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Characterization of Adsorbed Protein Films by Time-of-Flight Secondary Ion Mass Spectrometry with Principal Component Analysis

Wagner, M. S., Castner, David G.·2001·Langmuir

Abstract

Characterization of the adsorbed protein film that forms upon implantation of a biomedical device is a long-standing interest in biomaterials research. Time-of-flight secondary ion mass spectrometry (ToF−SIMS) is a powerful method for the characterization of adsorbed proteins on biomaterial surfaces due to its chemical specificity and surface sensitivity. However, the SIMS fragmentation patterns for proteins are quite complex due to the heterogeneity of the protein sequence. Therefore, the multivariate analysis technique principal components analysis (PCA) was used to obtain a more detailed interpretation of the protein SIMS spectra. This study utilizes single component adsorbed protein films on three model substrates and multivariate analysis of the ToF−SIMS data to determine the identity of protein films. Furthermore, ToF−SIMS and PCA were used to give insight into the composition of a 1% bovine plasma protein film. The single component spectra from 13 different proteins were readily distinguishable using PCA. The major component of the 1% bovine plasma film was found to shift from fibrinogen to γ-globulins over the course of 2 h, in agreement with the current literature. This study shows how combination of ToF−SIMS and PCA provides new insights into the composition of adsorbed protein films on biomaterial surfaces.

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Research works printed but not linked: 73

