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Tuning of Crystal Nucleation and Growth by Proteins: Molecular Interactions at Solid-Liquid Interfaces in Biomineralization

L. Addadi ; Departments of Structural Chemistry** and Isotope Research* The Weizmann Institute of Science, Rehovot, 76100 Israel
A. Berman ; Departments of Structural Chemistry** and Isotope Research* The Weizmann Institute of Science, Rehovot, 76100 Israel
J. Moradian-Oldak ; Departments of Structural Chemistry** and Isotope Research* The Weizmann Institute of Science, Rehovot, 76100 Israel
S. Weiner ; Departments of Structural Chemistry** and Isotope Research* The Weizmann Institute of Science, Rehovot, 76100 Israel

Puni tekst: engleski, pdf (7 MB) str. 539-544 preuzimanja: 203* citiraj
APA 6th Edition
Addadi, L., Berman, A., Moradian-Oldak, J. i Weiner, S. (1990). Tuning of Crystal Nucleation and Growth by Proteins: Molecular Interactions at Solid-Liquid Interfaces in Biomineralization. Croatica Chemica Acta, 63 (3), 539-544. Preuzeto s https://hrcak.srce.hr/137390
MLA 8th Edition
Addadi, L., et al. "Tuning of Crystal Nucleation and Growth by Proteins: Molecular Interactions at Solid-Liquid Interfaces in Biomineralization." Croatica Chemica Acta, vol. 63, br. 3, 1990, str. 539-544. https://hrcak.srce.hr/137390. Citirano 06.03.2021.
Chicago 17th Edition
Addadi, L., A. Berman, J. Moradian-Oldak i S. Weiner. "Tuning of Crystal Nucleation and Growth by Proteins: Molecular Interactions at Solid-Liquid Interfaces in Biomineralization." Croatica Chemica Acta 63, br. 3 (1990): 539-544. https://hrcak.srce.hr/137390
Harvard
Addadi, L., et al. (1990). 'Tuning of Crystal Nucleation and Growth by Proteins: Molecular Interactions at Solid-Liquid Interfaces in Biomineralization', Croatica Chemica Acta, 63(3), str. 539-544. Preuzeto s: https://hrcak.srce.hr/137390 (Datum pristupa: 06.03.2021.)
Vancouver
Addadi L, Berman A, Moradian-Oldak J, Weiner S. Tuning of Crystal Nucleation and Growth by Proteins: Molecular Interactions at Solid-Liquid Interfaces in Biomineralization. Croatica Chemica Acta [Internet]. 1990 [pristupljeno 06.03.2021.];63(3):539-544. Dostupno na: https://hrcak.srce.hr/137390
IEEE
L. Addadi, A. Berman, J. Moradian-Oldak i S. Weiner, "Tuning of Crystal Nucleation and Growth by Proteins: Molecular Interactions at Solid-Liquid Interfaces in Biomineralization", Croatica Chemica Acta, vol.63, br. 3, str. 539-544, 1990. [Online]. Dostupno na: https://hrcak.srce.hr/137390. [Citirano: 06.03.2021.]

Sažetak
The mineralized tissues of a bivalve mollusk and a sea urchin are both composed of calcium carbonate crystals that are intimately associated with acidic glycoproteins. In vitro studies in which carboxylate-, carbonate- and phosphate-containing crystals are grown in the presence of partially purified acidic glycoproteins from these two tissues show that some of these macro- molecules are able to interact specifically with certain crystal faces. Significantly all the affected crystal faces contain a common stereochemical motif. Interesting differences, however, were observed in the modes of interaction between the mollusk and sea urchin derived acidic glycoproteins. Only the former can induce oriented calcite nucleation in vitro and only the latter can interact from solution with specific calcite crystal faces. These differences are ascribed in part to the fact that the mollusk macromolecules are much more acidic than those from the sea urchin. Some of the acidic glycoproteins are also occluded inside the growing crystals. In the case of the sea urchin, and not of the mollusk, the proteins are preferentially located at specific crystal planes and their presence influences the mechanical properties of the crystal. A detailed study of these composite crystals by X-ray synchrotron radiation shows how the presence of the protein influences the crystal mosaicity. The interactions revealed by these studies follow well defined stereochemical rules, tuned by electrostatic forces. They, in turn, provide new 'insight into some of the basic underlying processes occurring in biomineralization.

Hrčak ID: 137390

URI
https://hrcak.srce.hr/137390

Posjeta: 382 *