Differential Scanning Calorimetry in the Biopharmaceutical Sciences

Biophysical Characterization of Proteins in Developing Biopharmaceuticals

Volumn , Issue , 2015, Pages 287-306

  Demarest, Stephen J ^a   Frasca, Verna ^b  

^a ELI LILLY AND COMPANY   (United States)

^b Malvern Instruments Inc   (United States)

Author keywords

Differential scanning calorimetry (DSC); Protein formulation; Therapeutic protein stability

Indexed keywords

EID: 84943517128     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-0-444-59573-7.00011-7     Document Type: Chapter

References (48)

1. Anfinsen C.B., Scheraga H.A. Experimental and theoretical aspects of protein folding. Adv Protein Chem 1975, 29:205-300.
2. Manning M.C., Patel K., Borchardt R.T. Stability of protein pharmaceuticals. Pharm Res 1989, 6:903-918.
3. Lumry R., Biltonen R. Validity of the "two-state" hypothesis for conformational transitions of proteins. Biopolymers 1966, 4:917-944.
4. Pace C.N. The stability of globular proteins. CRC Crit Rev Biochem 1975, 3:1-43.
5. Dill K.A. Dominant forces in protein folding. Biochemistry 1990, 29:7133-7155.
6. Privalov P.L. Stability of proteins: small globular proteins. Adv Protein Chem 1979, 33:167-241.
7. Privalov P.L., Gill S.J. Stability of protein structure and hydrophobic interaction. Adv Protein Chem 1988, 39:191-234.
8. Privalov P.L. Cold denaturation of proteins. Crit Rev Biochem Mol Biol 1990, 25:281-305.
9. Pace N.C., Tanford C. Thermodynamics of the unfolding of beta-lactoglobulin A in aqueous urea solutions between 5 and 55 degrees. Biochemistry 1968, 7:198-208.
10. Privalov P.L., Griko Yu V., Venyaminov S., Kutyshenko V.P. Cold denaturation of myoglobin. J Mol Biol 1986, 190:487-498.
11. Fleming P.J., Rose G.D. Do all backbone polar groups in proteins form hydrogen bonds?. Protein Sci 2005, 14:1911-1917.
12. Pace C.N. Measuring and increasing protein stability. Trends Biotechnol 1990, 8:93-98.
13. Pace C.N., Laurents D.V. A new method for determining the heat capacity change for protein folding. Biochemistry 1989, 28:2520-2525.
14. Myers J.K., Pace C.N., Scholtz J.M. Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding. Protein Sci 1995, 4:2138-2148.
15. Bull H.B., Breese K. Protein hydration. II. Specific heat of egg albumin. Arch Biochem Biophys 1968, 128:497-502.
16. Danforth R., Krakauer H., Sturtevant J.M. Differential calorimetry of thermally induced processes in solution. Rev Sci Instrum 1967, 38.
17. Jackson W.M., Brandts J.F. Thermodynamics of protein denaturation. A calorimetric study of the reversible denaturation of chymotrypsinogen and conclusions regarding the accuracy of the two-state approximation. Biochemistry 1970, 9:2294-2301.
18. Privalov P.L., Tiktopulo E.I. Thermal conformational transformation of tropocollagen. I. Calorimetric study. Biopolymers 1970, 9:127-139.
19. DSC Data Analysis in Origin. Tutorial Guide Version 5.0, 1998.
20. Marky L.A., Breslauer K.J. Calculating thermodynamic data for transitions of any molecularity from equilibrium melting curves. Biopolymers 1987, 26:1601-1620.
21. Brandts J.F., Lin L.N. Study of strong to ultratight protein interactions using differential scanning calorimetry. Biochemistry 1990, 29:6927-6940.
22. Sanchez-Ruiz J.M. Probing free-energy surfaces with differential scanning calorimetry. Annu Rev Phys Chem 2011, 62:231-255.
23. Morel B., Varela L., Conejero-Lara F. The thermodynamic stability of amyloid fibrils studied by differential scanning calorimetry. J Phys Chem B 2010, 114:4010-4019.
24. Sasahara K., Yagi H., Naiki H., Goto Y. Heat-induced conversion of beta(2)-microglobulin and hen egg-white lysozyme into amyloid fibrils. J Mol Biol 2007, 372:981-991.
25. Sasahara K., Yagi H., Naiki H., Goto Y. Heat-triggered conversion of protofibrils into mature amyloid fibrils of beta2-microglobulin. Biochemistry 2007, 46:3286-3293.
26. Dhulesia A., Cremades N., Kumita J.R., Hsu S.T., Mossuto M.F., Dumoulin M., et al. Local cooperativity in an amyloidogenic state of human lysozyme observed at atomic resolution. J Am Chem Soc 2010, 132:15580-15588.
