Hostname: page-component-78c5997874-8bhkd Total loading time: 0 Render date: 2024-11-19T13:44:01.220Z Has data issue: false hasContentIssue false

The Influence of Molecular Structure on Apatite Adsorption

Published online by Cambridge University Press:  15 February 2011

S. A. Johnsson Mats
Affiliation:
Dept's of Biomaterials and Oral Biology, SUNY at Buffalo. Buffalo NY 14214.
P. A. Raj
Affiliation:
Dept's of Biomaterials and Oral Biology, SUNY at Buffalo. Buffalo NY 14214.
M. J. Levine
Affiliation:
Dept's of Biomaterials and Oral Biology, SUNY at Buffalo. Buffalo NY 14214.
G. H. Nancollas
Affiliation:
Dept's of Biomaterials and Oral Biology, SUNY at Buffalo. Buffalo NY 14214.
Get access

Abstract

The hydroxyapatite (HAP) adsorption of salivary statherin, cystatins, proline-rich proteins and histatins has been compared to the influence of these molecules on HAP crystallization in supersaturated solution. This may yield, in many cases, information about protein conformation in the adsorbed state. The results of studies involving both parent molecules and their fragments, indicated that statherin binds to HAP primarily with a 2–5 residues segment in the N-terminal part while the cystatins and proline-rich proteins bind through a segment 2–3 times larger.

Type
Research Article
Copyright
Copyright © Materials Research Society 1992

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

REFERENCES

1. Gron, P., Archs Oral Biol. 18,1385 (1973).Google Scholar
2. Schlesinger, D.H., Buku, A., Wyssbrod, H.R. and Hay, D.I., Int.J.Pept.Prot.Res. 30,257 (1987).Google Scholar
3. Russell, R.G.G., Muhlbauer, R.C., Bisaz, S., Williams, D.A. and Fleisch, H., Calcif.Tiss.Res. 6,183 (1970).Google Scholar
4. Fleisch, H.A., Russell, R.G.G., Bisaz, S., Muhlbauer, R.C. and Williams, D.A., Europ.J.Clin.Invest. 1,12 (1970).Google Scholar
5. Moreno, E.C. and Varughese, K., J.Cryst.Growth 53,20 (1981).Google Scholar
6. Meyer, J.L. and Nancollas, G.H., Calcif.Tiss.Res. 13,295 (1973).Google Scholar
7. Williams, G. and Sallis, J.D., Calcif.Tiss.Int. 34, 169 (1982).Google Scholar
8. Moreno, E.C., Kresak, M. and Hay, D.I., Archs Oral Biol. 23,525 (1978).Google Scholar
9. Moreno, E.C., Kresak, M. and Hay, D.I., J.Biol.Chem. 257,2981 (1982).Google Scholar
10. Schlesinger, D.H. and Hay, D.I., J.Biol.Chem. 252,1689 (1977).Google Scholar
11. Wong, R.S.C., Hofmann, T. and Bennick, A., 254,4800 (1979).Google Scholar
12. Raj, P.A., Johnsson, M., Levine, M.J. and Nancollas, G.H. J.Biol.Chem. In press.Google Scholar
13. Johnsson, M.S.A., Raj, P.A., Perich, J.W., Reynolds, E.C., Levine, M.J. and Nancollas, G.H., J.Dent.Res. 70,276 (1991).CrossRefGoogle Scholar
14. Johnsson, M., Richardson, C.F., Sallis, J.D. and Nancollas, G.H., Calcif.Tiss.Int. 49,134 (1991).Google Scholar
15. Tomson, M.B. and Nancollas, G.H., Science 200,1059 (1978).Google Scholar
16. Johnsson, M., Richardson, C.F., Bergey, E.J., Levine, M.J. and Nancollas, G.H., Archs Oral Biol. 36,631 (1991).Google Scholar
17. Richardson, C.F., Johnsson, M.S.A., Raj, P.A., Levine, M.J., Reynolds, E.C. and Nancollas, G.H., J.Dent.Res. 69,351 (1990).Google Scholar
18. Jung, A., Bisaz, S. and Fleisch, H., Calcif.Tiss.Int. 11,269 (1973).Google Scholar
19. Al-Hashimi, I., Dickinson, D.P. and Levine, M.J., J.Biol.Chem. 263,9381 (1988).Google Scholar
20. Bode, W., Engh, R., Musil, D., Thiele, U., Huber, R., Karshinov, A. Brzin, J., Kos, J. and Turk, V., EMBO J. 7,2593 (1988).Google Scholar