The DOI matches its Crossref record.
Characterization of Adsorbed Protein Films by Time-of-Flight Secondary Ion Mass Spectrometry with Principal Component Analysis
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.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
No references could be resolved yet.
Research works printed but not linked: 73
- Baier R. E., 1969, J. Biomed. Mater. Res., 3, 191, 10.1002/jbm.820030115 · DOI · Paper page
- 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
- Bryers J. D., 1994, Colloids Surf. B, 2, 9, 10.1016/0927-7765(94)80013-8 · DOI
- 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
- 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
- Ertel S. I., 1994, J. Biomed. Mater. Res., 28, 667, 10.1002/jbm.820280603 · DOI
- Gristina A. G., 1987, Science, 237, 1588, 10.1126/science.3629258 · DOI · Paper page
- Horbett T. A., 1994, Colloids Surf. B, 2, 225, 10.1016/0927-7765(94)80037-5 · DOI · Paper page
- 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
- Kao, W. J.; Hubbel, J. A.; Anderson, J. M.J. Mater. Sci. Mater. Med.1999,10, 601. · DOI
- Montanaro L., 1999, Biomaterials, 20, 1945, 10.1016/S0142-9612(99)00099-X · DOI
- McDevitt D., 1997, Eur. J. Biochem., 247, 416, 10.1111/j.1432-1033.1997.00416.x · DOI · Paper page
- 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
- Lundberg F., 1997, Infect. Immun., 65, 897, 10.1128/iai.65.3.897-902.1997 · doi:10.1128/iai.65.3.897-902.1997
- Lopez G. P., 1992, J. Biomed. Mater. Res., 26, 415, 10.1002/jbm.820260402 · DOI · Paper page
- Sheu M.-S., 1993, Clin. Mater., 13, 41, 10.1016/0267-6605(93)90088-O · doi:10.1016/0267-6605(93)90088-o
- Sheu M.-S., 1993, J. Adhes. Sci. Technol., 7, 1065, 10.1163/156856193X00583 · doi:10.1163/156856193x00583
- Morra M., 1993, Clin. Mater., 14, 255, 10.1016/0267-6605(93)90010-5 · DOI
- Deng L., 1996, J. Am. Chem. Soc., 118, 5136, 10.1021/ja960461d · doi:10.1021/ja960461d
- Favia P., 1998, Surf. Coat. Technol., 98, 1102, 10.1016/S0257-8972(97)00285-5 · DOI
- Harder P., 1998, J. Phys. Chem. B, 102, 426, 10.1021/jp972635z · DOI · Paper page
- 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
- Bohnert J. L., 1990, J. Biomater. Sci. Polym. Ed., 1, 279, 10.1163/156856289X00154 · doi:10.1163/156856289x00154
- Kiaei D., 1992, J. Biomater. Sci. Polym. Ed., 4, 35, 10.1163/156856292X00286 · doi:10.1163/156856292x00286
- Shi H., 1999, Nature, 398, 593, 10.1038/19267 · DOI · Paper page
- Siedlecki C. A., 1998, Biomaterials, 19, 441, 10.1016/S0142-9612(97)00222-6 · DOI
- Elwing H., 1998, Biomaterials, 19, 397, 10.1016/S0142-9612(97)00112-9 · DOI · Paper page
- Chittur K. K., 1998, Biomaterials, 19, 357, 10.1016/S0142-9612(97)00223-8 · DOI · Paper page
- Ratner B. D., 1994, Colloids Surf. B, 2, 333, 10.1016/0927-7765(94)80048-0 · DOI
- Ratner B. D., 1995, Surf. Interface Anal., 23, 521, 10.1002/sia.740230712 · DOI
- Chittur K. K., 1998, Biomaterials, 19, 301, 10.1016/S0142-9612(97)00107-5 · DOI
- 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
- Paynter R. W., 1985, Surface and Interfacial Aspects of Biomedical Polymers
- Chowdhury P. B., 1998, Colloids Surf. A, 143, 53, 10.1016/S0927-7757(98)00408-7 · DOI
- Mantus D. S., 1993, Anal. Chem., 65, 1431, 10.1021/ac00058a021 · doi:10.1021/ac00058a021
- Benninghoven A., 1993, Anal. Chem., 65, 630A, 10.1021/ac00062a717 · doi:10.1021/ac00062a717
- Ratner B. D., 1992, Clin. Mater., 11, 25, 10.1016/0267-6605(92)90027-Q · doi:10.1016/0267-6605(92)90027-q
- Ratner B. D., 1993, Clin. Mater., 13, 71, 10.1016/0267-6605(93)90093-M · DOI
- Leonard D., 1999, Fresenius J. Anal. Chem., 365, 3, 10.1007/s002160051437 · doi:10.1007/s002160051437
- 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
- Ratner B. D., Fifth World Biomaterials Conference; Toronto
- Ratner B. D., 1996, Polym. Prepr. (Am. Chem. Soc., Div. Polym. Chem.), 37, 843
- Colliver T. L., 1997, Anal. Chem., 69, 2225, 10.1021/ac9701748 · DOI · Paper page
- Clerc J., 1997, Cell Biol. Inter., 21, 619, 10.1006/cbir.1998.0205 · doi:10.1006/cbir.1998.0205
- Fourre C., 1997, J. Anal. At. Spectrom., 12, 1105, 10.1039/A700777I · doi:10.1039/a700777i
- Kargacin M. E., 1986, Anal. Chem., 58, 2300, 10.1021/ac00124a041 · doi:10.1021/ac00124a041
- 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
- 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
- Vanden-Eynde X., 1999, Appl. Surf. Sci., 141, 1, 10.1016/S0169-4332(98)00626-6 · DOI
- Lhoest J.-B., J. Biomed. Mater. Res., in press.
