Protein adsorption on derivatives of hyaluronic acid and subsequent cellular response

✍ Scribed by Megan S. Lord; Daniela Pasqui; Rolando Barbucci; Bruce K. Milthorpe

• Book ID: 102873560
• Publisher: John Wiley and Sons
• Year: 2009
• Tongue: English
• Weight: 515 KB
• Volume: 91A
• Category: Article
• ISSN: 1549-3296
• DOI: 10.1002/jbm.a.32219

✦ Synopsis

Abstract

The modulation of biological interactions with artificial surfaces is a vital aspect of biomaterials research. Serum protein adsorption onto photoreactive hyaluronic acid (Hyal‐N~3~) and its sulfated derivative (HyalS‐N~3~) 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‐N~3~ compared with Hyal‐N~3~. Fibronectin was adsorbed onto HyalS‐N~3~ 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‐N~3~. This was confirmed by reduced cell adhesion on fibronectin precoated Hyal‐N~3~ compared with fibronectin precoated HyalS‐N~3~. Minimal cell adhesion was observed on albumin and serum precoated Hyal‐N~3~. The quartz crystal microbalance confirmed that specific cell‐surface interactions were experienced by cells interacting with the fibronectin precoated polymers and serum precoated HyalS‐N~3~. © 2008 Wiley Periodicals, Inc. J Biomed Mater Res, 2009