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Proteins From Oyster Shell: Biomineralization Regulators and Commercial Polymer Analogs

Published online by Cambridge University Press:  10 February 2011

A. P. Wheeler  and
C. S. Sikes
A. P. Wheeler
Affiliation:
Department of Biological Sciences, Clemson University, Clemson, SC USA 29634, wheeler@clemson.edu
C. S. Sikes
Affiliation:
The Mineralization Center, Department of Biological Sciences, University of South Alabama, Mobile, AL 36688, ssikes@usamail.usouthal.edu
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Abstract

Molluscan shell is a composite made up of μm-sized CaCO3 crystals and an organic phase (matrix). This report outlines our studies on the structure and activities of matrix proteins isolated from the inner calcite layer of shell of the Eastern oyster, including their cellular origin and structure and their relationship to the crystalline mineral phase. In addition, we present results of the synthesis and commercialization of polypeptide polymers which are based on the structure and activities of the oyster proteins. Extracted shell proteins are polyanionic and range in size from relatively small soluble forms to those which are crosslinked and insoluble. The soluble forms are capable of adsorbing to calcite in vitro and in the process changing its growth habit and acting as threshold growth inhibitors. Their function in vivo is not understood, but they may serve to control shell crystal morphology. The insoluble protein forms gels readily and may serve to provide resiliency to the shell and, from in vitro and in situ observations, appears to serve as a site for nucleation of crystals. However, from studies in vitro, these gels do not lower the energy of activation for nucleation, as previously expected. Matrix protein aggregates are identifiable by AFM on the surface of crystals, but as such do not serve as nucleation sites for new crystal growth. If the aggregates are removed, then ectopic crystal growth proceeds readily revealing orientation of the underlying crystals. All the matrix proteins contain domains rich in aspartic acid, are heavily phosphorylated, crossreact in antibody studies and may belong to a limited number of gene families with individuals modified post-synthesis. The proteins are made by a specialized group of cells located primarily some distance from the growing edge of the shell and appear to be assembled into sheets soon after secretion. Soluble anti-scalants and crosslinked insoluble water absorbents have been developed based on the structure and activity of the matrix proteins. These are primarily poly(aspartates) which can be made in large scale via thermal polycondensation of aspartic acid. The soluble forms are commercially used as biodegradable water treatment chemicals among other applications.

Type
Research Article
Information
MRS Online Proceedings Library (OPL) , Volume 599: Symposium DD – Mineralization in Natural & Synthetic Biomaterials , 1999 , 209
Copyright
Copyright © Materials Research Society 2000

