Conference paper

Behavior of Proteins at Interfaces

A. G. Walton ; Department of Macromolecular Science Case Western Reserve University, Cleveland, Ohio 44106, U.S.A.
M. E. Soderquist ; Department of Macromolecular Science Case Western Reserve University, Cleveland, Ohio 44106, U.S.A.

Abstract

The adsorption and conformational changes of three plasma
proteins, (bovine) serum albumin, .y-globulin and fibrinogen, on
several (bio)polymer surfaces are reported. A theory is developed
which invokes reversible adsorption of the proteins in the initial
stages and a time dependent conformational change of adsorbed
protein leading to essentially irreversible long-term adsorption.
In each case experimental evidence indicates that there .is a time-
dependent decrease in structural order. It is postulated that the
protein unfolds to optimize surface bonding, thus inducing the
c;hemistry of the protein/water interface by bonding at the protein/
/polymer interface. Cell binding studies support the concept that
the plasma proteins unfold to optimize the polymer/protein interaction.

Keywords

Hrčak ID:

194597

URI

https://hrcak.srce.hr/194597

Publication date:

5.11.1980.

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