Structural changes of protein antigens due to adsorption onto and release from aluminium hydroxide using FTIR-ATR

Spectroscopy

Volumn 21, Issue 4, 2007, Pages 211-226

  Zheng, Yiwu ^a,b   Lai, Xuxin ^a,b   Ipsen, Henrik ^a   Larsen, Jørgen Nedergaard ^a   Løwenstein, Henning ^a   Søndergaard, Ib ^b   Jacobsen, Susanne ^b  

^a ALK ABELLÓ   (Denmark)

^b TECHNICAL UNIVERSITY OF DENMARK   (Denmark)

Author keywords

Aluminium hydroxide; Antigen; FTIR ATR; Secondary structure

Indexed keywords

ADSORPTION; ALUMINUM COMPOUNDS; ANTIGENS; FOURIER TRANSFORMS; IMMUNOLOGY; INFRARED RADIATION; VACCINES;

ALUMINIUM HYDROXIDE; SECONDARY STRUCTURE; SERUM ALBUMIN;

PROTEINS;

ALUMINUM HYDROXIDE; BETA LACTOGLOBULIN; BOVINE SERUM ALBUMIN; PHOSPHATE BUFFERED SALINE;

ADSORPTION; ANTIGEN STRUCTURE; ARTICLE; CIRCULAR DICHROISM; CONCENTRATION RESPONSE; DRUG RELEASE; INFRARED SPECTROSCOPY; PH; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE;

EID: 35348874764     PISSN: 07124813     EISSN: None     Source Type: Journal    
DOI: 10.1155/2007/354051     Document Type: Article

References (45)

