The DOI matches its Crossref record; 65 of the 65 references it cites were found in a registry or an index.
Protein Immobilization Strategies for Protein Biochips
Abstract
In the past few years, protein biochips have emerged as promising proteomic and diagnostic tools for obtaining information about protein functions and interactions. Important technological innovations have been made. However, considerable development is still required, especially regarding protein immobilization, in order to fully realize the potential of protein biochips. In fact, protein immobilization is the key to the success of microarray technology. Proteins need to be immobilized onto surfaces with high density in order to allow the usage of small amount of sample solution. Nonspecific protein adsorption needs to be avoided or at least minimized in order to improve detection performances. Moreover, full retention of protein conformation and activity is a challenging task to be accomplished. Although a large number of review papers on protein biochips have been published in recent years, few have focused on protein immobilization technology. In this review, current protein immobilization strategies, including physical, covalent, and bioaffinity immobilization for the fabrication of protein biochips, are described. Particular consideration has been given to oriented immobilization, also referred to as site-specific immobilization, which is believed will improve homogeneous surface covering and accessibility of the active site.
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
Formation and Structure of Self-Assembled Monolayers
Ulman, A. (1996) · Chemical Reviews · doi:10.1021/cr9502357 · Cited by 7,906
An fMRI Investigation of Emotional Engagement in Moral Judgment
Greene, J. D., Sommerville, R. B., Nystrom, L. E., Darley, J. M., & Cohen, J. D. (2001) · Science · doi:10.1126/science.1062872 · Cited by 4,561
Printing Proteins as Microarrays for High-Throughput Function Determination
MacBeath, G., & Schreiber, S. L. (2000) · Science · doi:10.1126/science.289.5485.1760 · Cited by 2,767
Prime, K. L., & Whitesides, G. M. (1993) · Journal of the American Chemical Society · doi:10.1021/ja00076a032 · Cited by 1,620
Characterization of DNA Probes Immobilized on Gold Surfaces
Herne, T. M., & Tarlov, M. J. (1997) · Journal of the American Chemical Society · doi:10.1021/ja9719586 · Cited by 1,541
Johnsson, B., Löfås, S., & Lindquist, G. (1991) · Analytical Biochemistry · doi:10.1016/0003-2697(91)90424-r · Cited by 1,262
Sequence-specific detection of individual DNA strands using engineered nanopores
Howorka, S., Cheley, S., & Bayley, H. (2001) · Nature Biotechnology · doi:10.1038/90236 · Cited by 760
(1997) · General Pharmacology: The Vascular System · doi:10.1016/s0306-3623(97)89864-3 · Cited by 750
The Global Spread of Malaria in a Future, Warmer World
Rogers, D. J., & Randolph, S. E. (2000) · Science · doi:10.1126/science.289.5485.1763 · Cited by 696
Peptide chips for the quantitative evaluation of protein kinase activity
Houseman, B. T., Huh, J. H., Kron, S. J., & Mrksich, M. (2002) · Nature Biotechnology · doi:10.1038/nbt0302-270 · Cited by 690
Lutolf, M. P., & Hubbell, J. A. (2003) · Biomacromolecules · doi:10.1021/bm025744e · Cited by 679
Pale-Grosdemange, C., Simon, E. S., Prime, K. L., & Whitesides, G. M. (1991) · Journal of the American Chemical Society · doi:10.1021/ja00001a002 · Cited by 673
Schweitzer, B., Wiltshire, S., Lambert, J., O'Malley, S., Kukanskis, K., Zhu, Z., Kingsmore, S. F., Lizardi, P. M., & Ward, D. C. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.170237197 · Cited by 597
