Ultraviolet Absorption Spectroscopy

Analysis of Aggregates and Particles in Protein Pharmaceuticals

Volumn , Issue , 2012, Pages 169-200

  Esfandiary, Reza ^a   Middaugh, Charles Russell ^a  

^a UNIVERSITY OF KANSAS   (United States)

Author keywords

Direct measurement, probing protein aggregation, aggregation kinetics; Indirect measures of protein aggregation, UV absorption, a powerful tool; UV , spectroscopy in protein aggregate, probing intermediate states

Indexed keywords

EID: 84886230467     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9781118150573.ch8     Document Type: Chapter

References (103)

1. Beaven GH, Holiday ER. Ultraviolet absorption spectra of proteins and amino acids. Adv Protein Chem 1952;7:319-386.
2. Zhang Z, Smith DL, Smith JB. Human ß-crystallins modified by backbone cleavage, deamidation and oxidation are prone to associate. Exp Eye Res 2003;77(3): 259-272.
3. Ramachandran LK, Witkop B. Selective cleavage of C-tryptophyl peptide bonds in proteins and peptides. J Am Chem Soc 1959;81:4028-4032.
4. Morrison WW, Frajola WJ. Multiple assay of tryptophan pyrrolase in Drosophila. Ohio J Sci 1968;68(6):285-290.
5. Wetlaufer DB. Ultraviolet spectra of proteins and amino acids. Adv Protein Chem 1962;17:303-390.
6. Balestrieri C, Colonna G, Giovane A, Irace G, Servillo L. Second-derivative spectroscopy of proteins: studies on tyrosyl residues. Anal Biochem 1980;106(1):49-54.
7. Gemmill CL. The effects of iodine on the ultraviolet absorption spectra of thyroglobulin, casein, and insulin. Arch Biochem Biophys 1956;63:192-200.
8. Thompson EOP. Modification of tyrosine during performic acid oxidation. Biochim Biophys Acta 1954;15:440-441.
9. Raven DJ, Earland C, Littler M. Occurrence of dityrosine in Tussah silk fibroin and keratin. Biochim Biophys Acta, Protein Struct 1971;251(1):96-99.
10. LaBella FS, Keeley FW, Vivian S, Thornhill DP. Evidence for dityrosine in elastin. Biochem Biophys Res Commun 1967;26(6):748-753.
11. Waykole P, Heidemann E. Dityrosine in collagen. Connect Tissue Res 1976;4(4): 219-222.
12. Harms GS, Pauls SW, Hedstrom JF, Johnson CK. Fluorescence and rotational dynamics of dityrosine. J Fluoresc 1997;7(4):283-292.
13. Rosenheck K, Doty P. The far-ultraviolet absorption spectra of polypeptide and protein solutions and their dependence on conformation. Proc Natl Acad Sci U S A 1961;47:1775-1785.
14. McGlynn SP, Chaudhuri JN, Good M. Possible effect of charge transfer complexation on the dihedral angle of dialkyl disulfides. J Am Chem Soc 1962;84:9-12.
15. Favilla R, Goldoni M, Del Signore F, Di Muro P, Salvato B, Beltramini M. Guanidinium chloride induced unfolding of a hemocyanin subunit from Carcinus aestuarii II. Holo form. Biochim Biophys Acta Protein Struct Mol Enzymol 2002;1597(1):51-59.
16. Vergani L, Grattarola M, Dondero F, Viarengo A. Expression, purification, and characterization of metallothionein-A from rainbow trout. Protein Expr Purif 2003;27(2):338-345.
17. Burke CJ, Sanyal G, Bruner MW, Ryan JA, LaFemina RL, Robbins HL, Zeft AS, Middaugh CR, Cordingley MG. Structural implications of spectroscopic characterization of a putative zinc finger peptide from HIV-1 integrase. J Biol Chem 1992;267(14):9639-9644.
18. Inouye H, Kirschner DA. Alzheimer's ß-amyloid: insights into fibril formation and structure from congo red binding. Subcell Biochem 2005;38:203-224. (Alzheimer's disease: cellular and molecular aspects of amyloid ß).
19. Inouye H, Kirschner DA. Aß fibrillogenesis: kinetic parameters for fibril formation from Congo Red binding. J Struct Biol 2000;130(2/3):123-129.