  1. Baier R. E., 1969, J. Biomed. Mater. Res., 3, 191, 10.1002/jbm.820030115 · DOI · Paper page
  2. An Y. H., 1998, J. Biomed. Mater. Res., 43, 338, 10.1002/(SICI)1097-4636(199823)43:3<338::AID-JBM16>3.0.CO;2-B · DOI · Paper page
  3. Bryers J. D., 1994, Colloids Surf. B, 2, 9, 10.1016/0927-7765(94)80013-8 · DOI
  4. Rudnicka W., 1997, FEMS Immunol. Med. Microbiol., 19, 7, 10.1111/j.1574-695X.1997.tb01067.x · doi:10.1111/j.1574-695x.1997.tb01067.x
  5. Vasin S. L., 1998, J. Biomed. Mater. Res., 39, 491, 10.1002/(SICI)1097-4636(19980305)39:3<491::AID-JBM21>3.0.CO;2-C · DOI
  6. Ertel S. I., 1994, J. Biomed. Mater. Res., 28, 667, 10.1002/jbm.820280603 · DOI
  7. Gristina A. G., 1987, Science, 237, 1588, 10.1126/science.3629258 · DOI · Paper page
  8. Horbett T. A., 1994, Colloids Surf. B, 2, 225, 10.1016/0927-7765(94)80037-5 · DOI · Paper page
  9. Thomas C. H., 1997, J. Biomed. Mater. Res., 37, 81, 10.1002/(SICI)1097-4636(199710)37:1<81::AID-JBM10>3.0.CO;2-T · DOI
  10. Kao, W. J.; Hubbel, J. A.; Anderson, J. M.J. Mater. Sci. Mater. Med.1999,10, 601. · DOI
  11. Montanaro L., 1999, Biomaterials, 20, 1945, 10.1016/S0142-9612(99)00099-X · DOI
  12. McDevitt D., 1997, Eur. J. Biochem., 247, 416, 10.1111/j.1432-1033.1997.00416.x · DOI · Paper page
  13. Yu J.-L., 1997, FEMS Immunol. Med. Microbiol., 19, 247, 10.1111/j.1574-695X.1997.tb01094.x · doi:10.1111/j.1574-695x.1997.tb01094.x
  14. Lundberg F., 1997, Infect. Immun., 65, 897, 10.1128/iai.65.3.897-902.1997 · doi:10.1128/iai.65.3.897-902.1997
  15. Lopez G. P., 1992, J. Biomed. Mater. Res., 26, 415, 10.1002/jbm.820260402 · DOI · Paper page
  16. Sheu M.-S., 1993, Clin. Mater., 13, 41, 10.1016/0267-6605(93)90088-O · doi:10.1016/0267-6605(93)90088-o
  17. Sheu M.-S., 1993, J. Adhes. Sci. Technol., 7, 1065, 10.1163/156856193X00583 · doi:10.1163/156856193x00583
  18. Morra M., 1993, Clin. Mater., 14, 255, 10.1016/0267-6605(93)90010-5 · DOI
  19. Deng L., 1996, J. Am. Chem. Soc., 118, 5136, 10.1021/ja960461d · doi:10.1021/ja960461d
  20. Favia P., 1998, Surf. Coat. Technol., 98, 1102, 10.1016/S0257-8972(97)00285-5 · DOI
  21. Harder P., 1998, J. Phys. Chem. B, 102, 426, 10.1021/jp972635z · DOI · Paper page
  22. Boeckl M., 1998, Biopolymers, 47, 185, 10.1002/(SICI)1097-0282(1998)47:2<185::AID-BIP8>3.0.CO;2-Q · doi:10.1002/(sici)1097-0282(1998)47:2<185::aid-bip8>3.0.co;2-q
  23. Bohnert J. L., 1990, J. Biomater. Sci. Polym. Ed., 1, 279, 10.1163/156856289X00154 · doi:10.1163/156856289x00154
  24. Kiaei D., 1992, J. Biomater. Sci. Polym. Ed., 4, 35, 10.1163/156856292X00286 · doi:10.1163/156856292x00286
  25. Shi H., 1999, Nature, 398, 593, 10.1038/19267 · DOI · Paper page
  26. Siedlecki C. A., 1998, Biomaterials, 19, 441, 10.1016/S0142-9612(97)00222-6 · DOI
  27. Elwing H., 1998, Biomaterials, 19, 397, 10.1016/S0142-9612(97)00112-9 · DOI · Paper page
  28. Chittur K. K., 1998, Biomaterials, 19, 357, 10.1016/S0142-9612(97)00223-8 · DOI · Paper page
  29. Ratner B. D., 1994, Colloids Surf. B, 2, 333, 10.1016/0927-7765(94)80048-0 · DOI
  30. Ratner B. D., 1995, Surf. Interface Anal., 23, 521, 10.1002/sia.740230712 · DOI
  31. Chittur K. K., 1998, Biomaterials, 19, 301, 10.1016/S0142-9612(97)00107-5 · DOI
  32. Paynter R. W., 1984, J. Colloid Interface Sci., 191, 233, 10.1016/0021-9797(84)90023-7 · doi:10.1016/0021-9797(84)90023-7
  33. Paynter R. W., 1985, Surface and Interfacial Aspects of Biomedical Polymers
  34. Chowdhury P. B., 1998, Colloids Surf. A, 143, 53, 10.1016/S0927-7757(98)00408-7 · DOI
  35. Mantus D. S., 1993, Anal. Chem., 65, 1431, 10.1021/ac00058a021 · doi:10.1021/ac00058a021
  36. Benninghoven A., 1993, Anal. Chem., 65, 630A, 10.1021/ac00062a717 · doi:10.1021/ac00062a717
  37. Ratner B. D., 1992, Clin. Mater., 11, 25, 10.1016/0267-6605(92)90027-Q · doi:10.1016/0267-6605(92)90027-q
  38. Ratner B. D., 1993, Clin. Mater., 13, 71, 10.1016/0267-6605(93)90093-M · DOI
  39. Leonard D., 1999, Fresenius J. Anal. Chem., 365, 3, 10.1007/s002160051437 · doi:10.1007/s002160051437
  40. John C. M., 1997, Int. J. Mass Spectrom. Ion Processes, 161, 47, 10.1016/S0168-1176(96)04505-3 · doi:10.1016/s0168-1176(96)04505-3
