Collagen is the most abundant protein found in animals and is also utilized by many bacteria as an adhesin to adhere to different substrates. Previous studies have characterized components of collagen’s surface free energy (γSLW, γSAB, and γS) using the Owens-Wendt equation, but the separate acid-base components (γS+ and γS–) remained uncharacterized. The surface free energy of the isolated hydrophilic portion of collagen used by bacteria to adhere to substrates also had not been determined. The present study was designed to determine the full surface free energy profile (γS, γSLW, γSAB, γS+, and, γS–) of collagen’s hydrophilic portion to find a suitable surface coating capable of preventing bacterial adhesion and colonization. Glass slides were surface functionalized to produce a nonpolar surface onto which soluble and insoluble collagen was solvent case onto the slides. The sessile drop method for determining contact angles was used with three fully characterized solvents (e.g., α-bromonaphthalene, formamide and deionized water) whereupon the surface free energy components of the collagen-coated slides were determined via the Owens-Wendt and van Oss-Chaudhury-Good equations. The results, calculated via the linear algebraic matrix method, showed comparable surface free energy values to previous studies for the insoluble collagen. The soluble collagen also had comparable values meaning that the hydrophilic portions of the collagen had not oriented correctly. Though the surface free energy for the hydrophilic portion of collagen remains uncharacterized, the acid (γS+) and base (γS–) components of collagen’s surface free energy were determined using the van Oss-Chaudhury-Good equation.

Surface free energy characterization of an adhesin protein

255th National Meeting (2018)

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