Destabilization of cytochrome c by modified β-cyclodextrin

Journal of Thermal Analysis and Calorimetry

Volumn 113, Issue 3, 2013, Pages 1491-1496

  Kamiyama, Tadashi ^a   Tanaka, Toshiya ^a   Satoh, Megumi ^a   Kimura, Takayoshi ^a  

^a KINKI UNIVERSITY   (Japan)

Author keywords

Cyclodextrin; Cytochrome c; DSC; Hydrophobic interaction; Stability

Indexed keywords

CYTOCHROME C; DESTABILIZATION EFFECTS; DSC; HYDROPHOBIC GROUPS; HYDROPHOBIC INTERACTIONS; SECONDARY STRUCTURES; STABILIZATION EFFECTS; THERMAL DENATURATIONS;

CONVERGENCE OF NUMERICAL METHODS; DIFFERENTIAL SCANNING CALORIMETRY; FUNCTIONAL GROUPS; HYDROGEN BONDS; HYDROPHOBICITY; PROTEINS; UREA;

CYCLODEXTRINS;

EID: 84883158953     PISSN: 13886150     EISSN: None     Source Type: Journal    
DOI: 10.1007/s10973-013-2969-7     Document Type: Conference Paper

References (36)

1. Tanford C. Isothermal unfolding of globular proteins in aqueous urea solutions. J Am Chem Soc. 1964;86:2050-9.
2. Religa TL, Markson JS, Mayor U, Freund SMV, Fersht AR. Solution structure of a protein denatured state and folding intermediate. Nature. 2005;437:1053-6.
3. Shriver JW. Protein structure, stability, and interactions. Methods mol biol. 2009:490.
4. Schin CH. Solubility as a function of protein structure and solvent components. Nat Biotech. 1990;8:308-17.
5. Jaenicke R, Seckler R. Protein mis-assembly in vitro. Adv Prot Chem. 1997;50:1-59.
6. Goto Y, Ichimura N, Hamaguchi K. Effects of ammonium sulfate on the unfolding and refolding of the variable and constant fragments of an immunoglobulin light chain. Biochemistry. 1998;27:1670-7.
7. Kamiyama T, Liu H, Kimura T. Preferential solvation of lysozyme by dimethyl sulfoxide in binary solutions of water and dimethyl sulfoxide. J Therm Anal Calorim. 2009;95:353-9.
8. Baldwin RL. Temperature dependence of the hydrophobic interaction in protein folding. Proc Natl Acad Sci USA. 1986;83:8069-72.
9. Marshall KE, Morris KL, Charlton D, O'Reilly N, Lewis L, Walden H, Serpell LC. Hydrophobic, aromatic, and electrostatic interactions play a central role in amyloid fibril formation and stability. Biochemistry. 2011;50:2061-71.
10. Hills RD, Brooks CL. Hydrophobic cooperativity as a mechanism for amyloid nucleation. J Mol Biol. 2007;368:894-901.
11. Lewis EA, Hansen LD. Thermodynamics of binding of guest molecules to α- and β-cyclodextrins. J Chem Soc Perkin Trans. 1973;2:2081-5.
12. Takagi S, Fujisawa M, Kimura T. Enthalpy and entropy changes on molecular inclusion of 1,3-butanediol in to α and β-cyclodextrin cavities in aqueous solutions. Thermochim Acta. 1991;183:289-97.
13. Kitae T, Nakayama T, Kano K. Chiral recognition of α-amino acids by charged cyclodextrins through cooperative effects of Coulomb interaction and inclusion. J Chem Soc Perkin Trans. 1998;2:207-12.
14. Benko M, Tabajdi R, Király Z. Thermodynamics of formation of β-cyclodextrin inclusion complexes with four series of surfactant homologs. J Therm Anal Calorim. 2012. doi: 10.1007/s10973-012-2603-0.
15. Serafini MR, Menezes PP, Costa LP, Lima CM, Quintans LJ Jr, Cardoso JC, Matos JR, Soares-Sobrinho JL, Grangeiro S Jr, Nunes PS, Bonjadim LR, Araújo AAS. Interaction of p-cymene with β-cyclodextrin. J Therm Anal Calorim. 2012;109:951-5.
16. n CN:) n = 1-8) in aqueous solution. J Therm Anal Calorim. 2012;108:695-704.
