Osmotic pressure contribution of albumin to colloidal interactions.

Abstract

Two surfaces that come in close contact in a solution with macromolecules present experience an attractive force caused by the osmotic pressure. We present a measurement of this effect by using a micrometer-sized sphere bound to a flat plate through a single molecular attachment in an albumin-containing solution. We obtain the osmotic part of the interaction potential with a resolution of <1 nm and a fraction of kTroom. This attractive interaction is seen to have a range comparable to the size of the albumin molecule. The results are broadly in agreement with a geometric model first proposed by Asakura and Oosawa.