2017
DOI: 10.1016/j.procbio.2017.04.004
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Novel silica-forming peptides derived from Ectocarpus siliculosus

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Cited by 26 publications
(9 citation statements)
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“…1 a). The silica-forming Ectp1 peptide has been known to be capable of binding to mineral surface as well as allowing rapid silica deposition from silicic acid [ 20 ]. The sequence of negatively charged hexaglutamate (E6) was fused into the N-terminus of Ectp1 peptide, enabling the physical adsorption onto the surface of β-TCP particles via ionic interactions with the underlying positively charged calcium ions.…”
Section: Resultsmentioning
confidence: 99%
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“…1 a). The silica-forming Ectp1 peptide has been known to be capable of binding to mineral surface as well as allowing rapid silica deposition from silicic acid [ 20 ]. The sequence of negatively charged hexaglutamate (E6) was fused into the N-terminus of Ectp1 peptide, enabling the physical adsorption onto the surface of β-TCP particles via ionic interactions with the underlying positively charged calcium ions.…”
Section: Resultsmentioning
confidence: 99%
“…Considering that the mechanical property of hybrid composite strongly depends on interfacial bridging between organic polymer and inorganic particles [ 18 ], the incorporation of β-TCP with collagen (Col/β-TCP) could be an attractive approach to accomplish tailored delivery of BMP-2 and essential mechanical stiffness at different stage of bone regeneration. Second, the skeletal architectures of brown algae are composed of hierarchical silica nanostructures containing organic components that rapidly form silica nanoparticles (SiNPs) under physiological conditions [ 19 , 20 ]. This natural biosilica formation for protection and mechanical support has provided a captivating source as a more attractive approach for silica synthesis in biomedical applications over the conventional sol-gel methods due to mild processing in ambient temperature and pH without the presence of hazardous chemicals.…”
Section: Introductionmentioning
confidence: 99%
“…The EctP1 peptide (SSRSSSHRRHDHHDHRRGS) was genetically fused to the C-terminus of the bioengineered mussel adhesive protein (MAP) and named sMAP. sMAP was produced in an Escherichia coli expression system and purified following a previously reported method .…”
Section: Methodsmentioning
confidence: 99%
“…It has been reported that EctP1 has a superior silica-forming ability to the R5 peptide, which has been commonly used for biosilica formation. 27…”
Section: ■ Introductionmentioning
confidence: 99%
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