17. Wszelaka-Rylik M, Gierycz P. Isothermal titration calorimetry (ITC) study of natural cyclodextrins inclusion complexes with drugs. J Therm Anal Calorim. 2012. doi: 10.1007/s10973-012-2251-4.
18. Castronuovo G, Niccoli M. Solvent effects on the complexation of 1-alkanols by parent and modified cyclodextrins. Calorimetric studies at 298 K. J Therm Anal Calorim. 2011;103:641-6.
19. Kamiyama T, Satoh M, Tateishi T, Nojiri T, Takeuchi D, Kimura T. Effects of modified β-cyclodextrin on thermal stability and conformation of lysozyme. Thermochim Acta. 2012;532:10-4.
20. Kamiyama T. Thermodynamic properties of protein in solution. Netsu Sokutei. 2012;39(2):47-53.
21. Kamiyama T, Kimura T. Effects of cyclodextrin on thermal stability of cytochrome c. Netsu Sokutei. 2012;W39:1-5.
22. Nicholls A, Sharp KA, Honig B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins. 1991;11:281-96.
23. Easton CJ, Lincoln SF. Modified cyclodextrins: scaffolds and templates for supramolecular chemistry. London: Imperial college press: world scientific publishing company; 1999.
24. Diakur J, Zuo Z, Wiebe LI. Synthesis and drug complexation studies with β-cyclodextrins fluorinated on the primary face. J Carbohydrate Chem. 1999;18:209-23.
25. Uedaira H, Uedaira H. The effect of sugars on the thermal denaturation of lysozyme. Bull Chem Soc Jpn. 1980;53:2451-5.
26. Cooper A. Effect of cyclodextrins on the thermal stability of globular proteins. J Am Chem Soc. 1992;114:9208-9.
27. Maeda M, Takagi S. Calorimetric studies on molecular inclusion II. Systems of methanol +, 1-propanol +, and 1-pentanol + cycloheptaamylose in aqueous solutions at 298.15 K. Netsu Sokutei. 1983;10(2):43-7.
28. Maeda M, Takagi S. Calorimetric studies on Molecular inclusion III. Gibbs energies and entropies of 1-propanol and 1-pentanol into cyclohexaamylose and cycloheptaamylose in aqueous solutions at 298.15 K. Netsu Sokutei. 1983;10(3):103-7.
29. Takagi S, Maeda M. Calorimetric determination of enthalpies, Gibbs energies, and entropies of inclusion of some alcohols into α- and β-cyclodextrins in aqueous solutions. J Inclusion Phenom. 1984;2:775-80.
30. Pace CN. Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol. 1986;131:266-80.
31. Czarnik-Matusewicz B, Kim SB, Jung YM. A study of urea-dependent denaturation of beta-lactoglobulin by principal component analysis and two-dimensional correlation spectroscopy. J Phys Chem B. 2009;113:559-66.
32. O'Brien EP, Dima RI, Brooks B, Thirumalai D. Interactions between hydrophobic and ionic solutes in aqueous guanidinium chloride and urea solutions: lessons for protein denaturation mechanism. J Am Chem Soc. 2007;129:7346-53.
33. Deepak RC, Dietmar P, Angel EG. Equilibrium study of protein denaturation by urea. J Am Chem Soc. 2010;132:2338-44.
34. Sayle R, Milner-White EJ. RasMol: biomolecular graphics for all. Trends Biochem Sci. 1995;20:374.
35. Mirkin N, Jaconcic J, Stojanoff V, Moreno A. High resolution X-ray crystallographic structure of bovine heart cytochrome c and its application to the design of an electron transfer biosensor. (Cytochrome c from Bovine heart, PDB-ID: 2B4Z). Proteins. 2008;70:83-92.
36. Wilson KP, Malcolm BA, Matthews BW. Structural and thermodynamic analysis of compensating mutations within the core of chicken egg white lysozyme. (Lysozyme from Hen egg, PDB-ID: 1HEL). J Biol Chem. 1992;267:10842-9.