20. Maskevich AA, Stsiapura VI, Kuzmitsky VA, Kuznetsova IM, Povarova OI, Uversky VN, Turoverov KK. Spectral properties of thioflavin T in solvents with different dielectric properties and in a fibril-incorporated form. J Proteome Res 2007;6(4):1392-1401.
21. Luong TN, Kirsch JF. A continuous coupled spectrophotometric assay for tyrosine aminotransferase activity with aromatic and other nonpolar amino acids. Anal Biochem 1997;253(1):46-49.
22. Piersma SR, Visser AJWG, de Vries S, Duine JA. Optical spectroscopy of nicotinoprotein alcohol dehydrogenase from Amycolatopsis methanolica: a comparison with horse liver alcohol dehydrogenase and UDP-galactose epimerase. Biochemistry 1998;37(9):3068-3077.
23. Lucas LH, Ersoy BA, Kueltzo LA, Joshi SB, Brandau DT, Thyagarajapuram N, Peek LJ, Middaugh CR. Probing protein structure and dynamics by secondderivative ultraviolet absorption analysis of cation-p interactions. Protein Sci 2006;15(10):2228-2243.
24. Ichikawa T, Terada H. Estimation of state and amount of phenylalanine residues in proteins by second derivative spectrophotometry. Biochim Biophys Acta Protein Struct 1979;580(1):120-128.
25. Mach H, Volkin DB, Burke CJ, Middaugh CR. Ultraviolet absorption spectroscopy. Methods Mol Biol 1995;40:91-114. Totowa (NJ), USA.
26. Mach H, Sanyal G, Volkin DB, Middaugh CR. Applications of ultraviolet absorption spectroscopy to the analysis of biopharmaceuticals. Therapeutic protein and peptide formulation and delivery, ACS Symposium Series, No. 675.Washington (DC): ACS Publications; 1997. pp. 186-205.
27. Balestrieri C, Colonna G, Giovane A, Irace G, Servillo L. Second-derivative spectroscopy of proteins. A method for the quantitative determination of aromatic amino acids in proteins. Eur J Biochem 1978;90(3):433-440.
28. Servillo L, Colonna G, Balestrieri C, Ragone R, Irace G. Simultaneous determination of tyrosine and tryptophan residues in proteins by second-derivative spectroscopy. Anal Biochem 1982;126(2):251-257.
29. Brandts JF. The thermodynamics of protein denaturation. I. The denaturation of chymotrypsinogen. J Am Chem Soc 1964;86(20):4291-4301.
30. Brandts JF. The thermodynamics of protein denaturation. II. A model of reversible denaturation and interpretations regarding the stability of chymotrypsinogen. J Am Chem Soc 1964;86(20):4302-4314.
31. Hayashi K, Imoto T, Funatsu M. The enzyme-substrate complex in a muramidase-catalyzed reaction. I. Difference spectrum of the complex. J Biochem 1963;54(5):381-387. (Tokyo, Japan).
32. Ray A, Reynolds JA, Polet H, Steinhardt J. Binding of large organic anions and neutral molecules by native bovine serum albumin. Biochemistry 1966;5(8):2606-2616.
33. Donovan JW. Changes in ultraviolet absorption produced by alteration of protein conformation. J Biol Chem 1969;244(8):1961-1967.
34. Chervenka CH. Ultraviolet spectral changes related to the enzymic activity of chymotrypsin. Biochem Biophys Acta 1959;31:85-95.
35. Bailey JE, Beaven GH, Chignell DA, Gratzer WB. Analysis of perturbations in the ultraviolet absorption spectra of proteins and model compounds. Eur J Biochem 1968;7(1):5-14.
36. Kornblatt JA, Kornblatt MJ, Lange R, Mombelli E, Guillemette JG. The individual tyrosines of proteins: their spectra may or may not differ from those in water or other solvents. Biochim Biophys Acta Protein Struct Mol Enzymol 1999;1431(1):238-248.
37. Herskovits T, Laskowski M Jr. Location of chromophoric residues in proteins by solvent perturbation. I. Tyrosyls in serum albumins. J Biol Chem 1962;237:2481-2492.
38. De Young LR, Dill KA, Fink AL. Aggregation and denaturation of apomyoglobin in aqueous urea solutions. Biochemistry 1993;32(15):3877-3886.
39. Stigter D, Dill KA. Theory for protein solubilities. Fluid Phase Equilib 1993; 82:237-249.
