Berlin 2012 – scientific programme

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BP: Fachverband Biologische Physik

BP 10: Biopolymers and Biomaterials (with CPP)

BP 10.11: Talk

Tuesday, March 27, 2012, 12:30–12:45, H 1058

Subspecies of nacre protein “perlucin” favors binding to aragonite over binding to calcite microcrystals — •Hanna Rademaker, Malte Launspach, and Monika Fritz — Institute for Biophysics, University of Bremen, Germany

Nacre is a compound material of calcium carbonate platelets and organic layers of chitin and proteins. The outstanding mechanical properties of nacre make it desirable to understand the details of the biomineralizing process. The calcium carbonate platelets in nacre show the crystal structure of aragonite and not of calcite. Therefore we are especially interested in proteins which favor binding to aragonite over binding to calcite. We adapted a simple detection method from Suzuki et al. [1] for this purpose.

In this work [2] biomineralizing proteins were chemically removed from the acid-insoluble matrix of nacre from Haliotis laevigata and incubated with aragonite and calcite microcrystals, respectively. The crystals were washed and then dissolved. SDS-PAGE of these solutions showed that one protein, a subspecies of perlucin, favors binding to aragonite crystals. This might be a hint that perlucin plays a key role in the biomineralization process.

[1] M. Suzuki et al., Science, 325 (5946), 1388-1390, 2009

[2] H. Rademaker and M. Launspach, Beilstein J. Nanotechnol., 2, 222-227, 2011