  41. Ratner B. D., Fifth World Biomaterials Conference; Toronto
  42. Ratner B. D., 1996, Polym. Prepr. (Am. Chem. Soc., Div. Polym. Chem.), 37, 843
  43. Colliver T. L., 1997, Anal. Chem., 69, 2225, 10.1021/ac9701748 · DOI · Paper page
  44. Clerc J., 1997, Cell Biol. Inter., 21, 619, 10.1006/cbir.1998.0205 · doi:10.1006/cbir.1998.0205
  45. Fourre C., 1997, J. Anal. At. Spectrom., 12, 1105, 10.1039/A700777I · doi:10.1039/a700777i
  46. Kargacin M. E., 1986, Anal. Chem., 58, 2300, 10.1021/ac00124a041 · doi:10.1021/ac00124a041
  47. Ohrlund A., 1997, Surf. Interface Anal., 25, 105, 10.1002/(SICI)1096-9918(199702)25:2<105::AID-SIA213>3.0.CO;2-R · doi:10.1002/(sici)1096-9918(199702)25:2<105::aid-sia213>3.0.co;2-r
  48. Vanden-Eynde X., 1997, Surf. Interface Anal., 25, 878, 10.1002/(SICI)1096-9918(199710)25:11<878::AID-SIA311>3.0.CO;2-C · doi:10.1002/(sici)1096-9918(199710)25:11<878::aid-sia311>3.0.co;2-c
  49. Vanden-Eynde X., 1999, Appl. Surf. Sci., 141, 1, 10.1016/S0169-4332(98)00626-6 · DOI
  50. Lhoest J.-B., J. Biomed. Mater. Res., in press.
  51. Horbett T., 1986, Techniques of Biocompatibility Testing
  52. Marletta G., 1990, Surf. Interface Anal., 16, 407, 10.1002/sia.740160185 · doi:10.1002/sia.740160185
  53. Bartiaux S., 1995, Faculte des Sciences Agronomiques, Universite Catholique de Louvain
  54. Bouchonnet S., 1992, Anal. Chem., 64, 743, 10.1021/ac00031a009 · DOI
  55. Vandeginste B. G. M., 1998, Handbook of Chemometrics and Qualimetrics: Part B
  56. Jackson J. E., 1991, A User's Guide to Principal Components, 10.1002/0471725331 · DOI · Paper page
  57. Wold S., 1987, Chemom. Intell. Lab. Syst., 2, 37, 10.1016/0169-7439(87)80084-9 · DOI · Paper page
  58. Hotelling H., 1931, An. Math. Stat., 2, 360, 10.1214/aoms/1177732979 · DOI · Paper page
  59. Wold S., 1978, Technometrics, 20, 397, 10.1080/00401706.1978.10489693 · DOI · Paper page
  60. Eastment H. T., 1982, J. Technometrics, 24, 73, 10.1080/00401706.1982.10487712 · DOI · Paper page
  61. Tidwell, C. D.; Castner, D. G.; Golledge, S. L.; Ratner, B. D.; Meyer, K.; Hagenhoff, B.; Benninghoven, A.Surf.Interface Anal.2001, in press.
  62. Derue C., 1999, J. Trace Microprobe Technol., 17, 451
  63. Heald S., 1988, X-ray AbsorptionPrinciples, Applications, Techniques of EXAFS, SEXAFS and XANES
  64. Ohta T., 1998, J. Electron Spectrosc. Relat. Phenom., 92, 131, 10.1016/S0368-2048(98)00114-5 · doi:10.1016/s0368-2048(98)00114-5
  65. Dannenberger O., 1997, Thin Solid Films, 307, 183, 10.1016/S0040-6090(97)00280-0 · doi:10.1016/s0040-6090(97)00280-0
  66. Fischer D., 1997, J. Vac. Sci. Technol. A, 15, 2173, 10.1116/1.580529 · doi:10.1116/1.580529
  67. Mallet Y., 1996, Chemom. Intell. Lab. Syst., 35, 157, 10.1016/S0169-7439(96)00050-0 · doi:10.1016/s0169-7439(96)00050-0
  68. Thompson P. M., 1991, Anal. Chem., 63, 2447, 10.1021/ac00021a012 · doi:10.1021/ac00021a012
  69. Wold S., 1976, Pattern Recognition, 8, 127, 10.1016/0031-3203(76)90014-5 · DOI · Paper page
  70. Uniyal S., 1982, Thromb. Haemostas., 47, 285, 10.1055/s-0038-1657186 · DOI · Paper page
  71. Brash J. L., 1984, Thromb. Haemostasis, 51, 326, 10.1055/s-0038-1661093 · DOI · Paper page
  72. Horbett T. A., 1984, Thromb. Haemostasis, 51, 174, 10.1055/s-0038-1661052 · DOI · Paper page
  73. Lhoest J.-B., 1998, J. Biomed Mater. Res., 41, 95, 10.1002/(SICI)1097-4636(199807)41:1<95::AID-JBM12>3.0.CO;2-G · DOI

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Metadata

Authors
Wagner, M. S., & Castner, D. G.
Venue
Langmuir
Published
2001-06-21
Volume
17
Issue
15
Pages
4649-4660
ISSN
  • 0743-7463 (ISSN-L)
  • 1520-5827
OpenAlex
W1981211088
Cited by
409
References
0
FWCI
18.98
Type
journal article
Language
en
Open access
closed

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Wagner, M. S., & Castner, D. G. (2001). Characterization of Adsorbed Protein Films by Time-of-Flight Secondary Ion Mass Spectrometry with Principal Component Analysis. Langmuir. https://doi.org/10.1021/la001209t

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