Compositions and methods for selectively sequestering metal ions
Compositions and methods for the selective sequestration of metal ions are generally described.
1. A composition, comprising:
a plurality of S100 protein molecules; and
a support comprising a plurality of functional groups,
wherein the plurality of S100 protein molecules are covalently immobilized on the support via reactions between the plurality of functional groups and amine groups of the plurality of S100 protein molecules, such that the covalently immobilized S100 protein molecules have binding sites available for chelation of metal ions and are thus configured to selectively sequester metal ions.
2. The composition of claim 1 , wherein the plurality of S100 protein molecules is a plurality of S100A12 protein molecules.
3. The composition of claim 1 , wherein the support is a solid support.
4. The composition of claim 1 , wherein the support is agarose resin.
5. The composition of claim 4 , wherein the agarose resin is N-hydroxy-succinimide-modified agarose resin.
6. The composition of claim 1 , wherein the plurality of S100 protein molecules is covalently attached to the support through amide linkages.
7. The composition of claim 1 , wherein the functional groups are ester groups.
8. The composition of claim 1 , wherein selectively sequestering metal ions comprises:
exposing the composition to a sample comprising a plurality of a first type of metal ion and a plurality of a second type of metal ion;
wherein following the exposing step, greater than about 90% of the first type of metal ion in the sample are sequestered by the plurality of S100 protein molecules immobilized on the support, and;
less than about 5% of the second type of metal ion in the sample are sequestered by the plurality of S100 protein molecules immobilized on the support.
9. A composition, comprising:
a plurality of S100 protein molecules; and
a support comprising a plurality of functional groups,
wherein the plurality of S100 protein molecules are covalently immobilized on the support via reactions between the plurality of functional groups and amine groups of the plurality of S100 protein molecules,
whereby the covalently immobilized protein molecules have more binding sites available for chelation of metal ions than an essentially identical comparative protein immobilized on a comparative support via reactions between carboxy functional groups on the comparative protein and functional groups on the comparative support, such that the covalently immobilized protein molecules are thus better able to carry out their function as compared to the comparative protein immobilized on the comparative support,
wherein the function comprises:
exposing the composition to a sample comprising a plurality of a first type of metal ion and a plurality of a second type of metal ion,
wherein following the exposing step, greater than about 90% of the first type of metal ion in the sample are sequestered by the plurality of protein molecules immobilized on the support, and
less than about 5% of the second type of metal ion in the sample are sequestered by the plurality of protein molecules immobilized on the support.