The DOI matches its Crossref record; 16 of the 16 references it cites were found in a registry or an index.
Protein Interactions with Polymer Coatings and Biomaterials
Abstract
Protein adsorption is considered to be the most important factor of the interaction between polymeric biomaterials and body fluids or tissues. Water‐mediated hydrophobic and hydration forces as well as electrostatic interactions are believed to be the major factors of protein adsorption. A systematic analysis of various monolayer systems has resulted in general guidelines, the so‐called “Whitesides rules”. These concepts have been successfully applied for designing various protein‐resistant surfaces and are being studied to expand the understanding of protein–material interactions beyond existing limitations. Theories on the mechanisms of protein adsorption are constantly being improved due to the fast‐developing analytical technologies. This Review is aimed at improving these empirical guidelines with regard to present theoretical and analytical advances. Current analytical methods to test mechanistic hypotheses and theories of protein–surface interactions will be discussed. Special focus will be given to state‐of‐the‐art bioinert and biospecific coatings and their applications in biomedicine.
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
Measurement of protein using bicinchoninic acid
Smith, P. K., Krohn, R. I., Hermanson, G. T., Mallia, A. K., Gartner, F. H., Provenzano, M. D., Fujimoto, E. K., Goeke, N. M., Olson, B. J., & Klenk, D. C. (1985) · Analytical Biochemistry · doi:10.1016/0003-2697(85)90442-7 · Cited by 18,482
Mussel-inspired surface chemistry for multifunctional coatings
Lee, H., Dellatore, S. M., Miller, W. M., & Messersmith, P. B. (2007) · Science · doi:10.1126/science.1147241 · Cited by 10,965
Monopoli, M. P., Walczyk, D., Campbell, A., Elia, G., Lynch, I., Baldelli Bombelli, F., & Dawson, K. A. (2011) · Journal of the American Chemical Society · doi:10.1021/ja107583h · Cited by 1,835
A Survey of Structure−Property Relationships of Surfaces that Resist the Adsorption of Protein
Ostuni, E., Chapman, R. G., Holmlin, R. E., Takayama, S., & Whitesides, G. M. (2001) · Langmuir · doi:10.1021/la010384m · Cited by 1,799
Biological Responses to Materials
Anderson, J. M. (2001) · Annual Review of Materials Research · doi:10.1146/annurev.matsci.31.1.81 · Cited by 1,465
Effects of protein aggregates: An immunologic perspective
Rosenberg, A. S. (2006) · The AAPS Journal · doi:10.1208/aapsj080359 · Cited by 1,355
Time Evolution of the Nanoparticle Protein Corona
Casals, E., Pfaller, T., Duschl, A., Oostingh, G. J., & Puntes, V. (2010) · ACS Nano · doi:10.1021/nn901372t · Cited by 1,211
Biocompatible polymer materials: Role of protein–surface interactions
Chen, H., Yuan, L., Song, W., Wu, Z., & Li, D. (2008) · Progress in Polymer Science · doi:10.1016/j.progpolymsci.2008.07.006 · Cited by 706
Armstrong, J. K., Hempel, G., Koling, S., Chan, L. S., Fisher, T., Meiselman, H. J., & Garratty, G. (2007) · Cancer · doi:10.1002/cncr.22739 · Cited by 699
Hydrolysis and amino acid composition analysis of proteins
Fountoulakis, M., & Lahm, H.-W. (1998) · Journal of Chromatography A · doi:10.1016/s0021-9673(98)00721-3 · Cited by 606
Cited by
Antifouling membranes for sustainable water purification: strategies and mechanisms
Zhang, R., Liu, Y., He, M., Su, Y., Zhao, X., Elimelech, M., & Jiang, Z. (2016) · Chemical Society Reviews · doi:10.1039/c5cs00579e · Cited by 1,365
Molecular Understanding and Design of Zwitterionic Materials
Shao, Q., & Jiang, S. (2015) · Advanced Materials · doi:10.1002/adma.201404059 · Cited by 908
Physicochemical Stability of Monoclonal Antibodies: A Review
Le Basle, Y., Chennell, P., Tokhadze, N., Astier, A., & Sautou, V. (2020) · Journal of Pharmaceutical Sciences · doi:10.1016/j.xphs.2019.08.009 · Cited by 429
Factors affecting the physical stability (aggregation) of peptide therapeutics
Zapadka, K. L., Becher, F. J., Gomes dos Santos, A. L., & Jackson, S. E. (2017) · Interface Focus · doi:10.1098/rsfs.2017.0030 · Cited by 401
Biological responses to physicochemical properties of biomaterial surface
Rahmati, M., Silva, E. A., Reseland, J. E., A. Heyward, C., & Haugen, H. J. (2020) · Chemical Society Reviews · doi:10.1039/d0cs00103a · Cited by 391
Metadata
- Authors
- Wei, Q., Becherer, T., Angioletti‐Uberti, S., Dzubiella, J., Wischke, C., Neffe, A. T., Lendlein, A., Ballauff, M., & Haag, R.
- Venue
- Angewandte Chemie International Edition
- Publisher
- Wiley
- Published
- 2014-07-15
- Volume
- 53
- Issue
- 31
- Pages
- 8004-8031
- ISSN
- 1433-7851 (ISSN-L)
- 1521-3773
- OpenAlex
- W2135004341
- Cited by
- 743
- References
- 16
- FWCI
- 23.39
- 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: Protein Interactions with Polymer Coatings and Biomaterials. https://app.cochat.ai/papers/10.1002/anie.201400546
- The paper
- Wei, Q., Becherer, T., Angioletti‐Uberti, S., Dzubiella, J., Wischke, C., Neffe, A. T., Lendlein, A., Ballauff, M., & Haag, R. (2014). Protein Interactions with Polymer Coatings and Biomaterials. Angewandte Chemie International Edition. https://doi.org/10.1002/anie.201400546
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.