- Horbett T., 1986, Techniques of Biocompatibility Testing
- Marletta G., 1990, Surf. Interface Anal., 16, 407, 10.1002/sia.740160185 · doi:10.1002/sia.740160185
- Bartiaux S., 1995, Faculte des Sciences Agronomiques, Universite Catholique de Louvain
- Bouchonnet S., 1992, Anal. Chem., 64, 743, 10.1021/ac00031a009 · DOI
- Vandeginste B. G. M., 1998, Handbook of Chemometrics and Qualimetrics: Part B
- Jackson J. E., 1991, A User's Guide to Principal Components, 10.1002/0471725331 · DOI · Paper page
- Wold S., 1987, Chemom. Intell. Lab. Syst., 2, 37, 10.1016/0169-7439(87)80084-9 · DOI · Paper page
- Hotelling H., 1931, An. Math. Stat., 2, 360, 10.1214/aoms/1177732979 · DOI · Paper page
- Wold S., 1978, Technometrics, 20, 397, 10.1080/00401706.1978.10489693 · DOI · Paper page
- Eastment H. T., 1982, J. Technometrics, 24, 73, 10.1080/00401706.1982.10487712 · DOI · Paper page
- Tidwell, C. D.; Castner, D. G.; Golledge, S. L.; Ratner, B. D.; Meyer, K.; Hagenhoff, B.; Benninghoven, A.Surf.Interface Anal.2001, in press.
- Derue C., 1999, J. Trace Microprobe Technol., 17, 451
- Heald S., 1988, X-ray AbsorptionPrinciples, Applications, Techniques of EXAFS, SEXAFS and XANES
- 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
- Dannenberger O., 1997, Thin Solid Films, 307, 183, 10.1016/S0040-6090(97)00280-0 · doi:10.1016/s0040-6090(97)00280-0
- Fischer D., 1997, J. Vac. Sci. Technol. A, 15, 2173, 10.1116/1.580529 · doi:10.1116/1.580529
- Mallet Y., 1996, Chemom. Intell. Lab. Syst., 35, 157, 10.1016/S0169-7439(96)00050-0 · doi:10.1016/s0169-7439(96)00050-0
- Thompson P. M., 1991, Anal. Chem., 63, 2447, 10.1021/ac00021a012 · doi:10.1021/ac00021a012
- Wold S., 1976, Pattern Recognition, 8, 127, 10.1016/0031-3203(76)90014-5 · DOI · Paper page
- Uniyal S., 1982, Thromb. Haemostas., 47, 285, 10.1055/s-0038-1657186 · DOI · Paper page
- Brash J. L., 1984, Thromb. Haemostasis, 51, 326, 10.1055/s-0038-1661093 · DOI · Paper page
- Horbett T. A., 1984, Thromb. Haemostasis, 51, 174, 10.1055/s-0038-1661052 · DOI · Paper page
- 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
Cited by
Biomedical surface science: Foundations to frontiers
Castner, D. G., & Ratner, B. D. (2002) · Surface Science · doi:10.1016/s0039-6028(01)01587-4 · Cited by 1,329
Self-citationProteins, platelets, and blood coagulation at biomaterial interfaces
Xu, L.-C., Bauer, J. W., & Siedlecki, C. A. (2014) · Colloids and Surfaces B: Biointerfaces · doi:10.1016/j.colsurfb.2014.09.040 · Cited by 391
The Vroman effect: Competitive protein exchange with dynamic multilayer protein aggregates
Hirsh, S. L., McKenzie, D. R., Nosworthy, N. J., Denman, J. A., Sezerman, O. U., & Bilek, M. M. M. (2013) · Colloids and Surfaces B: Biointerfaces · doi:10.1016/j.colsurfb.2012.10.039 · Cited by 340
Regulation of decellularized matrix mediated immune response
Chakraborty, J., Roy, S., & Ghosh, S. (2020) · Biomaterials Science · doi:10.1039/c9bm01780a · Cited by 130
Semenyshyn, R., Hentschel, M., Stanglmair, C., Teutsch, T., Tarin, C., Pacholski, C., Giessen, H., & Neubrech, F. (2019) · Nano Letters · doi:10.1021/acs.nanolett.8b02372 · Cited by 60
Metadata
- Authors
- Wagner, M. S., & Castner, D. G.
- Venue
- Langmuir
- Publisher
- American Chemical Society (ACS)
- 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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Characterization of Adsorbed Protein Films by Time-of-Flight Secondary Ion Mass Spectrometry with Principal Component Analysis. https://app.cochat.ai/papers/10.1021/la001209t
- The paper
- 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
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.