Covalent modification of chitin with silk-derivatives acts as an amphiphilic self-organizing template in nacre biomineralisation

Weiss, Ingrid M. and Kaufmann, Stefan and Heiland, Birgit and Tanaka, Motomu (2009) Covalent modification of chitin with silk-derivatives acts as an amphiphilic self-organizing template in nacre biomineralisation. JOURNAL OF STRUCTURAL BIOLOGY, 167 (1). pp. 68-75. ISSN 1047-8477, 1095-8657

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Abstract

Molluscs have a well-deserved reputation for being expert mineralizers of various shell types such as nacre. Nacre is defined as regularly arranged layers and stacks of similar to 0.5 mu m thick aragonite platelets that are extracellularly formed within a complex mixture of organic matrix. The control of species-specific layer thickness by the animal is still enigmatic. Despite the recent findings on the periodic layer-by-layer structures of chitin layers and silk-like protein layers in nacre-type biominerals, little is known about how the interface is defined between two different layers. In this paper, we demonstrate the presence of covalently attached, hydrophobic amino acid side chains in the chitin matrix in the bivalve mollusc Mytilus galloprovincialis by the combination of infrared spectroscopy and mass spectroscopy. The accumulation of the modified chitin matrix at the interface is quantified by the critical aggregate concentration of the purified chitin matrix, which is approximately an order of magnitude smaller than that of pure chitin. Our finding suggests an active role of such chemically modified chito-oligosaccharides in the creation of a defined interface and guidance of the periodic matrix textures, which would result in unique material properties of natural mollusc shells. (C) 2009 Elsevier Inc. All rights reserved.

Item Type: Article
Uncontrolled Keywords: MOLLUSK SHELL FORMATION; X-RAY-DIFFRACTION; MECHANICAL-PROPERTIES; 2-AMINOBENZOIC ACID; CALCIUM-CARBONATE; CRUSTACEAN CHITIN; LARVAL SHELLS; ATRINA-RIGIDA; AMINO-ACIDS; MATRIX; Chitin; Oligosaccharide; Mollusc shell; Nacre; Self-assembly
Subjects: 500 Science > 570 Life sciences
Divisions: Biology, Preclinical Medicine > Institut für Biochemie, Genetik und Mikrobiologie > Lehrstuhl für Biochemie I
Depositing User: Dr. Gernot Deinzer
Date Deposited: 14 Sep 2020 05:44
Last Modified: 14 Sep 2020 05:44
URI: https://pred.uni-regensburg.de/id/eprint/28767

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