title: The role of the silicatein-alpha interactor silintaphin-1 in biomimetic biomineralization.
abstract: Biosilicification in sponges is initiated by formation of proteinaceous filaments, predominantly consisting of silicateins. Silicateins enzymatically catalyze condensation of silica nanospheres, resulting in symmetric skeletal elements (spicules). In order to create tailored biosilica structures in biomimetic approaches it is mandatory to elucidate proteins that are fundamental for the assembly of filaments. Silintaphin-1 is a core component of modularized filaments and also part of a spicule-enfolding layer. It bears no resemblance to other proteins, except for the presence of an interaction domain that is fundamental for its function as scaffold/template. In the presence of silicatein silintaphin-1 facilitates the formation of in vitro filaments. Also, it directs the assembly of gamma-Fe(2)O(3) nanoparticles and surface-immobilized silicatein to rod-like biocomposites, synthetic spicules. Thus, silintaphin-1 will contribute to biomimetic approaches that pursue a controlled formation of patterned biosilica-based materials. Its combination with gamma-Fe(2)O(3) nanoparticles and immobilized silicatein will furthermore inspire future biomedical applications and clinical diagnostics.
authors.affiliation: Institute for Physiological Chemistry and Pathobiochemistry, Johannes Gutenberg University, Medical School, Duesbergweg 6, Mainz, Germany. wiens@uni-mainz.de
authors.forename: Matthias
authors.initials: M
authors.lastname: Wiens
authors.forename: Melanie
authors.initials: M
authors.lastname: Bausen
authors.forename: Filipe
authors.initials: F
authors.lastname: Natalio
authors.forename: Thorben
authors.initials: T
authors.lastname: Link
authors.forename: Ute
authors.initials: U
authors.lastname: Schlossmacher
authors.forename: Werner E G
authors.initials: WE
authors.lastname: Müller
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D000906:Antibodies / Q000494:pharmacology; D040761:Biomimetic Materials / Q000378:metabolism*; D002113:Calcification, Physiologic / Q000187:drug effects; D002403:Cathepsins / Q000378:metabolism* / Q000648:ultrastructure; D018076:DNA, Complementary / Q000235:genetics; D004800:Enzymes, Immobilized / Q000378:metabolism; D005290:Ferric Compounds / Q000378:metabolism; D008969:Molecular Sequence Data; D011485:Protein Binding / Q000187:drug effects; D021381:Protein Transport / Q000187:drug effects; D011506:Proteins / Q000737:chemistry / Q000378:metabolism*; D011994:Recombinant Proteins / Q000378:metabolism; D012038:Regeneration / Q000187:drug effects; D012824:Silicic Acid / Q000494:pharmacology; D047233:Suberites / Q000033:anatomy & histology / Q000166:cytology / Q000187:drug effects / Q000201:enzymology*; D020798:Two-Hybrid System Techniques
chemical_list: D000906:Antibodies; D018076:DNA, Complementary; D004800:Enzymes, Immobilized; D005290:Ferric Compounds; D011506:Proteins; D011994:Recombinant Proteins; C112571:silicatein alpha; D012824:Silicic Acid; C000499:ferric oxide; D002403:Cathepsins