1. R.A. Goldsby, T. Kindt and B.A. Osborne, Immunology, 4th edn, W.H. Freeman and Company, New York, 2001, pp. 63-65.
2. C. Schoneich, M.J. Hageman and R.T. Borchardt, Stability of peptides and proteins, in: Controlled Drug Delivery, Challenges and strategies, K. Park, ed., American Chemical Society, Washington, DC, 1997, pp. 205-228.
3. M.C. Manning, K. Patel and R.T. Borchardt, Stability of protein pharmaceuticals, Pharm. Res. 6 (1989), 903-918.
4. K. Fu, K. Greibenow, L. Hsieh, A.M. Klibanov and R. Langer, Use of FTIR spectroscopy to characterize the secondary structure of proteins encapsulated with PLGA microspheres, J. Con. Rel. 58 (1999), 357-366.
5. T.H. Yang, A. Dong, J. Meyer, O.L. Johnson, J. Cleland and J.F. Carpenter, Use of infrared spectroscopy to assess secondary structure of human growth hormone within biodegradable microspheres, J. Pharm. Sci. 88 (1999), 161-165.
6. C. Castelain and C. Genot, Conformational changes of bovine serum albumin upon its adsorption in dodecane-in-water emulsions as revealed by front-face steady-state fluorescence, Biochim. Biophys. Acta 1199 (1994), 59-64.
7. D. Kowalczyk, S. Slomkowski and F.W. Wang, Changes in conformation of human serum albumin and gamma globulins upon adsorption to polystyrene and poly latexes: Studies by fluorescence spectroscopy, J. Bioact. Compat. Polym. 9 (1994), 282-309.
8. M.C.L. Maste, W. Norde and A.J.W.G. Visser, Adsorption-induced conformational changes in the serine proteinase sannase: A tryptophan fluorescence and circular dichroism study, J. Colloid Interface Sci. 196 (1997), 224-230.
9. S.L. Hem and J.L. White, Characterization of aluminium hydroxide for use as an adjuvant in parenteral vaccines, J. Parent. Sci. Techn. 38 (1984), 2-10.
10. L.S. Jones, L.J. Peek, J. Power, A. Marham, B. Yazzie and C.R. Middaugh, Effects of adsorption to aluminium salt adjuvants on the structure and stability of model protein antigens, J. Biol. Chem. 280 (2005), 13406-13414.
11. A. Dong, L.S. Jones, B.A. Kerwin, S. Krishnan and J.F. Carpenter, Secondary structures of proteins adsorbed onto aluminium hydroxide adjuvant: infrared spectroscopic analysis of proteins from low solution concentrations, Anal. Biochem. 351 (2006), 282-289.
12. A. Barth and C. Zscherp, What vibrations tell us about proteins, Q. Rev. Biophys. 35 (2002), 369-430.
13. P.I. Haris, Theory and basic principles - 3. Fourier transform infrared spectroscopic studies of peptides: potentials and pitfalls, ACS Symp. Ser. 750 (2000), 54-95.
14. J.S. Sharp, J.A. Forrest and R.A.L. Jones, Surface denaturation and amyloid fibril formation of insulin at model lipid-water interface, Biochemistry 41 (2002), 15810-15819.
15. C.E. Giacomelli, M.G.E.G. Bremer and W. Norde, ATR-FTIR study of IgG adsorbed on different silica surface, J. Colloid Interface Sci. 220 (1999), 13-23.
16. Y.I. Tarasevich and L.I. Monakhova, Interaction between globular proteins and silica surfaces, Colloid J. 64 (2002), 482-487.
17. P.M. Bummer, An FTIR study of the structure of human serum albumin adsorbed to polysulfone, Int. J. Pharm. 132 (1996), 143-151.
18. K.K. Chittur, FTIR/ATR for protein adsorption to biomaterial surfaces, Biomaterials 19 (1998), 357-369.
19. P.I. Haris and F. Seveercan, FTIR spectroscopic characterization of protein structure in aqueous and non-aqueous media, J. Mol. Catal. B: Enzym. 7 (1999), 207-221.
20. H.H. Mantsch, A. Perczel, M. Hollosi and G.D. Fasman, Characterization of beta-turns in cyclic hexapeptides in solution by Fourier-transform IR spectroscopy, Biopolymers 33 (1993), 201-207.
21. L.K. Tamm and S.A. Tatulian, Infrared spectroscopy of proteins and peptides in lipids bilayers, Q. Rev. Biophys. 30 (1997), 365-429.
22. J.O. Speare and T.S. Rush, IR spectra of cytochrome C denatured with deuterated guanidine hydrochloride show increase in β sheet, Biopolymers 72 (2003), 193-204.
23. D.J. Lacey, N. Wellner, F. Beaudoin, J.A. Napier and P.R. Shewry, Secondary structure of oleosins in oil bodies isolated from seeds of safflower (Carthamus tinctorius L.) and sunflower (Helianthus annuus L.), Biochem. J. 334 (1998), 469-477.
24. S. Krimm and J. Bandekar, Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins, Adv. Protein Chem. 38 (1986), 181-364.
25. R. Itri, W. Caetano, L.R.S. Barbosa and M.S. Baptista, Effect of urea on bovine serum albumin in aqueous and reverse micelle environments investigated by small angle X-ray scattering, fluorescence and circular dichroism, Braz. J. Phys. 34 (2004), 58-63.
26. N. Kossovsky, A. Nguyen, K. Sukiassians, A. Festekjian, A. Gelman and E. Sponesler, Secondary structure of albumin acquired rapidly by modified conventional ATR-FTIR is comparable to CD spectral data, J. Colloid Interface Sci. 166 (1994), 350-355.
27. J. Liu, J.L. Feldkamp, J.L. White and S.L. Hem, Adsorption of phosphate by aluminium hydroxycarbonate, J. Pharm. Sci. 10 (1984), 1355-1358.
28. P. Robert, M.F. Devaux, N. Mouhous and E. Dufour, Monitoring the secondary structure of proteins by near infrared spectroscopy, Appl. Spectrosc. 53 (1999), 226-232.
29. N.S. Servagent, M. Revault, H. Quiquampoix and M.H. Baron, Conformational changes of bovine serum albumin induced by adsorption on different clay surfaces: FTIR analysis, J. Colloid Interface Sci. 221 (2000), 272-283.
30. L. Sawyer, G. Kontopidis and S.Y. Wu, β-Lactoglobulin - A three-dimensional perspective, Int. J. Food Sci. Technol. 34 (1999), 409-418.
31. T. Lefevre and M. Subirade, Interaction of β-lactoglobulin with phospholipids bilayers: a molecular level elucidation as revealed by infrared spectroscopy, Int. J. Biol. Macromol. 28 (2000), 59-67.
32. T.J. Lenk, Infrared studies of protein adsorption and transitions on polyurethanes, PhD dissertation, University of Washington Chemical Engineering, 1994.
33. C. Schladitz, E.P. Vieira, H. Hermel and H. Mohrwald, Amyloid-β-sheet formation at the air-water interface, Biophysics 77 (1999), 3305-3310.
34. B.S. Kendrick, J.L. Cleland, X. Lam, T. Nguyen, T.W. Randolph, M.C. Manning and J.F. Carpenter, Aggregation of recombinant human interferon gamma: kinetics and structural transitions, J. Pharm. Sci. 87 (1998), 1069-1076.
35. A. Dong, S.J. Prestrelski, S.D. Allison and J.F. Carpenter, Infrared spectroscopy studies of lyophilization- and temperature-induced protein aggregation, J. Pharm. Sci. 84 (1995), 415-424.
36. T. Lefevre and M. Subirade, Conformational rearrangement of β-lactoglobulin upon interaction with an anionic membrane, Biochim. Biophys. Acta 1549 (2001), 37-50.
37. H. Urano and S. Fukuzaki, Conformation of adsorbed bovine serum albumin governing its desorption behavior at alumina-water interfaces, J. Biosci. Bioeng. 90 (2000), 105-111.
38. S. Hajra and D.K. Chattoraj, Protein adsorption at solid-liquid interfaces: part II - adsorption from binary protein mixture, Indian J. Biochem. Biophys. 2 (1991), 124-132.
39. J. Xie, C. Riley, M. Kumar and K. Chittur, FTIR/ATR study of protein adsorption and brushite transformation to hydroxyappatite, Biomaterials 23 (2002), 3609-3616.
40. W. Norde, Behavior of proteins at interfaces, with special attention to the role of the structure stability of the protein molecule, Clin. Mater. 11 (1992), 85-90.
41. K.A. Oberg and A.L. Fink, A new attenuated total reflectance Fourier transform infrared spectroscopy method for the study of proteins in solution, Anal. Biochem. 256 (1988), 92-106.
42. M. van de Weet, W.E. Hennink and W. Jiskoot, Protein instability in poly(lactic-co-glycolic acid) microparticles, Pharm. Res. 17 (2000), 1159-1167.
43. J.L. Cleland, M.F. Powell and S.J. Shire, The development of stable protein formulations: a close look at protein aggregation, deamidation, and oxidation, Crit. Rev. Ther. Drug 10 (1993), 307-377.
44. J.V. Rinella, R.F. Workman, J.L. White and S.L. Hem, Elutability of proteins from aluminium-containing vaccine adjuvants by treatment with surfactants, J. Colloid Interface Sci. 197 (1998), 48-56.
45. M.F.M. Engel, A.J.W.G. Visser and C.P.M. Mierlo, Refolding of adsorbed bovine α-lactalbumin during surfactant induced displacement from a hydrophobic interface, Langmuir 7 (2003), 2929-2937.