Protein adsorption on derivatives of hyaluronic acid and subsequent cellular response
- Publication Type:
- Journal Article
- Citation:
- Journal of Biomedical Materials Research - Part A, 2009, 91 (3), pp. 635 - 646
- Issue Date:
- 2009-12-01
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The modulation of biological interactions with artificial surfaces is a vital aspect of biomaterials research. Serum protein adsorption onto photoreactive hyaluronic acid (Hyal-N3) and its sulfated derivative (HyalS-N3) was analyzed to determine extent of protein interaction and protein conformation as well as subsequent cell adhesion. There were no significant (p < 0.01) differences in the amount of protein adsorbed to the two polymers; however, proteins were found to be more loosely bound on HyalS-N3 compared with Hyal-N3. Fibronectin was adsorbed onto HyalS-N3 in such an orientation as to allow the availability of the cell binding region, while there was more restricted access to this region on fibronectin adsorbed onto Hyal-N3. This was confirmed by reduced cell adhesion on fibronectin precoated Hyal-N3 compared with fibronectin precoated HyalS-N3. Minimal cell adhesion was observed on albumin and serum precoated Hyal-N3. The quartz crystal microbalance confirmed that specific cell-surface interactions were experienced by cells interacting with the fibronectin precoated polymers and serum precoated HyalS-N3. © 2008 Wiley Periodicals, Inc.
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