Nonspecific interactions between human serum albumin and poly(ethylene oxide) via high-resolution force spectroscopy

COLL 47

Monica A. Rixman1, Delphine Dean2, Celia Macias1, and Christine Ortiz1. (1) Department of Materials Science and Engineering, Massachusetts Institute of Technology, MIT Room #12-022, 77 Massachusetts Ave., Cambridge, MA 02139, (2) Electrical Engineering and Computer Science, Massachusetts Instittute of Technology, 60 Vassar Street, Room 38-377, Cambridge, MA 02139
A critical determinant of the biocompatibility of implanted blood-contacting devices is the initial nonspecific adsorption of blood plasma proteins onto the biomaterial surface. Using the technique of high-resolution force spectroscopy (HRFS) we have measured the nonspecific interaction forces between a nanosized probe tip covalently bound with human serum albumin (HSA, the most abundant blood plasma protein in the human body) and poly(ethylene oxide) (PEO, one of the most extensively used polymers for biomaterial surface coatings) chains end-grafted to a planar substrate at low density in aqueous buffer solution. Our experimental data, combined with rigorous theoretical approaches, provide important nanoscale information, such as estimations of the contributions of different types of constituent forces (e.g. steric, electrostatic, van der Waals) to the net interaction and clues to the important roles of the solvent, intramolecular bonding, and macromolecular conformation.

 

Nanoscale Imaging of Biological Systems

Division of Colloid and Surface Chemistry
The 225th ACS National Meeting, New Orleans, LA, March 23-27, 2003