by 18 cal K(-1) mol(-1). The hydrophobic interaction has an opposite effect: in alpha-cyclodextrin, delta C(po) = -13.3 cal K(-1) mol(-1) per ligand -CH(2)-, identical to values found for the transfer of a -CH(2)-group from water to a nonpolar environment. At room temperature, the hydrogen bond and the -CH(2)-interaction each contribute about -600 cal mol(-1) to the stability (delta G(o)) of the complex. With increased temperature, the hydrogen bond stability decreases (i.e., hydrogen bonds "melt"), but the stability of the hydrophobic interaction remains essentially constant.

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Selected References

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  1. Hamilton J. A., Sabesan M. N., Steinrauf K. L., Geddes A. The crystal structure of a complex of cycloheptaamylose with 2,5-diiodobenzoic acid. Biochem Biophys Res Commun. 1976 Dec 6;73(3):659–664. doi: 10.1016/0006-291x(76)90861-5. [DOI] [PubMed] [Google Scholar]
  2. Krapunov S. N., Dragan A. I. Spektroskopiia mezhmolekuliarnykh vzaimodeistvii tirozinovogo khromofora. III. Klassifikatsiia sostoianiia ostatkov tirozina v belkakh po ikh élektronnym spektram. Biofizika. 1989 May-Jun;34(3):357–363. [PubMed] [Google Scholar]
  3. Makhatadze G. I., Privalov P. L. Contribution of hydration to protein folding thermodynamics. I. The enthalpy of hydration. J Mol Biol. 1993 Jul 20;232(2):639–659. doi: 10.1006/jmbi.1993.1416. [DOI] [PubMed] [Google Scholar]
  4. Martin P. J., Strauss U. P. Thermodynamics of hydrophobic polyacids. Biophys Chem. 1980 Jun;11(3-4):397–402. doi: 10.1016/0301-4622(80)87013-x. [DOI] [PubMed] [Google Scholar]
  5. Murphy K. P., Freire E. Thermodynamics of structural stability and cooperative folding behavior in proteins. Adv Protein Chem. 1992;43:313–361. doi: 10.1016/s0065-3233(08)60556-2. [DOI] [PubMed] [Google Scholar]
  6. Murphy K. P., Gill S. J. Solid model compounds and the thermodynamics of protein unfolding. J Mol Biol. 1991 Dec 5;222(3):699–709. doi: 10.1016/0022-2836(91)90506-2. [DOI] [PubMed] [Google Scholar]
  7. Naghibi H., Tamura A., Sturtevant J. M. Significant discrepancies between van't Hoff and calorimetric enthalpies. Proc Natl Acad Sci U S A. 1995 Jun 6;92(12):5597–5599. doi: 10.1073/pnas.92.12.5597. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Privalov P. L., Makhatadze G. I. Contribution of hydration to protein folding thermodynamics. II. The entropy and Gibbs energy of hydration. J Mol Biol. 1993 Jul 20;232(2):660–679. doi: 10.1006/jmbi.1993.1417. [DOI] [PubMed] [Google Scholar]
  9. SCHELLMAN J. A. The thermodynamics of urea solutions and the heat of formation of the peptide hydrogen bond. C R Trav Lab Carlsberg Chim. 1955;29(14-15):223–229. [PubMed] [Google Scholar]
  10. SUSI H., TIMASHEFF S. N., ARD J. S. NEAR INFRARED INVESTIGATION OF INTERAMIDE HYDROGEN BONDING IN AQUEOUS SOLUTION. J Biol Chem. 1964 Sep;239:3051–3054. [PubMed] [Google Scholar]
  11. Shirley B. A., Stanssens P., Hahn U., Pace C. N. Contribution of hydrogen bonding to the conformational stability of ribonuclease T1. Biochemistry. 1992 Jan 28;31(3):725–732. doi: 10.1021/bi00118a013. [DOI] [PubMed] [Google Scholar]
  12. Takeda Y., Ross P. D., Mudd C. P. Thermodynamics of Cro protein-DNA interactions. Proc Natl Acad Sci U S A. 1992 Sep 1;89(17):8180–8184. doi: 10.1073/pnas.89.17.8180. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Wiseman T., Williston S., Brandts J. F., Lin L. N. Rapid measurement of binding constants and heats of binding using a new titration calorimeter. Anal Biochem. 1989 May 15;179(1):131–137. doi: 10.1016/0003-2697(89)90213-3. [DOI] [PubMed] [Google Scholar]

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