Chromatographic and Traditional Albumin Isotherms on Cellulose: A Model for Wound Protein Adsorption on Modified Cotton

Abstract

Albumin is the most abundant protein found in healing wounds. Traditional and chromatographic 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.

Designing cellulosic and nanocellulosic sensors for interface with a protease sequestrant wound-dressing prototype: Implications of material selection for dressing and protease sensor design

“…30,31 In addition, we and others have shown that albumin, which is the protein of highest concentration in wounds, does not unfold on cellulosic materials. 32,33 The hydrophilic material and surface charge derives from an abundance of hydroxyl functionality present in the nanocellulose structure. As discussed above, the ability to combine measurable protease detection with a dressing motif that neutralizes the effect of proteases is one of the specific goals of wound-healing biomaterial design.…”

Clinical Translational Potential in Skin Wound Regeneration for Adipose-Derived, Blood-Derived, and Cellulose Materials: Cells, Exosomes, and Hydrogels

“…Compared to proteins, cellulose polymers are relatively non-immunogenic [ 107 , 108 ]. In addition, it has been shown that albumin, which is the protein of highest concentration in wounds, does not unfold on cellulosic materials [ 109 , 110 , 111 ]. However, the human body lacks enzymes necessary to completely breakdown of cellulose materials, however through chemical modification it is possible to augment the biodegradation [ 103 ].…”

Affinity of Serum Albumin and Fibrinogen to Cellulose, Its Hydrophobic Derivatives and Blends

“…Among these bio-based polymers are cellulose and its esters and ethers (Klemm et al, 2005; Arca et al, 2018). Many authors therefore investigated the interaction of proteins with surfaces of polymers and elucidated its relation to hydrophilicity (Fujimori et al, 1998; Alves et al, 2010), charge (Edwards et al, 2012), morphology or solvation (Lu et al, 2007). Such studies were also conducted for cellulose and surface modified materials composed of it (Solin et al, 2019).…”