Dresden 2014 – wissenschaftliches Programm
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O: Fachverband Oberflächenphysik
O 31: Molecular Films: Properties and Preparation
O 31.4: Vortrag
Dienstag, 1. April 2014, 11:15–11:30, WIL A317
Molecular level insights into diatom biomineralization — •Helmut Lutz1, Joe Baio2, Adrienne Roehrich3, Mischa Bonn1, Gary Drobny3, and Tobias Weidner1 — 1Max Planck Institute for Polymer Research, Ackermannweg 10, 55128 Mainz — 2Oregon State University, Merryfield South 102A, Corvallis OR 97331 — 3University of Washington, Seattle, Washington 98195, United States
The nano-patterned silica shells of diatoms represent a remarkable example for biomineralization, a process controlled by protein*mineral interactions. Within the unicellular algae Cylindrotheca fusiformis, the silaffin proteins play a crucial role in the molecular biomineralization machinery. A specific repeat unit within the silaffin precursor protein, SSKKSGSYSGSKGSKRRIL (R5), precipitates silica-peptide nanoparticles out of a solution of silicic acid. We found that artificial peptides consisting of lysine and leucine (LK peptides) can mimic this capability of forming various biosilica structures. These peptides were designed to adopt helical or beta-sheet structures due to their hydrophobic periodicities and represent simple model systems to study the effect of protein folding on mineralization. In order to propose rational protein- and surface design rules it is essential to elucidate the driving force of the biosilification process. By means of surface sensitive techniques, e.g. sum frequency generation (SFG) we have studied the interactions of R5 and the LK peptides within biosilica composites and on silica surfaces.