Aggregates of α-chymotrypsinogen anneal to access more stable states

Biotechnology and Bioengineering

Volumn 111, Issue 4, 2014, Pages 782-791

  Maurer, Ronald W ^a   Hunter, Alan K ^b   Robinson, Anne S ^a,c   Roberts, Christopher J ^a  

^a UNIVERSITY OF DELAWARE   (United States)

^b MEDIMMUNE   (United States)

^c Tulane University   (United States)

Author keywords

Aggregate dissociation; Protein aggregation; Protein stability

Indexed keywords

ANNEALING; DENATURATION; DISSOCIATION; MONOMERS; PROTEINS; STRUCTURAL RELAXATION; UREA;

DENATURING CONDITIONS; DISSOCIATION PROCESS; ELEVATED TEMPERATURE; FREE ENERGY LANDSCAPE; PHARMACEUTICAL DEVELOPMENT; PROTEIN AGGREGATION; PROTEIN STABILITY; QUALITY AND SAFETIES;

AGGREGATES;

CHYMOTRYPSINOGEN; MONOMER; THIOFLAVINE; TRYPTOPHAN; UREA;

ARTICLE; CIRCULAR DICHROISM; COMPETITION; DEPOLYMERIZATION; DISSOCIATION; FLUORESCENCE; GEL PERMEATION CHROMATOGRAPHY; INCUBATION TEMPERATURE; LIGHT SCATTERING; MOLECULAR WEIGHT; POLYMERIZATION; PROTEIN AGGREGATION; PROTEIN FOLDING; PROTEIN REFOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; TEMPERATURE;

AGGREGATE DISSOCIATION; PROTEIN AGGREGATION; PROTEIN STABILITY;

CHYMOTRYPSINOGEN; CIRCULAR DICHROISM; POLYMERIZATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN MULTIMERIZATION; PROTEIN STABILITY; TEMPERATURE;

EID: 84894282128     PISSN: 00063592     EISSN: 10970290     Source Type: Journal    
DOI: 10.1002/bit.25129     Document Type: Article

References (39)

