KOPS - Das Institutionelle Repositorium der Universität Konstanz

Secrets of the Sea Urchin Spicule Revealed : Protein Cooperativity Is Responsible for ACC Transformation, Intracrystalline Incorporation, and Guided Mineral Particle Assembly in Biocomposite Material Formation

Secrets of the Sea Urchin Spicule Revealed : Protein Cooperativity Is Responsible for ACC Transformation, Intracrystalline Incorporation, and Guided Mineral Particle Assembly in Biocomposite Material Formation

Zitieren

Dateien zu dieser Ressource

Prüfsumme: MD5:466cdd8e091b5c1609b04ffc5d953a9a

PENDOLA, Martin, Gaurav JAIN, Yu-Chieh HUANG, Denis GEBAUER, John Spencer EVANS, 2018. Secrets of the Sea Urchin Spicule Revealed : Protein Cooperativity Is Responsible for ACC Transformation, Intracrystalline Incorporation, and Guided Mineral Particle Assembly in Biocomposite Material Formation. In: ACS Omega. 3(9), pp. 11823-11830. eISSN 2470-1343. Available under: doi: 10.1021/acsomega.8b01697

@article{Pendola2018-09-30Secre-43743, title={Secrets of the Sea Urchin Spicule Revealed : Protein Cooperativity Is Responsible for ACC Transformation, Intracrystalline Incorporation, and Guided Mineral Particle Assembly in Biocomposite Material Formation}, year={2018}, doi={10.1021/acsomega.8b01697}, number={9}, volume={3}, journal={ACS Omega}, pages={11823--11830}, author={Pendola, Martin and Jain, Gaurav and Huang, Yu-Chieh and Gebauer, Denis and Evans, John Spencer} }

<rdf:RDF xmlns:dcterms="http://purl.org/dc/terms/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" xmlns:bibo="http://purl.org/ontology/bibo/" xmlns:dspace="http://digital-repositories.org/ontologies/dspace/0.1.0#" xmlns:foaf="http://xmlns.com/foaf/0.1/" xmlns:void="http://rdfs.org/ns/void#" xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > <rdf:Description rdf:about="https://kops.uni-konstanz.de/rdf/resource/123456789/43743"> <dc:contributor>Pendola, Martin</dc:contributor> <foaf:homepage rdf:resource="http://localhost:8080/jspui"/> <dcterms:title>Secrets of the Sea Urchin Spicule Revealed : Protein Cooperativity Is Responsible for ACC Transformation, Intracrystalline Incorporation, and Guided Mineral Particle Assembly in Biocomposite Material Formation</dcterms:title> <dcterms:rights rdf:resource="https://kops.uni-konstanz.de/page/termsofuse"/> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2018-11-09T08:21:47Z</dcterms:available> <dcterms:issued>2018-09-30</dcterms:issued> <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/rdf/resource/123456789/29"/> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2018-11-09T08:21:47Z</dc:date> <dc:creator>Gebauer, Denis</dc:creator> <dc:creator>Huang, Yu-Chieh</dc:creator> <bibo:uri rdf:resource="https://kops.uni-konstanz.de/handle/123456789/43743"/> <dspace:hasBitstream rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/43743/3/Pendola_2-15jm0598v0fzk4.pdf"/> <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/> <dc:contributor>Evans, John Spencer</dc:contributor> <dc:contributor>Huang, Yu-Chieh</dc:contributor> <dc:creator>Jain, Gaurav</dc:creator> <dcterms:abstract xml:lang="eng">The formation of the sea urchin spicule involves the stabilization and transformation of amorphous calcium carbonate (ACC) and assembly of ACC nanoparticle precursors into a mesoscale single crystal of fracture-resistant calcite. This process of particle assembly or attachment is under the control of a family of proteins known as the spicule matrix [Strongylocentrotus purpuratus (SpSM)] proteome. Recently, two members of this proteome, SpSM50 and the glycoprotein SpSM30B/C-G (in recombinant forms), were found to interact together via SpSM30B/C-G oligosaccharide–SpSM50 protein interactions to form hybrid protein hydrogels with unique physical properties. In this study, we investigate the mineralization properties of this hybrid hydrogel alongside the hydrogels formed by SpSM50 and SpSM30B/C-G individually. We find that the SpSM50 + SpSM30B/C-G hybrid hydrogel is synergistic with regard to surface modifications and intracrystalline inclusions of existing calcite crystals, the inhibition of ACC formation, and the kinetic destabilization of ACC to form a crystalline phase. Most importantly, the hybrid hydrogel phase assembles and organizes mineral particles into discrete clusters or domains within in vitro mineralization environments. Thus, the interactions of SpSM50 and SpSM30B/C-G, mediated by carbohydrate–protein binding, reflect the need for protein cooperativity for the ACC-to-crystalline transformation, intracrystalline void formation, and guided mineral particle assembly processes that are instrumental in spicule formation.</dcterms:abstract> <dc:creator>Evans, John Spencer</dc:creator> <dc:contributor>Gebauer, Denis</dc:contributor> <dc:rights>terms-of-use</dc:rights> <dc:creator>Pendola, Martin</dc:creator> <dcterms:hasPart rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/43743/3/Pendola_2-15jm0598v0fzk4.pdf"/> <dc:language>eng</dc:language> <dc:contributor>Jain, Gaurav</dc:contributor> <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/rdf/resource/123456789/29"/> </rdf:Description> </rdf:RDF>

Dateiabrufe seit 09.11.2018 (Informationen über die Zugriffsstatistik)

Pendola_2-15jm0598v0fzk4.pdf 20

Das Dokument erscheint in:

KOPS Suche


Stöbern

Mein Benutzerkonto