40. Fields GB, Alonso DOV, Stigter D, Dill KA. Theory for the aggregation of proteins and copolymers. J Phys Chem 1992;96(10):3974-3981.
41. Fink AL. Protein aggregation: folding aggregates, inclusion bodies and amyloid. Fold Des 1998;3(1): R9-R23.
42. Kueltzo LA, Middaugh CR. Ultraviolet absorption spectroscopy. Biotechnol: Pharm Aspects 2005;3:1-25. (Methods for Structural Analysis of Protein Pharmaceuticals).
43. Lange R, Balny C. UV-visible derivative spectroscopy under high pressure. Biochem Biophys Acta Protein Struct Mol Enzymol 2002;1595(1-2):80-93.
44. Kueltzo LA, Ersoy B, Ralston JP, Middaugh CR. Derivative absorbance spectroscopy and protein phase diagrams as tools for comprehensive protein characterization: a bGCSF case study. J Pharm Sci 2003;92:1805-1820.
45. Fan H, Vitharana SN, Chen T, O'Keefe D, Middaugh CR. Effects of pH and polyanions on the thermal stability of fibroblast growth factor 20. Mol Pharm 2007;4:232-240.
46. Fan H, Kashi RS, Middaugh CR. Conformational lability of two molecular chaperones Hsc70 and GP96: effects of pH and temperature. Arch Biochem Biophys 2006;447:34-45.
47. Fan H, Ralston J, DiBase M, Faulkner E, Middaugh CR. Solution behavior of IFN- ß-1a: an empirical phase diagram based approach. J Pharm Sci 2005;94:1893-1911.
48. Fan H, Li H, Zhang M, Middaugh CR. Effects of solutes on empirical phase diagrams of human fibroblast growth factor 1. J Pharm Sci 2007;96:1490-1503.
49. Esfandiary R, Kickhoefer VA, Rome LH, Joshi SB, Middaugh CR. Structural stability of vault particles. J Pharm Sci 2009;98(4):1376-1386.
50. Peek LJ, Brey RN, Middaugh CR. A rapid, three-step process for the preformulation of a recombinant ricin toxin A-chain vaccine. J Pharm Sci 2007;96:44-60.
51. Brandau DT, Joshi SB, Smalter AM, Kim S, Steadman B, Middaugh CR. Stability of the Clostridium botulinum type A neurotoxin complex: an empirical phase diagram based approach. Mol Pharm 2007;4:571-582.
52. Ausar SF, Rexroad J, Frolov VG, Look JL, Konar N, Middaugh CR. Analysis of the thermal and pH stability of human respiratory syncytial virus. Mol Pharm 2005;2:491-499.
53. Ausar SF, Foubert TR, Hudson MH, Vedvick TS, Middaugh CR. Conformational stability and disassembly of Norwalk virus like particles: effect of pH and temperature. J Biol Chem 2006;281:19478-19488.
54. Harn N, Allan C, Oliver C, Middaugh CR. Highly concentrated monoclonal antibodies: direct analysis of structure and stability. J Pharm Sci 2007;96:532-546.
55. Peek LJ, Brandau DT, Jones LS, Joshi SB, Middaugh CR. A systematic approach to stabilizing EBA-175 RII-NG for use as a malaria vaccine. Vaccine 2006;24:5839-5851.
56. Rexroad J, Martin TT, McNeilly D, Godwin S, Middaugh CR. Thermal stability of adenovirus type 2 as a function of pH. J Pharm Sci 2006;95:1469-1479.
57. Rexroad J, Evans RK, Middaugh CR. Effect of pH and ionic strength on the physical stability of adenovirus type 5. J Pharm Sci 2006;95:237-247.
58. Ruponen M, Braun CS, Middaugh CR. Biophysical characterization of polymeric and liposomal gene delivery systems using empirical phase diagrams. J Pharm Sci 2006;95:2101-2114.
59. Thyagrajapuram N, Olsen D, Middaugh CR. The structure stability and complex behavior of recombinant human gelatins. J Pharm Sci 2007;96:3363-3378.
60. Guo J, Harn N, Robbins A, Dougherty R, Middaugh CR. Stability of helix-rich proteins at high concentrations. Biochemistry 2006;45(28):8686-8696.
61. Harn N, Allan C, Oliver C, Middaugh CR. Highly concentrated monoclonal antibody solutions: direct analysis of physical structure and thermal stability. J Pharm Sci 2007;96(3):532-546.
62. Kamerzell TJ, Middaugh CR. The complex inter-relationships between protein flexibility and stability. J Pharm Sci 2008;97(9):3494-3517.