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References

1. Simkiss, K. and Wilbur, K.M., Biomineralization: Cell Biology and Mineral Deposition. Academic Press, Inc., San Diego, 1989, pp. 231–260.Google Scholar
2. Carriker, M.R. in The Eastern Oyster, Crassostrea virginica, edited by Kennedy, V.S., Nowell, R.I.E., and Eble, A.F., Maryland Sea Grant, College Park, MD, 1996, pp. 75–168.Google Scholar
3. Watabe, N., J of Ultrustruct. Res. 12, p. 351–370 (1965).Google Scholar
4. Weiner, S. and Traub, W., Phil. Trans. R. Soc. London, 304, p. 15–24 (1984).Google Scholar
5. Sikes, C.S., Wheeler, A.P., Wierzbicki, A., Dillaman, R.M., and DeLuca, L., Biol. Bull. 194, p. 304–316 (1998).Google Scholar
6. Weiner, S., Traub, W., and Lowenstam, H.A., in Biomineralization and Biological Metal Accumulation, edited by Westbroek, P.W. and deJong, E.W., (D. Reidel Publishing Co., Dordrecht, Holland 1983), p. 205–222.Google Scholar
7. Weiner, S., Calc. Tiss. Int., 29, p. 163–167 (1979).Google Scholar
8. Cariolou, M.A. and Morse, D.E., J. Comp. Phys., B, 157, p. 717–729 (1988).Google Scholar
9. Rusenko, K.W., Donachy, J.E., and Wheeler, A.P., in Surface Reactive Peptides and Polymers (ACS, Washington, DC, 1991), p. 107–124.Google Scholar
10. Keith, J., Stockwell, S., Ball, D., Remillard, K., Kaplan, D., Thannhauser, T., and Sherwood, R., J. Comp. Biochem. Phys., B, 105B, p. 487–496 (1993).Google Scholar
11. Miyamoto, H., Miyashita, T., Okushima, M., Nakano, S., Morita, T., and Matsushiro, A., Proc. Nat. Acad. Sci. USA, 93, p. 9657–9660 (1996).Google Scholar
12. Shen, X., Belcher, A.M., Hansma, P.K., Stucky, G. D., and Morse, D.E., J. Biol. Chem., 272, p. 32472–32481 (1997).Google Scholar
13. Sudo, S., Fujikawa, T., Nakakura, T., Ohkubo, T., Sakaguchi, K., Tanaka, M., and Nakashima, K., Nature, 387, p. 563–564 (1997).Google Scholar
14. Sarashina, I. and Endo, K., American Mineralogist, 83, p. 1510–1515 (1998).Google Scholar
15. Wheeler, A.P., Rusenko, K.W., Swift, D.M., and Sikes, C.S., Marine Biol., 98, p. 71–80 (1988).Google Scholar
16. Wheeler, A.P., Mount, A.S., Swift, D.M., and Sikes, C.S., in preparation.Google Scholar
17. Myers, J.M., Veis, A., Sabsay, B., and Wheeler, A.P., Anal. Biochem., 240, p. 300–302 (1996).Google Scholar
18. Mount, A.S., Nucleation of Calcite in the Eastern Oyster, Crassostrea virginica: Biochemical and Functional Studies of the Organic Matrix from Foliated Shell, Ph.D. Dissertation, Clemson University, 1999.Google Scholar
19. Johnstone, M.B. and Wheeler, A.P., in preparation.Google Scholar
20. Borbas, J.E., Wheeler, A.P., and Sikes, C.S., J. Exper. Zool., 258, p. 1–13 (1991).Google Scholar
21. Akiyama, M., Proc. Japanese Acad., 42, p. 800–805 (1966).Google Scholar
22. Sarnata, T., Veliger, 33, p. 190–201 (1990).Google Scholar
23. Crenshaw, M., Biol. Bull., 143, p. 506–512 (1972).Google Scholar
24. Ingle, S.E., Culberson, C.H., Hawley, J.E., and Pytkowicz, R.M., Mar. Chem., 1, p. 259–307 (1972).Google Scholar
25. Greenfield, M.E., Wilson, D.C., and Crenshaw, M.A., Amer. Zool., 24, p. 925–932 (1984).Google Scholar
26. Bernhardt, A.M., Manyak, D.M., and Wilbur, K.M., J. Moll. Stud., 51, p. 284–289 (1985).Google Scholar
27. Addadi, L. and Weiner, S., Proc. Natl. Acad. Sci. USA, 82, p. 4110–4114 (1985).Google Scholar
28. Addadi, L., Moradian, J., Shay, E., Maroudas, N.C., and Weiner, S., Proc. Natl. Acad. Sci. USA, 84, p. 2732–2736 (1987).Google Scholar
29. Falini, G., Albeck, S., Weiner, S., and Addadi, L., Science, 271, p. 67–69 (1996).Google Scholar
30. Wheeler, A.P., Rusenko, K.W., George, J.W., and Sikes, C.S., Comp. Biochem. Physiol., 87B, p. 953–960 (1987).Google Scholar
31. Sikes, C.S., Wheeler, A.P., Wierzbicki, A., Mount, A.S., and Dillaman, R.M., Biol. Bull., in press.Google Scholar
32. Wheeler, A.P. and Sikes, C.S., Amer. Zool., 24, p. 933–944 (1984)Google Scholar
