The DOI matches its Crossref record; 157 of the 157 references it cites were found in a registry or an index.
Protein–polyelectrolyte interactions
Abstract
The interactions of proteins and polyelectrolytes lead to diverse applications in separations, delivery and wound repair, and are thus of interest to scientists in e.g. (a) glycobiology, (b) tissue engineering, (c) biosensing, and (d) pharmacology. This breadth is accompanied by an assortment of contexts and models in which polyelectrolytes are seen as (a) protein cognates assisting in complex cellular roles, (b) surrogates for the extracellular matrix, mimicking its hydration, mechanical and sequestering properties, (c) benign hosts that gently entrap, deposit and tether protein substrate specificity, and (d) selective but non-specific agents that modify protein solubility. Unsurprisingly, this literature is somewhat segregated by objectives and paradigms. We hope this review, which emphasizes publications over the last 8 years, represents and also counterbalances that divergence. An ongoing theme is the role of electrostatics, and we show how this leads to the variety of physical forms taken by protein–polyelectrolyte complexes. We present approaches towards analysis and characterization, motivated by the goal of structure–property elucidation. Such understanding should guide in applications, our third topic. We present recent developments in modeling and simulations of protein–polyelectrolyte systems. We close with a prospective on future developments in this field.
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Cites
Principles of polymer chemistry
(1995) · Choice Reviews Online · doi:10.5860/choice.33-2140 · Cited by 15,218
Milner, S. T. (1991) · Science · doi:10.1126/science.251.4996.905 · Cited by 1,821
Biomedical Applications of Layer‐by‐Layer Assembly: From Biomimetics to Tissue Engineering
Tang, Z., Wang, Y., Podsiadlo, P., & Kotov, N. A. (2006) · Advanced Materials · doi:10.1002/adma.200600113 · Cited by 1,302
Schlessinger, J., Plotnikov, A. N., Ibrahimi, O. A., Eliseenkova, A. V., Yeh, B. K., Yayon, A., Linhardt, R. J., & Mohammadi, M. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)00073-3 · Cited by 1,199
Protein secondary structure and circular dichroism: A practical guide
Johnson, W. C. (1990) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.340070302 · Cited by 940
Protein/polysaccharide complexes and coacervates in food systems
Schmitt, C., & Turgeon, S. L. (2011) · Advances in Colloid and Interface Science · doi:10.1016/j.cis.2010.10.001 · Cited by 874
Ladd, J., Zhang, Z., Chen, S., Hower, J. C., & Jiang, S. (2008) · Biomacromolecules · doi:10.1021/bm701301s · Cited by 808
Crystal structure of fibroblast growth factor receptor ectodomain bound to ligand and heparin
Pellegrini, L., Burke, D. F., von Delft, F., Mulloy, B., & Blundell, T. L. (2000) · Nature · doi:10.1038/35039551 · Cited by 704
The anticoagulant activation of antithrombin by heparin
Jin, L., Abrahams, J. P., Skinner, R., Petitou, M., Pike, R. N., & Carrell, R. W. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.26.14683 · Cited by 685
Polyelectrolyte–protein complexes
Cooper, C. L., Dubin, P. L., Kayitmazer, A. B., & Turksen, S. (2005) · Current Opinion in Colloid & Interface Science · doi:10.1016/j.cocis.2005.05.007 · Cited by 674
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Cited by
Protein–polysaccharide interactions and aggregates in food formulations
Gentile, L. (2020) · Current Opinion in Colloid & Interface Science · doi:10.1016/j.cocis.2020.03.002 · Cited by 325
Complex coacervate‐based materials for biomedicine
Blocher, W. C., & Perry, S. L. (2017) · WIREs Nanomedicine and Nanobiotechnology · doi:10.1002/wnan.1442 · Cited by 312
Metadata
- Authors
- Kayitmazer, A. B., Seeman, D., Minsky, B. B., Dubin, P. L., & Xu, Y.
- Venue
- Soft Matter
- Publisher
- Royal Society of Chemistry (RSC)
- Published
- 2013
- Volume
- 9
- Issue
- 9
- Pages
- 2553
- ISSN
- 1744-683X (ISSN-L)
- 1744-6848
- OpenAlex
- W2144314861
- Cited by
- 406
- References
- 157
- FWCI
- 25.65
- Type
- journal article
- Language
- en
- Open access
- closed
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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