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Self-Assembly of Highly Phosphorylated Silaffins and Their Function in Biosilica Morphogenesis

Kröger, Nils, Lorenz, Sonja, Brunner, Eike, Sumper, Manfred·2002·Science

Abstract

Silaffins are uniquely modified peptides that have been implicated in the biogenesis of diatom biosilica. A method that avoids the harsh anhydrous hydrogen fluoride treatment commonly used to dissolve biosilica allows the extraction of silaffins in their native state. The native silaffins carry further posttranslational modifications in addition to their polyamine moieties. Each serine residue was phosphorylated, and this high level of phosphorylation is essential for biological activity. The zwitterionic structure of native silaffins enables the formation of supramolecular assemblies. Time-resolved analysis of silica morphogenesis in vitro detected a plastic silaffin-silica phase, which may represent a building material for diatom biosilica.

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Metadata

Authors
Kröger, N., Lorenz, S., Brunner, E., & Sumper, M.
Venue
Science
Published
2002-10-18
Volume
298
Issue
5593
Pages
584-586
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2003721128
Cited by
792
References
0
FWCI
25.94
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Self-Assembly of Highly Phosphorylated Silaffins and Their Function in Biosilica Morphogenesis. https://app.cochat.ai/papers/10.1126/science.1076221
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Kröger, N., Lorenz, S., Brunner, E., & Sumper, M. (2002). Self-Assembly of Highly Phosphorylated Silaffins and Their Function in Biosilica Morphogenesis. Science. https://doi.org/10.1126/science.1076221

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.