The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
RGD‐grafted poly‐l‐lysine‐graft‐(polyethylene glycol) copolymers block non‐specific protein adsorption while promoting cell adhesion
Abstract
A novel class of surface‐active copolymers is described, designed to protect surfaces from nonspecific protein adsorption while still inducing specific cell attachment and spreading. A graft copolymer was synthesized, containing poly‐(L‐lysine) (PLL) as the backbone and substrate binding and poly(ethylene glycol) (PEG) as protein adsorption‐resistant pendant side chains. A fraction of the grafted PEG was pendantly functionalized by covalent conjugation to the peptide motif RGD to induce cell binding. The graft copolymer spontaneously adsorbs from dilute aqueous solution onto negatively charged surfaces. The performance of RGD‐modified PLL‐g‐PEG copolymers was analyzed in protein adsorption and cell culture assays. These coatings efficiently blocked the adsorption of serum proteins to Nb 2 O 5 and tissue culture polystyrene while specifically supporting attachment and spreading of human dermal fibroblasts. This surface functionalization technology is expected to be valuable in both the biomaterial and biosensor fields, because different signals can easily be combined, and sterilization and application are straightforward and cost‐effective. © 2003 Wiley Periodicals, Inc. Biotechnol Bioeng 82: 784–790, 2003.
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Holland, N. B., Qiu, Y., Ruegsegger, M., & Marchant, R. E. (1998) · Nature · doi:10.1038/33894 · Cited by 308
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Franz, S., Rammelt, S., Scharnweber, D., & Simon, J. C. (2011) · Biomaterials · doi:10.1016/j.biomaterials.2011.05.078 · Cited by 1,391
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Metadata
- Authors
- VandeVondele, S., Vörös, J., & Hubbell, J. A.
- Venue
- Biotechnology and Bioengineering
- Publisher
- Wiley
- Published
- 2003-04-11
- Volume
- 82
- Issue
- 7
- Pages
- 784-790
- ISSN
- 0006-3592 (ISSN-L)
- 1097-0290
- OpenAlex
- W1980873308
- Cited by
- 328
- References
- 1
- FWCI
- 9.69
- Type
- journal article
- Language
- en
- Open access
- closed
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