1. Andrews JM, Roberts CJ. 2007a. Non-native aggregation of alpha-chymotrypsinogen occurs through nucleation and growth with competing nucleus sizes and negative activation energies. Biochemistry 46(25):7558-7571.
2. Andrews JM, Roberts CJ. 2007b. A Lumry-Eyring nucleated polymerization model of protein aggregation kinetics: 1. Aggregation with pre-equilibrated unfolding. J Phys Chem B 111(27):7897-7913.
3. Bauer HH, Aebi U, Häner M, Hermann R, Müller M, Arvinte T, Merkle HP. 1995. Architecture and polymorphism of fibrillar supramolecular assemblies produced by in vitro aggregation of human calcitonin. J Struct Biol 115(1):1-15.
4. Brummitt RK, Nesta DP, Chang L, Chase SD, Laue TM, Roberts CJ. 2011. Nonnative aggregation of an IgG1 antibody in acidic conditions: Part 1. unfolding, colloidal interactions, and formation of high-molecular-weight aggregates. J Pharm Sci 100(6):2087-2103.
5. Brummitt RK, Andrews JM, Jordan JL, Fernandez EJ, Roberts CJ. 2012. Thermodynamics of amyloid dissociation provide insights into aggregate stability regimes. Biophys Chem 168-169:10-18.
6. Chi EY, Krishnan S, Randolph TW, Carpenter JF. 2003. Physical stability of proteins in aqueous solution: mechanism and driving forces in nonnative protein aggregation. Pharm Res 20(9):1325-1336.
7. Chiti FD, Dobson CM. 2006. Protein misfolding, functional amyloid, and human disease. Annu Rev Biochem 75:333-366.
8. De Bernardez Clark ES, Schwarz E, Rudolph R. 1999. Inhibition of aggregation side reactions during in vitro protein folding. Methods Enzymol 309:217-236.
9. Dobson CM. 2004. Principles of protein folding, misfolding and aggregation. Semin Cell Dev Biol 15(1):3-16.
10. Dobson CM. 2006. Protein aggregation and its consequences for human disease. Prot Pept Lett 13(3):219-227.
11. Eisenberg DN, Nelson R, Sawaya MR, Balbirnie M, Sambashivan S, Ivanova MI, Madsen AØ, Riekel C. 2006. The structural biology of protein aggregation diseases: Fundamental questions and some answers. Acc Chem Res 39(9):568-575.
12. Fink AL. 1998. Protein aggregation: Folding aggregates, inclusion bodies and amyloid. Fold Des 3(1):R9-R23.
13. Foguel DR, Robinson CR, de Sousa PC, Silva JL, Robinson AS. 1999. Hydrostatic pressure rescues native protein from aggregates. Biotech Bioeng 63(5):552-558.
14. Gast KM, Modler AJ, Damaschun H, Krober R, Lutsch G, Zirwer D, Golbik R, Damaschun G. 2003. Effect of environmental conditions on aggregation and fibril formation of barstar. Eur Biophys J 32(8):710-723.
15. Goldsbury CF, Frey P, Olivieri V, Aebi U, Müller SA. 2005. Multiple assembly pathways underlie amyloid-beta fibril polymorphisms. J Mol Biol 352(2):282-298.
16. Gorovits BM, Horowitz PM. 1998. High hydrostatic pressure can reverse aggregation of protein folding intermediates and facilitate acquisition of native structure. Biochem 37(17):6132-6135.
17. Hawe A, Sutter M, Jiskoot W. 2008. Extrinsic fluorescent dyes as tools for protein characterization. Pharm Res 25(7):1487-1499.
18. Hong DP, Ahmad A, Fink AL. 2006. Fibrillation of human insulin A and B chains. Biochemistry 45(30):9342-9353.
19. Jahn TR, Radford SE. 2005. The yin and yang of protein folding. FEBS J 272(23):5962-5970.
20. Jiménez JL, Guijarro JI, Orlova E, Zurdo J, Dobson CM, Sunde M, Sibil HR. 1999. Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing. EMBO J 18(4):815-821.
21. Jiménez JL, Nettleton EJ, Bouchard M, Robinson CV, Dobson CM, Sibil HR. 2002. The protofilament structure of insulin amyloid fibrils. Proc Nat Acad Sci USA 99(14):9196-9201.
22. Kiefhaber TR, Rudolph R, Kohler HH, Buchner J. 1991. Protein aggregation in vitro and in vivo: A quantitative model of the kinetic competition between folding and aggregation. Nat Biotechnol 9:825-829.
23. Kelly SM, Price NC. 2000. The use of circular dichroism in the investigaiton of protein structure and function. Curr Prot Pep Sci 1(4):349-384.
24. Krebs MRH, Domike KR, Donald AM. 2009. Protein aggregation: More than just fibrils. Biochem Soc Trans 37(4):682-686.
25. Levine H. 1993. Thioflavine T interaction with synthetic Alzheimer's disease β-amyloid peptides: Detection of amyloid aggregation in solution. Prot Sci 2(3):404-410.
26. Li Y, Weiss WF, Roberts CJ. 2009. Characterization of high-molecular-weight nonnative aggregates and aggregation kinetics by size exclusion chromatography with inline multi-angle laser light scattering. J Pharm Sci 98(11):3997-4016.
27. Lilie H, Schwarz E, Rudolph R. 1998. Advances in refolding of proteins produced in E. coli. Curr Opin Biotechnol 9(5):497-501.
28. Orsini G, Goldberg ME. 1978. The renaturation of reduced chymotrypsinogen A in guanidine HCl. Refolding versus aggregation. J Biol Chem 253(10):3453-3458.
29. Rosenberg AS. 2006. Effects of protein aggregates: An immunologic perspective. AAPS J 8(3):E501-E507.
30. Ross CA, Poirer MA. 2004. Protein aggregation and neurodegenerative disease. Nat Med 10:S10-S17.
31. Sahin E, Grillo AO, Perkins MD, Roberts CJ. 2010. Comparative effects of pH and ionic strength on protein-protein interactions, unfolding, and aggregation for IgG1 antibodies. J Pharm Sci 99(12):4830-4848.
32. Smith MH. 1970. Peptides and proteins. In: Sober HA, editor. Handbook of biochemistry. 2nd edn. Cleveland, OH: The Chemical Rubber Co. p 71-98.
33. Threlfall T. 2003. Structural and thermodynamic explanations of Ostwald's rule. Org Process Rev Dev 7:1017-1027.
34. Uversky VN, Fink AL. 2004. Conformational constraints for amyloid fibrillation: The importance of being unfolded. Biochim Biophys Acta 1698(2):131-153.
35. Wang W. 2005. Protein aggregation and its inhibition in biopharmaceutics. Int J Pharm 289(1):1-30.
36. Weiss WF, Hodgdon TK, Kaler EW, Lenhoff AM, Roberts CJ. 2007. Nonnative protein polymers: Structure, morphology, and relation to nucleation and growth. Biophys J 93(12):4392-4403.
37. Weiss WF, Young TM, Roberts CJ. 2009. Principles, approaches, and challenges for predicting protein aggregation rates and shelf life. J Pharm Sci 98(4):1246-1277.
38. Wetzel R. 1994. Mutations and off-pathway aggregation of proteins. Trends Biotech 12(5):193-198.
39. Zhang A, Jordan JL, Ivanova MI, Weiss WF, Roberts CJ, Fernandez EJ. 2010. Molecular level insights into thermally induced α-chymotrypsinogen A amyloid aggregation mechanism and semiflexible protofibril morphology. Biochemistry 49(49):10553-10564.