The Staudinger Ligation—A Gift to Chemical Biology
Köhn, M., & Breinbauer, R. (2004) · Angewandte Chemie International Edition · doi:10.1002/anie.200401744 · Cited by 585
Templin, M. F., Stoll, D., Schrenk, M., Traub, P. C., Vöhringer, C. F., & Joos, T. O. (2002) · Trends in Biotechnology · doi:10.1016/s0167-7799(01)01910-2 · Cited by 572
Sigal, G. B., Bamdad, C., Barberis, A., Strominger, J., & Whitesides, G. M. (1996) · Analytical Chemistry · doi:10.1021/ac9504023 · Cited by 498
Label-free screening of bio-molecular interactions
Cooper, M. A. (2003) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-003-2111-y · Cited by 460
SPR for molecular interaction analysis: a review of emerging application areas
Karlsson, R. (2004) · Journal of Molecular Recognition · doi:10.1002/jmr.660 · Cited by 449
Protein microarrays: Meeting analytical challenges for clinical applications
Liotta, L. A., Espina, V., Mehta, A. I., Calvert, V., Rosenblatt, K., Geho, D., Munson, P. J., Young, L., Wulfkuhle, J., & Petricoin, E. F. (2003) · Cancer Cell · doi:10.1016/s1535-6108(03)00086-2 · Cited by 446
Microarrayed allergen molecules: diagnostic gatekeepers for allergy treatment
Hiller, R., Laffer, S., Harwanegg, C., Huber, M., Schmidt, W. M., Twardosz, A., Barletta, B., Becker, W. M., Blaser, K., Breiteneder, H., et al. (2002) · The FASEB Journal · doi:10.1096/fj.01-0711fje · Cited by 440
Betancor, L., López-Gallego, F., Hidalgo, A., Alonso-Morales, N., Mateo, G. D.-O. C., Fernández-Lafuente, R., & Guisán, J. M. (2006) · Enzyme and Microbial Technology · doi:10.1016/j.enzmictec.2006.01.014 · Cited by 414
Miller, J. C., Zhou, H., Kwekel, J., Cavallo, R., Burke, J., Butler, E. B., Teh, B. S., & Haab, B. B. (2003) · PROTEOMICS · doi:10.1002/pmic.200390009 · Cited by 388
High-Affinity Adaptors for Switchable Recognition of Histidine-Tagged Proteins
Lata, S., Reichel, A., Brock, R., Tampé, R., & Piehler, J. (2005) · Journal of the American Chemical Society · doi:10.1021/ja050690c · Cited by 384
Mixed Azide-Terminated Monolayers: A Platform for Modifying Electrode Surfaces
Collman, J. P., Devaraj, N. K., Eberspacher, T. P. A., & Chidsey, C. E. D. (2006) · Langmuir · doi:10.1021/la052947q · Cited by 376
Patel, N., Davies, M. C., Hartshorne, M., Heaton, R. J., Roberts, C. J., Tendler, S. J. B., & Williams, P. M. (1997) · Langmuir · doi:10.1021/la970933h · Cited by 369
Lu, B., Smyth, M. R., & O'Kennedy, R. (1996) · The Analyst · doi:10.1039/an996210029r · Cited by 360
Hodneland, C. D., Lee, Y.-S., Min, D.-H., & Mrksich, M. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.072685299 · Cited by 346
Turková, J. (1999) · Journal of Chromatography B: Biomedical Sciences and Applications · doi:10.1016/s0378-4347(98)00434-4 · Cited by 318
Molecular recognition at self-assembled monolayers: Optimization of surface functionalization
Spinke, J., Liley, M., Schmitt, F.-J., Guder, H.-J., Angermaier, L., & Knoll, W. (1993) · The Journal of Chemical Physics · doi:10.1063/1.465447 · Cited by 313
Progress in protein and antibody microarray technology
Angenendt, P. (2005) · Drug Discovery Today · doi:10.1016/s1359-6446(05)03392-1 · Cited by 289
Protein microarrays as tools for functional proteomics
LaBaer, J., & Ramachandran, N. (2005) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2004.12.006 · Cited by 266
Antigen microarray profiling of autoantibodies in rheumatoid arthritis
Hueber, W., Kidd, B. A., Tomooka, B. H., Lee, B. J., Bruce, B., Fries, J. F., Sønderstrup, G., Monach, P., Drijfhout, J. W., van Venrooij, W. J., et al. (2005) · Arthritis & Rheumatism · doi:10.1002/art.21269 · Cited by 261
