Studies of equilibria between Streptococcus sanguis and artificial pellicle have suggested that there are multiple binding sites for the organism. In the present study, adhesion of S. sanguis to saliva-coated hydroxylapatite was examined by means of kinetic methods. Cell-pellicle complex formation was measured from initiation of binding to equilibrium. Rate constants were calculated for forward reactions (adsorption) and reverse reactions (desorption). Initial binding obeyed reversible, first-order kinetics, whereas desorption of bound cells followed biphasic kinetics. Initial desorption proceeded approximately ten times faster than the slower second rate. The results are consistent with the mechanism in which CP* represents the reversible equilibrium that shifts at a discrete rate to the high-affinity CP state. Thus, the biphasic binding behavior that has been previously deduced from equilibrium studies may be attributed to a time-dependent shift from close apposition to pellicle, stabilized by low-specificity forces, to a higher-affinity binding.
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