27. Garbett N.C., Chaires J.B. Thermodynamic studies for drug design and screening. Expert Opin Drug Discov 2012, 7:299-314.
28. Garbett N.C., Mekmaysy C.S., Helm C.W., Jenson A.B., Chaires J.B. Differential scanning calorimetry of blood plasma for clinical diagnosis and monitoring. Exp Mol Pathol 2009, 86:186-191.
29. Johnson R., Lewis L. Freeze-drying protein formulations above their collapse temperatures: possible issues and concerns. Am Pharm Rev 2011, 14.
30. Pikal M.J., Rigsbee D.R., Roy M.L. Solid state chemistry of proteins: I. glass transition behavior in freeze dried disaccharide formulations of human growth hormone (hGH). J Pharm Sci 2007, 96:2765-2776.
31. Cleland J.L., Lam X., Kendrick B., Yang J., Yang T.H., Overcashier D., et al. A specific molar ratio of stabilizer to protein is required for storage stability of a lyophilized monoclonal antibody. J Pharm Sci 2001, 90:310-321.
32. Carpenter J.F., Pikal M.J., Chang B.S., Randolph T.W. Rational design of stable lyophilized protein formulations: some practical advice. Pharm Res 1997, 14:969-975.
33. Wen J., Arthur K., Chemmalil L., Muzammil S., Gabrielson J., Jiang Y. Applications of differential scanning calorimetry for thermal stability analysis of proteins: qualification of DSC. J Pharm Sci 2012, 101:955-964.
34. Fang W.J., Qi W., Kinzell J., Prestrelski S., Carpenter J.F. Effects of excipients on the chemical and physical stability of glucagon during freeze-drying and storage in dried formulations. Pharm Res 2012, 29:3278-3291.
35. Neet K.E., Timm D.E. Conformational stability of dimeric proteins: quantitative studies by equilibrium denaturation. Protein Sci 1994, 3:2167-2174.
36. Johnson C.M. Differential scanning calorimetry as a tool for protein folding and stability. Arch Biochem Biophys 2013, 531:100-109.
37. Tischenko V.M., Zav'yalov V.P., Medgyesi G.A., Potekhin S.A., Privalov P.L. A thermodynamic study of cooperative structures in rabbit immunoglobulin G. Eur J Biochem 1982, 126:517-521.
38. Garber E., Demarest S.J. A broad range of Fab stabilities within a host of therapeutic IgGs. Biochem Biophys Res Commun 2007, 355:751-757.
39. Demarest S.J., Chen G., Kimmel B.E., Gustafson D., Wu J., Salbato J., et al. Engineering stability into Escherichia coli secreted Fabs leads to increased functional expression. Protein Eng Des Sel 2006, 19:325-336.
40. Michaelson J.S., Demarest S.J., Miller B., Amatucci A., Snyder W.B., Wu X., et al. Anti-tumor activity of stability-engineered IgG-like bispecific antibodies targeting TRAIL-R2 and LTbetaR. MAbs 2009, 1:128-141.
41. Atwell S., Ridgway J.B., Wells J.A., Carter P. Stable heterodimers from remodeling the domain interface of a homodimer using a phage display library. J Mol Biol 1997, 270:26-35.
42. Dimasi N., Gao C., Fleming R., Woods R.M., Yao X.T., Shirinian L., et al. The design and characterization of oligospecific antibodies for simultaneous targeting of multiple disease mediators. J Mol Biol 2009, 393:672-692.
43. Demarest S.J., Hopp J., Chung J., Hathaway K., Mertsching E., Cao X., et al. An intermediate pH unfolding transition abrogates the ability of IgE to interact with its high affinity receptor FcepsilonRIalpha. J Biol Chem 2006, 281:30755-30767.
44. Tsai P.K., Volkin D.B., Dabora J.M., Thompson K.C., Bruner M.W., Gress J.O., et al. Formulation design of acidic fibroblast growth factor. Pharm Res 1993, 10:649-659.
45. Lah J., Prislan I., Krzan B., Salobir M., Francky A., Vesnaver G. Erythropoietin unfolding: thermodynamics and its correlation with structural features. Biochemistry 2005, 44:13883-13892.
46. Fan H., Ralston J., Dibiase M., Faulkner E., Middaugh C.R. Solution behavior of IFN-beta-1a: an empirical phase diagram based approach. J Pharm Sci 2005, 94:1893-1911.
47. Wang B., Cicerone M.T., Aso Y., Pikal M.J. The impact of thermal treatment on the stability of freeze-dried amorphous pharmaceuticals: II. Aggregation in an IgG1 fusion protein. J Pharm Sci 2010, 99:683-700.
48. Harn N., Allan C., Oliver C., Middaugh C.R. Highly concentrated monoclonal antibody solutions: direct analysis of physical structure and thermal stability. J Pharm Sci 2007, 96:532-546.