TY  - THES
AB  - In this work model studies on the oriented growth of CaCO3 at biomimetic interfaces were performed. The primary structure of acidic proteins which control the texture of biogenic CaCO3 were mimicked with oligoacids based on calixarenes, resorcarenes and peptides. Crystallization studies underneath Langmuir monolayers have shown that macrocyclic oligoacids act as templates for CaCO3 crystal growth. Systematic structural variations of various organic matrices and investigations on the influence of these on the growth of CaCO3 have shown that the average charge density of the organic template is the dominant factor which fixes the selection of the CaCO3 polymorphs and the growth direction of the inorganic constituents. Crystallization of CaCO3 in the presence of acidic oligopeptides yield truncated calcite rhombohedra with specifically inhibited crystal faces which has been reported before exclusively for natural acidic proteins. Since conformationally flexible peptides stabilize two energetically different crystal faces, the results point to the influence of electrostatic effects. Therefore, an epitaxial correlation is ruled out for all presented examples.
DA  - 2004
KW  - Biomineralisation , Calciumcarbonat , Amphiphile Verbindungen , Modellverbindung , Matrixproteine , Calixarene , Peptide , Monoschichten , Kristall-Engineering , Calciumcarbonat , Biomineralisation , Supramolekulare Chemie , Calixarenes , Peptides , Monolayers , Crystal engineering , Calcium carbonate , Biomineralization
LA  - ger
PY  - 2004
TI  - Modellstudien zur Funktion saurer Matrixproteine in der Biomineralisation
UR  - https://nbn-resolving.org/urn:nbn:de:hbz:361-5828
Y2  - 2024-11-22T02:57:51
ER  -