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W. Richard Bowen and Nidal Hilal 4

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2.3 INTERACTION FORCES 49<br />

A choice of boundary conditions is available at the particle surface. It<br />

is important to choose physically meaningful conditions at the particle<br />

surface, which may depend on the colloidal material being considered.<br />

For metal sols in a solution, a constant surface potential boundary condition<br />

is appropriate, given by:<br />

� o r� �<br />

α<br />

constant<br />

(2.32)<br />

where � is the particle radius plus the distance to the OHP (� a � d)<br />

(see Figure 2.4).<br />

A constant surface charge boundary condition may be appropriate<br />

when the surface charge is caused by crystal lattice defects, such as in<br />

clay minerals.<br />

� � ε ε �<br />

o d r o<br />

d<br />

�� �� � constant<br />

dr<br />

r�α<br />

(2.33)<br />

A boundary condition where the zeta potential is held constant is also<br />

possible [37, 48].<br />

� d r=α<br />

� ζ � constant<br />

(2.34)<br />

In the case of biomaterials <strong>and</strong> oxide surfaces, the charge can be generated<br />

by surface dissociation reactions, which are influenced by the solution<br />

conditions. This can be described by a boundary condition known as<br />

charge regulation [49].<br />

� � f ( � ) ≠ constant<br />

o o<br />

(2.35)<br />

As an example of this, consider the protein bovine serum albumin<br />

(BSA). The protein is made up of a number of different types of amino<br />

acids. Only certain amino acids will take part in the ionisation reactions,<br />

which will generate a charge on the protein surface. The development of<br />

a charge regulation model for BSA requires the number of these chargegenerating<br />

amino acids to be known. This data is available in the literature<br />

from the amino acid sequence of the protein [50] or from titration<br />

data [51]. The relevant equilibria reactions are illustrated by:<br />

1<br />

� �<br />

for aspartic or glutamic acid � COOH �� �� �� ��<br />

� COO � H (2.36)<br />

2<br />

for lysine � NH �� �� �� ��<br />

� NH � H<br />

K<br />

� K<br />

�<br />

3 2<br />

(2.37)

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