63. Esfandiary R, Hunjan JS, Lushington GH, Joshi SB, Middaugh CR. Temperature dependent 2nd derivative absorbance spectroscopy of aromatic amino acids as a probe of protein dynamics. Protein Sci 2009;18(12):2603-2614.
64. Dwyer JJ, Gittis AG, Karp DA, Lattman EE, Spencer DS, Stites WE, Garcia-Moreno E B. High apparent dielectric constants in the interior of a protein reflect water penetration. Biophys J 2000;79(3):1610-1620.
65. Wang W, Wang YJ, Wang DQ. Dual effects of Tween 80 on protein stability. Int J Pharm 2008;347(1-2):31-38.
66. Adachi K, Asakura T. Nucleation-controlled aggregation of deoxyhemoglobin S. Possible difference in the size of nuclei in different phosphate concentrations. J Biol Chem 1979;254(16):7765-7771.
67. Wegner A, Savko P. Fragmentation of actin filaments. Biochemistry 1982;21(8):1909-1913.
68. Murphy R, Tsai A Misbehaving proteins: protein (mis) folding, aggregation, and stability. New York (NY): Springer Science; 2006.
69. Eberlein GA, Stratton PR, Wang YJ. Stability of rhbFGF as determined by UV spectroscopic measurements of turbidity. PDA J Pharm Sci Technol 1994;48(5):224-230.
70. MacLean DS, Qian Q, Middaugh CR. Stabilization of proteins by low molecular weight multi-ions. J Pharm Sci 2002;91(10):2220-2229.
71. Middaugh CR, Kehoe JM, Prystowsky MB, Gerber-Jenson B, Jenson JC, Litman GW. Molecular basis for the temperature-dependent insolubility of cryoglobulins. IV. Structural studies of the IgM monoclonal cryoglobulin McE. Immunochemistry 1978;15(3):171-187.
72. Kim Y-S, Randolph TW, Seefeldt MB, Carpenter JF. High-pressure studies on protein aggregates and amyloid fibrils. Methods Enzymol 2006;413:237-253. (Amyloid, Prions, and Other Protein Aggregates, Part C).
73. Jones LS, Kaufmann A, Middaugh CR. Silicone oil induced aggregation of proteins. J Pharm Sci 2005;94(4):918-927.
74. Jiang G, Joshi SB, Peek LJ, Brandau DT, Huang CR, Ferriter MS, Woodley WD, Ford BM, Mar KD, Mikszta JA, Hwang CR, Ulrich R, Harvey NG, Middaugh CR, Sullivan VJ. Anthrax vaccine powder formulations for nasal mucosal delivery. J Pharm Sci 2006;95:80-96.
75. Kissmann J, Ausar SF, Foubert TR, Brock J, Switzer MH, Detzi EJ, Vedvick TS, Middaugh CR. Physical stabilization of Norwalk virus-like particles. J Pharm Sci 2008;97(10):4208-4218.
76. Ausar SF, Espina M, Brock J, Thyagarayapuran N, Repetto R, Khandke L, Middaugh CR. High-throughput screening of stabilizers for respiratory syncytial virus: identification of stabilizers and their effects on the conformational thermostability of viral particles. Hum Vaccines 2007;3(3):94-103.
77. Fan H, Vitharana SN, Chen T, O'Keefe D, Middaugh CR. Effects of pH and polyanions on the thermal stability of fibroblast growth factor 20. Mol Pharm 2007;4(2):232-240.
78. Salnikova MS, Joshi SB, Rytting JH, Warny M, Middaugh CR. Physical characterization of clostridium difficile toxins and toxoids: effect of the formaldehyde crosslinking on thermal stability. J Pharm Sci 2008;97(9):3735-3752.
79. Murphy RM. Kinetics of amyloid formation and membrane interaction with amyloidogenic proteins. Biochim Biophys Acta Biomembr 2007;1768(8):1923-1934.
80. Kim Y-S, Cape SP, Chi E, Raffen R, Wilkins-Stevens P, Stevens FJ, Manning MC, Randolph TW, Solomon A, Carpenter JF. Counteracting effects of renal solutes on amyloid fibril formation by immunoglobulin light chains. J Biol Chem 2001;276(2):1626-1633.
81. Hamada D, Dobson CM. A kinetic study of ß-lactoglobulin amyloid fibril formation promoted by urea. Protein Sci 2002;11(10):2417-2426.
82. Come JH, Fraser PE, Lansbury PT Jr. A kinetic model for amyloid formation in the prion diseases: importance of seeding. Proc Natl Acad Sci U S A 1993;90(13):5959-5963.
