The DOI matches its Crossref record; 39 of the 39 references it cites were found in a registry or an index.
Strong Repulsive Forces between Protein and Oligo (Ethylene Glycol) Self-Assembled Monolayers: A Molecular Simulation Study
Open accessAbstract
Restrained molecular dynamics simulations were performed to study the interaction forces of a protein with the self-assembled monolayers (SAMs) of S(CH2)4(EG)4OH, S(CH2)11OH, and S(CH2)11CH3 in the presence of water molecules. The force-distance curves were calculated by fixing the center of mass of the protein at several separation distances from the SAM surface. Simulation results show that the relative strength of repulsive force acting on the protein is in the decreasing order of OEG-SAMs > OH-SAMs > CH3-SAMs. The force contributions from SAMs and water molecules, the structural and dynamic behavior of hydration water, and the flexibility and conformation state of SAMs were also examined to study how water structure at the interface and SAM flexibility affect the forces exerted on the protein. Results show that a tightly bound water layer adjacent to the OEG-SAMs is mainly responsible for the large repulsive hydration force.
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
CHARMM: A program for macromolecular energy, minimization, and dynamics calculations
Brooks, B. R., Bruccoleri, R. E., Olafson, B. D., States, D. J., Swaminathan, S., & Karplus, M. (1983) · Journal of Computational Chemistry · doi:10.1002/jcc.540040211 · Cited by 14,944
All-Atom Empirical Potential for Molecular Modeling and Dynamics Studies of Proteins
MacKerell, A. D., Bashford, D., Bellott, M., Dunbrack, R. L., Evanseck, J. D., Field, M. J., Fischer, S., Gao, J., Guo, H., Ha, S., et al. (1998) · The Journal of Physical Chemistry B · doi:10.1021/jp973084f · Cited by 14,311
Weiner, J., & Ho, P.-T. (2003) · Wiley eBooks · Cited by 2,020
Self-Assembled Organic Monolayers: Model Systems for Studying Adsorption of Proteins at Aurfaces
Prime, K. L., & Whitesides, G. M. (1991) · Science · doi:10.1126/science.252.5009.1164 · Cited by 1,831
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
Prime, K. L., & Whitesides, G. M. (1993) · Journal of the American Chemical Society · doi:10.1021/ja00076a032 · Cited by 1,620
Protein—surface interactions in the presence of polyethylene oxide
Jeon, S. I., Lee, J. H., Andrade, J. D., & De Gennes, P. G. (1991) · Journal of Colloid and Interface Science · doi:10.1016/0021-9797(91)90043-8 · Cited by 1,523
Poly(ethylene glycol) chemistry : biotechnical and biomedical applications
Harris, J. M. (1992) · Plenum Press eBooks · Cited by 1,426
New spherical‐cutoff methods for long‐range forces in macromolecular simulation
Steinbach, P. J., & Brooks, B. R. (1994) · Journal of Computational Chemistry · doi:10.1002/jcc.540150702 · Cited by 1,147
Adsorption of proteins from solution at the solid-liquid interface
Norde, W. (1986) · Advances in Colloid and Interface Science · doi:10.1016/0001-8686(86)80012-4 · Cited by 1,102
Cited by
Anti-PEG antibodies in the clinic: Current issues and beyond PEGylation
Zhang, P., Sun, F., Liu, S., & Jiang, S. (2016) · Journal of Controlled Release · doi:10.1016/j.jconrel.2016.06.040 · Cited by 688
Self-citationCao, Z., & Jiang, S. (2012) · Nano Today · doi:10.1016/j.nantod.2012.08.001 · Cited by 329
Self-citationVaterrodt, A., Thallinger, B., Daumann, K., Koch, D., Guebitz, G. M., & Ulbricht, M. (2016) · Langmuir · doi:10.1021/acs.langmuir.5b04303 · Cited by 150
Surface functionalization of biomaterials by radical polymerization
Zhou, T., Zhu, Y., Li, X., Liu, X., Yeung, K. W. K., Wu, S., Wang, X., Cui, Z., Yang, X., & Chu, P. K. (2016) · Progress in Materials Science · doi:10.1016/j.pmatsci.2016.04.005 · Cited by 145
Ou, X., Xue, B., Lao, Y., Wutthinitikornkit, Y., Tian, R., Zou, A., Yang, L., Wang, W., Cao, Y., & Li, J. (2020) · Science Advances · doi:10.1126/sciadv.abb7620 · Cited by 109
Metadata
- Authors
- Zheng, J., Li, L., Tsao, H.-K., Sheng, Y.-J., Chen, S., & Jiang, S.
- Venue
- Biophysical Journal
- Publisher
- Elsevier BV
- Published
- 2005-07
- Volume
- 89
- Issue
- 1
- Pages
- 158-166
- ISSN
- 0006-3495 (ISSN-L)
- OpenAlex
- W2019366993
- Cited by
- 340
- References
- 39
- FWCI
- 6.00
- Type
- journal article
- Language
- en
- Open access
- bronze
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: Strong Repulsive Forces between Protein and Oligo (Ethylene Glycol) Self-Assembled Monolayers: A Molecular Simulation Study. https://app.cochat.ai/papers/10.1529/biophysj.105.059428
- The paper
- Zheng, J., Li, L., Tsao, H.-K., Sheng, Y.-J., Chen, S., & Jiang, S. (2005). Strong Repulsive Forces between Protein and Oligo (Ethylene Glycol) Self-Assembled Monolayers: A Molecular Simulation Study. Biophysical Journal. https://doi.org/10.1529/biophysj.105.059428
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.