Chapman, R. G., Ostuni, E., Yan, L., & Whitesides, G. M. (2000) · Langmuir · doi:10.1021/la991579l · Cited by 254
Epoxy-Amino Groups: A New Tool for Improved Immobilization of Proteins by the Epoxy Method
Mateo, C., Torres, R., Fernández-Lorente, G., Ortiz, C., Fuentes, M., Hidalgo, A., López-Gallego, F., Abian, O., Palomo, J. M., Betancor, L., et al. (2003) · Biomacromolecules · doi:10.1021/bm0257661 · Cited by 249
Integrin targeting using RGD‐PEI conjugates for in vitro gene transfer
Kunath, K., Merdan, T., Hegener, O., Häberlein, H., & Kissel, T. (2003) · The Journal of Gene Medicine · doi:10.1002/jgm.382 · Cited by 231
Site-Specific Protein Immobilization by Staudinger Ligation
Soellner, M. B., Dickson, K. A., Nilsson, B. L., & Raines, R. T. (2003) · Journal of the American Chemical Society · doi:10.1021/ja036712h · Cited by 227
Protein-Functionalized Polymer Brushes
Tugulu, S., Arnold, A., Sielaff, I., Johnsson, K., & Klok, H.-A. (2005) · Biomacromolecules · doi:10.1021/bm050016n · Cited by 217
Rizzi, S. C., & Hubbell, J. A. (2005) · Biomacromolecules · doi:10.1021/bm049614c · Cited by 197
Wegner, G. J., Lee, H. J., Marriott, G., & Corn, R. M. (2003) · Analytical Chemistry · doi:10.1021/ac0344438 · Cited by 192
Fan, C., Teixeira, M., Moura, J., Moura, I., Hanh, H. B., Le Gall, J., Peck, H. D., & Hoffman, B. M. (1991) · Journal of the American Chemical Society · doi:10.1021/ja00001a003 · Cited by 190
Preparation and Characterization of Poly(ethylene glycol) Vinyl Sulfone
Morpurgo, M., Veronese, F. M., Kachensky, D., & Harris, J. M. (1996) · Bioconjugate Chemistry · doi:10.1021/bc9600224 · Cited by 175
Lata, S., & Piehler, J. (2005) · Analytical Chemistry · doi:10.1021/ac048813j · Cited by 171
Boozer, C., Ladd, J., Chen, S., Yu, Q., Homola, J., & Jiang, S. (2004) · Analytical Chemistry · doi:10.1021/ac048908l · Cited by 161
Tinazli, A., Tang, J., Valiokas, R., Pićurić, S., Lata, S., Piehler, J., Liedberg, B., & Tampé, R. (2005) · Chemistry - A European Journal · doi:10.1002/chem.200500154 · Cited by 157
Emerging tools for real‐time label‐free detection of interactions on functional protein microarrays
Ramachandran, N., Larson, D. N., Stark, P. R. H., Hainsworth, E., & LaBaer, J. (2005) · FEBS Journal · doi:10.1111/j.1742-4658.2005.04971.x · Cited by 156
Hendrickson, E. R., Truby, T. M. H., Joerger, R. D., Majarian, W. R., & Ebersole, R. C. (1995) · Nucleic Acids Research · doi:10.1093/nar/23.3.522 · Cited by 147
Gershon, P. D., & Khilko, S. N. (1995) · Journal of Immunological Methods · doi:10.1016/0022-1759(95)00032-6 · Cited by 127
Covalent Microcontact Printing of Proteins for Cell Patterning
Rożkiewicz, D. I., Kraan, Y. M., Werten, M. W. T., de Wolf, F. A., Subramaniam, V., Ravoo, B. J., & Reinhoudt, D. N. (2006) · Chemistry - A European Journal · doi:10.1002/chem.200501554 · Cited by 125
Zhen, G., Falconnet, D., Kuennemann, E., Vörös, J., Spencer, N. D., Textor, M., & Zürcher, S. (2005) · Advanced Functional Materials · doi:10.1002/adfm.200500232 · Cited by 120
Vermette, P., Gengenbach, T. R., Divisekera, U., Kambouris, P. A., Griesser, H. J., & Meagher, L. (2003) · Journal of Colloid and Interface Science · doi:10.1016/s0021-9797(02)00185-6 · Cited by 105
Protein biochips: A new and versatile platform technology for molecular medicine
Lueking, A., Cahill, D. J., & Müllner, S. (2005) · Drug Discovery Today · doi:10.1016/s1359-6446(05)03449-5 · Cited by 91
Grazú, V., Abián, O., Mateo, C., et al. (2003) · Biomacromolecules · doi:10.1021/bm034262f · Cited by 90
