Albumin adsorption onto pyrolytic carbon: A molecular mechanics approach

A number of implants of cardiac valve prosthesis, vascular prosthesis, and coronary stents present a pyrolytic carbon interface to blood. Plasma protein adsorption is essential for the hemocompatibility of the implanted devices. This work quantitatively evaluates the molecular interaction force between a biomaterial surface (pyrolytic carbon) and plasma protein (albumin) binding sites through a simplified molecular model of the interface consisting of (i) multioriented graphite micro crystallites; (ii) selected fragments of albumin; and (iii) a water environment. A number of simplifying assumptions were made in the calculation: the albumin molecule was divided into hydrophobic and hydrophilic subunits (helices); an idealized clean, nonoxidized polycrystalline graphite surface was assumed to approximate the surface of pyrolytic carbon. The interaction forces between albumin helices and pyrolytic carbon surfaces are evaluated from potential energy data. These forces are decomposed into a normal and a tangential component. The first one is calculated using a docking procedure (F-perpendicular to tot MAX = 4.16 x 10(-20) N). The second one (F-parallel to), calculated by mean of geometric models estimating the energy variation associated with the protein sliding on the material surface, varies within the range +/-9.62 x 10(-21) N. The molecular simulations were performed using the commercial soft-ware package Hyperchem 5.0 (Hyperchem, Hypercube, Canada). (C) 2001 John Wiley & Sons, Inc.