Skip to Main Content
Table 3.

Predicted and observed effects of macromolecular adsorption

Predicted effect Relevant observations
Enhancement of equilibrium self- and/or hetero-association of adsorbed macromolecules (Minton, 1995).   Proteins that do not self-associate in solution form 2D crystals when nonspecifically adsorbed to surfaces (Darst et al., 1988).  
Association of adsorbed macromolecules enhances adsorption capacity and may result in cooperative equilibrium adsorption isotherms (Chatelier and Minton, 1996; Minton, 2000b).   Equilibrium adsorption isotherms of proteins onto various types of surfaces exhibit positive cooperativity (Blanco et al., 1989; Cutsforth et al., 1989).  
Association of adsorbed macromolecules can accelerate the maximum rate of adsorption and may result in cooperative adsorption progress profiles (Minton, 2001b).   Time-dependent adsorption of several proteins onto supported lipid bilayers and other surfaces exhibits a rate that increases with increasing surface occupancy (Fernandez and Berry, 2003; Nygren and Stenberg, 1990; Ramsden et al., 1994).  
Adsorption can destabilize the solution conformation of a protein relative to alternate conformations that interact more strongly with the adsorbing surface (Minton, 1995; Cheung and Thirumalai, 2006).   Surface denaturation is a widely recognized obstacle to the purification and preparation of proteins at very low concentration (e.g. Edwards and Huber, 1992).  
Predicted effect Relevant observations
Enhancement of equilibrium self- and/or hetero-association of adsorbed macromolecules (Minton, 1995).   Proteins that do not self-associate in solution form 2D crystals when nonspecifically adsorbed to surfaces (Darst et al., 1988).  
Association of adsorbed macromolecules enhances adsorption capacity and may result in cooperative equilibrium adsorption isotherms (Chatelier and Minton, 1996; Minton, 2000b).   Equilibrium adsorption isotherms of proteins onto various types of surfaces exhibit positive cooperativity (Blanco et al., 1989; Cutsforth et al., 1989).  
Association of adsorbed macromolecules can accelerate the maximum rate of adsorption and may result in cooperative adsorption progress profiles (Minton, 2001b).   Time-dependent adsorption of several proteins onto supported lipid bilayers and other surfaces exhibits a rate that increases with increasing surface occupancy (Fernandez and Berry, 2003; Nygren and Stenberg, 1990; Ramsden et al., 1994).  
Adsorption can destabilize the solution conformation of a protein relative to alternate conformations that interact more strongly with the adsorbing surface (Minton, 1995; Cheung and Thirumalai, 2006).   Surface denaturation is a widely recognized obstacle to the purification and preparation of proteins at very low concentration (e.g. Edwards and Huber, 1992).  
Close Modal

or Create an Account

Close Modal
Close Modal