Protein-sensing assay formats and devices
Bilitewski, U. (2006) · Analytica Chimica Acta · doi:10.1016/j.aca.2005.12.073 · Cited by 81
Blawas, A. S., Oliver, T. F., Pirrung, M. C., & Reichert, W. M. (1998) · Langmuir · doi:10.1021/la971231v · Cited by 79
Current status of protein chip development in terms of fabrication and application
Seong, S., & Choi, C. (2003) · PROTEOMICS · doi:10.1002/pmic.200300609 · Cited by 76
Ia, K., Melnyk, P. C., Stromsborg, K. E., Chee, M. S., Barker, D. L. A., & Zhao, C. (2004) · Biopolymers · doi:10.1002/bip.20009 · Cited by 76
Pirrung, M. C., & Huang, C. (1996) · Bioconjugate Chemistry · doi:10.1021/bc960013v · Cited by 74
Antigen arrays for antibody profiling
Robinson, W. H. (2006) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2005.12.028 · Cited by 63
Site-specific immobilization of proteins in a microarray using intein-mediated protein splicing
Girish, A., Sun, H., Yeo, D. S.-Y., Chen, G. Y. J., Chua, T. K., & Yao, S. Q. (2005) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2005.03.079 · Cited by 60
Protein Function Microarrays Based on Self‐Immobilizing and Self‐Labeling Fusion Proteins
Sielaff, I., Arnold, A., Godin, G., Tugulu, S., Klok, H., & Johnsson, K. (2005) · ChemBioChem · doi:10.1002/cbic.200500278 · Cited by 54
Combining SPOT Synthesis and Native Peptide Ligation to Create Large Arrays of WW Protein Domains
Toepert, F., Knaute, T., Guffler, S., Pires, J. R., Matzdorf, T., Oschkinat, H., & Schneider‐Mergener, J. (2003) · Angewandte Chemie International Edition · doi:10.1002/anie.200390298 · Cited by 54
Reetz, M. T., Fu, Y., & Meiswinkel, A. (2006) · Angewandte Chemie International Edition · doi:10.1002/anie.200503604 · Cited by 53
Protein Immobilization to a Partially Cross-Linked Organic Monolayer
Viitala, T., Vikholm, I., & Peltonen, J. P. K. (2000) · Langmuir · doi:10.1021/la990817+ · Cited by 49
Microarray: A Versatile Platform for High-Throughput Functional Proteomics
Hu, Y., Uttamchandani, M., & Yao, S. Q. (2006) · Combinatorial Chemistry & High Throughput Screening · doi:10.2174/138620706776055467 · Cited by 42
Glynou, K. M., Ioannou, P. C., & Christopoulos, T. K. (2003) · Bioconjugate Chemistry · doi:10.1021/bc0341021 · Cited by 24
Cited by
Surface Plasmon Resonance Sensors for Detection of Chemical and Biological Species
Homola, J. (2008) · Chemical Reviews · doi:10.1021/cr068107d · Cited by 4,525
Hernandez, K., & Fernandez-Lafuente, R. (2011) · Enzyme and Microbial Technology · doi:10.1016/j.enzmictec.2010.10.003 · Cited by 614
Barbosa, O., Torres, R., Ortiz, C., Berenguer-Murcia, Á., Rodrigues, R. C., & Fernandez-Lafuente, R. (2013) · Biomacromolecules · doi:10.1021/bm400762h · Cited by 494
Selective Covalent Protein Immobilization: Strategies and Applications
Wong, L. S., Khan, F., & Micklefield, J. (2009) · Chemical Reviews · doi:10.1021/cr8004668 · Cited by 489
Sam, S., Touahir, L., Salvador Andresa, J., Allongue, P., Chazalviel, J.-N., Gouget-Laemmel, A. C., Henry de Villeneuve, C., Moraillon, A., Ozanam, F., Gabouze, N., et al. (2010) · Langmuir · doi:10.1021/la902220a · Cited by 377
Metadata
- Authors
- Rusmini, F., Zhong, Z., & Feijen, J.
- Venue
- Biomacromolecules
- Publisher
- American Chemical Society (ACS)
- Published
- 2007-04-20
- Volume
- 8
- Issue
- 6
- Pages
- 1775-1789
- ISSN
- 1525-7797 (ISSN-L)
- 1526-4602
- OpenAlex
- W2032736963
- Cited by
- 869
- References
- 65
- FWCI
- 17.36
- 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
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.
