Submitted to: Journal of Biomaterials Applications
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 3/1/2011
Publication Date: 5/26/2012
Citation: Edwards, J.V., Castro, N.J., Condon, B.D., Costable, C.R., Goheen, S.C. 2012. Chromatographic and traditional albumin isotherms on cellulose: a model for wound protein adsorption on modified cotton. Journal of Biomaterials Applications. 26(8):939-961. Interpretive Summary: The creation of new markets for value-added, protective cotton textiles is currently an agriculture issue. Work in Southern Regional Research Center’s Cotton Textile Chemistry Unit is addressing the application of bio-active molecules to cotton textiles as a model to explore the creation of new value-added cotton products with highly selective properties and an environmentally acceptable finishes. In this paper we examine the way albumin, and important blood and wound healing protein interacts with cotton wound dressings. The paper studies how albumin binds to dressings that have been shown to lower protease levels in chronic wound fluid. Thus, it is an important contribution toward understanding the way cotton wound dressing interact with proteins significant to wound healing.
Technical Abstract: Albumin is the most abundant protein found in healing wounds. Traditional and chromatogrpahic protein isotherms of albumin binding on modified cotton fibers are useful in understanding albumin binding to cellulose wound dressings. An important consideration in the design of cellulosic wound dressings is adsorption and accumulation of proteins like albumin at the solid-liquid interface of the biological fluid and wound dressing fiber. To better understand the effect of fiber charge and molecular modifications in cellulose-containing fibers on the binding of serum albumin as observed in protease sequestrant dressings, albumin binding to modified cotton fibers was compared with traditional and chromatographic isotherms. Modified cotton including carboxymethylated, citrate-crosslinked, dialdehyde and phosphorylated cotton, which sequester elastase and collagenase, were compared for their albumin binding isotherms. Albumin isotherms on citrate-cellulose, cross-linked cotton demonstrated a two-fold increased binding affinity over untreated cotton. A comparison of albumin binding between traditional, solution isotherms and chromatographic isotherms on modified cellulose yielded similar equilibrium constants. Application of the binding affinity of albumin obtained in the in vitro protein isotherm to the in vivo wound dressing uptake of the protein is discussed. The chromatographic approach to assessment of albumin isotherms on modified cellulose offers a more rapid approach to evaluating protein binding on modified cellulose over traditional solution approaches.