The competitive adsorption of human proteins onto natural-based biomaterials

• Author(s): Alves, Catarina M. ; Reis, R. L. ; Hunt, John A.
• Date: 2010
• Persistent ID: http://hdl.handle.net/1822/20752
• Origin: RepositóriUM - Universidade do Minho
• Subject(s): Adsorption; Biomaterials; Biodegradable materials; Competition; Proteins
• Document Type: Article
• Language: English

Description

This study aims to further the understanding of nanoscale structures relevant for cellular recognition on contact and interaction with natural-based materials. The correlation between surface characteristics and protein adsorption from unitary and complex protein systems was investigated with respect to altering the bulk chemistry of the substrate material. Polymeric blends of starch and cellulose acetate, polycaprolactone (SPCL) and ethylene vinyl alcohol (SEVA-C) were used. Different proteins, bovine serum albumin, human serum albumin (HSA) and human fibronectin (HFN), were selected for this study. The construction of adsorption isotherms is an important starting point towards characterizing the interactions between surfaces and proteins. In this study, albumin adsorption isotherms fit the Freundlich model and were correlated with the chemistry and morphology of surfaces. In addition, protein distribution, quantification and competition were measured using fluorimetry and visualized by confocal microscopy. The analysis of unitary systems demonstrated that the adsorption of HSA was generally lower than that of HFN. In the latter case, SPCL and SEVA-C blends reached adsorption values of 97 and 89 per cent, respectively. In studying the co-adsorption of proteins, an increase in both HSA and HFN on SEVA-C surfaces was observed. SPCL showed no substantial increase in the adsorption of the proteins in competitive conditions. The similarity of these materials with other polysaccharide-based materials increases the relevance of the presented results. This study provides valuable information for the development of strategies towards the control of protein orientation and functionality as the availability of cell signalling epitopes for a broader family of materials that continue to be a significant component of this field of research.