83. Zurdo J, Guijarro JI, Jimenez JL, Saibil HR, Dobson CM. Dependence on solution conditions of aggregation and amyloid formation by an SH3 domain. J Mol Biol 2001;311(2):325-340.
84. Morris AM, Watzky MA, Agar JN, Finke RG. Fitting neurological protein aggregation kinetic data via a 2-step, minimal/"Ockham's razor" model: the Finke-Watzky mechanism of nucleation followed by autocatalytic surface growth. Biochemistry 2008;47(8):2413-2427.
85. Jarrett JT, Lansbury PT Jr. Seeding "one-dimensional crystallization" of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie? Cell 1993; 73(6):1055-1058.
86. Hofrichter J, Ross PD, Eaton WA. Kinetics and mechanism of deoxyhemoglobin S gelation. New approach to understanding sickle cell disease. Proc Natl Acad Sci U S A 1974;71(12):4864-4868.
87. Hofrichter J, Ross PD, Eaton WA. Supersaturation in sickle cell hemoglobin solutions. Proc Natl Acad Sci U S A 1976;73(9):3035-3039.
88. Cellmer T, Douma R, Huebner A, Prausnitz J, Blanch H. Kinetic studies of protein L aggregation and disaggregation. Biophys Chem 2007;125(2-3):350-359.
89. Kodaka M. Interpretation of concentration-dependence in aggregation kinetics. Biophys Chem 2004;109(2):325-332.
90. Andrews JM, Weiss WF, Roberts CJ IV. Nucleation, growth, and activation energies for seeded and unseeded aggregation of a-chymotrypsinogen A. Biochemistry 2008;47(8):2397-2403.
91. Wood SJ, Wypych J, Steavenson S, Louis J-C, Citron M, Biere AL. a-Synuclein fibrillogenesis is nucleation-dependent. Implications for the pathogenesis of Parkinson's disease. J Biol Chem 1999;274(28):19509-19512.
92. Roberts CJ. Non-native protein aggregation kinetics. Biotechnol Bioeng 2007;98(5):927-938.
93. Woody AYM, Reisbig RR, Woody RW. Spectroscopic studies of Congo Red binding to RNA polymerase. Biochim Biophys Acta Nucleic Acids Protein Synth 1981;655(1):82-88.
94. Edwards RA, Woody RW. Spectroscopic studies of Cibacron Blue and Congo Red bound to dehydrogenases and kinases. Evaluation of dyes as probes of the dinucleotide fold. Biochemistry 1979;18(23):5197-5204.
95. Quenin I, Henrissat B. Precipitation and crystallization of cellulose doped with dyes. Makromol Chem Rapid Commun 1985;6(11):737-741.
96. Tan OT, Faris B, Franzblau C. Aortic elastin fluorescence after in vivo labeling with Congo Red. J Fluoresc 1991;1(2):147-151.
97. Bartnicki-Garcia S, Persson J, Chanzy H. An electron microscope and electron diffraction study of the effect of calcofluor and Congo red on the biosynthesis of chitin in vitro. Arch Biochem Biophys 1994;310(1):6-15.
98. Ojala WH, Ojala CR, Gleason WB. The X-ray crystal structure of the sulfonated azo dye Congo Red, a non-peptidic inhibitor of HIV-1 protease which also binds to reverse transcriptase and amyloid proteins. Antivir Chem Chemother 1995;6(1):25-33.
99. Timasheff SN. Turbidity as a criterion of coagulation. J Colloid Interface Sci 1966;21(5):489-497.
100. Duysens LNM. Flattening of the absorption spectrum of suspensions, as compared to that of solutions. Biochim Biophys Acta 1956;19:1-12.
101. Schneider AS, Harmatz D. An experimental method correcting for absorption flattening and scattering in suspensions of absorbing particles: circular dichroism and absorption spectra of hemoglobin in situ in red blood cells. Biochemistry 1976;15(19):4158-4162.
102. Jones LS, Bam NB, Randolph TW. Surfactant-stabilized protein formulations: a review of protein-surfactant interactions and novel analytical methodologies. Therapeutic protein and peptide formulation and delivery, ACS Symposium Series, No. 675. Washington (DC): ACS Publications;1997. pp. 206-222.
103. Kuwajima K. The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure. Proteins 1989;6:87-103.