33. Berman, A., Addadi, L., and Weiner, S., Nature, 331, p. 546–548 (1988).Google Scholar
34. Mann, S., Didymus, J.M., Sanderson, N.P., Heywood, B.R., and Samper, E.J.A., J. Chem. Soc., Faraday Trans., 86, p. 1873–1880 (1990).Google Scholar
35. Wheeler, A.P., Low, K.C., and Sikes, C.S., in Surface Reactive Peptides and Polymers: Discovery and Commercialization, edited by Sikes, C.S. and Wheeler, A.P., (ACS, Washington, DC, 1991) p. 72–84.Google Scholar
36. Belcher, A.M., Wu, X.H., Christensen, R.J., Hansma, P.K., Stucky, G.D., and Morse, D.E., Nature, 381, p. 56–58 (1996).Google Scholar
37. Wheeler, A.P., George, J.W., and Evans, C.A., Science, 212, p. 1397–1398 (1981).Google Scholar
38. Sikes, C.S. and Wheeler, A.P., Biol. Bull., 170, p. 494–505 (1986).Google Scholar
39. Wierzbicki, A., Sikes, C.S., Madura, J.D., and Drake, B., Calc. Tiss. Int., 54, p. 133–141 (1994).Google Scholar
40. Sikes, C.S., Yeung, M.L., and Wheeler, A.P., in Surface Reactive Peptides and Polymers: Discovery and Commercialization, edited by Sikes, C.S. and Wheeler, A.P., (ACS, Washington, DC, 1991) p. 50–71.Google Scholar
41. Morrison, C., Amer. Malacol. Bull., 10, p. 1–24 (1993).Google Scholar
42. Myers, J.M., Studies on the Secretory Epithelium of the Mantle from the Eastern Oyster, Crassostrea virginica, in Relation to Shell Growth, Ph.D. Dissertation, Clemson University (1999).Google Scholar
43. Myers, J.M., Wheeler, A.P. and Silverman, H., in preparation.Google Scholar
44. Marsh, M. E. and Sass, R. L., J. Exp. Zool., 226, p. 193–203 (1983).Google Scholar
45. Wheeler, A.P. and Sikes, C.S., U.S. Patent #4,585,560, (1986).Google Scholar
46. Sikes, C.S. and Wheeler, A.P., CHEMTECH, 18, p. 620–626 (1988).Google Scholar
47. Wheeler, A.P. and Koskan, L.P., in Biomolecular Materials, edited by Viney, C., Chase, S.T., and Waite, J.H., (Mater. Res. Soc. Proc. 292, Pittsburgh, PA, 1992) p. 277–283.Google Scholar
48. Sikes, C.S. and Wierzbicki, A., in Biomimetic Materials Chemistry, edited by Mann, S., (VCH Publishers, Inc., New York, 1996) p. 249–278.Google Scholar
49. Wilson, D. and Hepburn, B.J., Corrosion 97 (NA CE), paper no. 172 (1997).Google Scholar
50. Hater, W., Corrosion 98 (NACE), paper no. 213 (1998).Google Scholar
51. DBain, I., Fan, G., and Ross, R.J., Corrosion 99 (NACE), paper no. 120 (1999).Google Scholar
52. Low, K.C., Wheeler, A.P., and Koskan, L.P., in Hydrophilic Polymers: Performance with Environmental Acceptability, edited by Glass, J.E., (ACS, Washington, DC, 1996) p. 99–111.Google Scholar
53. Neri, P., Antoni, G., Benvenuti, F., Cocola, F., and Gazzei, G., Medicinal, J. Chem., 16, p. 893–897 (1973).Google Scholar
54. Ross, R.J., Low, K.C., and Shannon, J.E., Corrosion 96 (NACE), paper no. 162 (1996).Google Scholar
55. Freeman, M.B., Paik, Y.H., Swift, G., Wilczynski, R., Wolk, S.K., and Yozum, K.M., in Hydrogels and Biodegradable Polymers for Bioapplication, (ACS, Washington, DC, 1996) p. 118–136.Google Scholar
56. Ross, R.J., Low, K.C., Koskan, L.P., and Wheeler, A.P., U.S. Patent #5,612,384 (1997).Google Scholar
57. Donachy, J.E. and Sikes, C.S., U.S. Patent #5,284,936 (1994).Google Scholar
58. Kinnersley, A.M., Koskan, L.P., Strom, D.J., and Meah, A.R.Y., U.S. Patent #5,350,735 (1994).Google Scholar
59. Wang, X.T., Zeko, A.M., and Below, F.E., Agron. Abstracts, p. 106 (1996).Google Scholar
60. Wheeler, A.P., Alford, D.D., and Pettigrew, C.A., J. Environ. Polymer Degrad., 2, p. 225–2,44 (1994).Google Scholar
61. Wolk, S.K., Swift, G., Paik, Y.H., Yocum, K.M., Smith, R.L., and Simon, E.S., Macromolecules, 27, p. 7613–7620 (1994).Google Scholar
62. Tang, Y. and Wheeler, A.P., in Polymers from Renewable Resources: Carbohydrates and Agroproteins, (ACS, Washington, DC, in press).Google Scholar
63. Kawaguchi, T. and Watabe, N., J Exp. Mar. Biol. Ecol., 170, p. 11–28 (1993).Google Scholar