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Siliplant1 B-domain precipitates silica spheres, aggregates, or gel, depending on Si-precursor to peptide ratios.
Ayieko, Vincent Otieno; Cohen, Lilian; Diehn, Sabrina; Goobes, Gil; Elbaum, Rivka.
Afiliación
  • Ayieko VO; The Robert H. Smith Institute of Plant Sciences and Genetics in Agriculture, The Hebrew University of Jerusalem, 7610001 Rehovot, Israel.
  • Cohen L; Department of Chemistry, Bar-Ilan University, Ramat Gan 5290002, Israel.
  • Diehn S; The Robert H. Smith Institute of Plant Sciences and Genetics in Agriculture, The Hebrew University of Jerusalem, 7610001 Rehovot, Israel.
  • Goobes G; Department of Chemistry, Bar-Ilan University, Ramat Gan 5290002, Israel.
  • Elbaum R; The Robert H. Smith Institute of Plant Sciences and Genetics in Agriculture, The Hebrew University of Jerusalem, 7610001 Rehovot, Israel. Electronic address: rivka.elbaum@mail.huji.ac.il.
Colloids Surf B Biointerfaces ; 232: 113582, 2023 Dec.
Article en En | MEDLINE | ID: mdl-37862949
Silica is extensively deposited by plants, however, only little is known about the molecular control over this process. Siliplant1 is the only known plant protein to precipitate biosilica. The protein contains seven repeats made of three domains. One of the domains exhibits a conserved sequence, which catalyzes silica precipitation in vitro. Here, silica was synthesized by the activity of a peptide carrying this conserved sequence. Infrared spectroscopy and thermal gravimetric analyses showed that the peptide was bound to the mineral. Scanning electron microscopy showed that silica-peptide particles of 22 ± 4 nm aggregated to spherical structures of 200-300 nm when the ratio of silicic acid to the peptide was below 183:1 molecules. When the ratio was about 183:1, similar particles aggregated into irregular structures, and silica gel formed at higher ratios. Solid-state NMR spectra indicated that the irregular aggregates were richer in Si-O-Si bonds as well as disordered peptide. Our results suggest that the peptide catalyzed the condensation of silicic acid and the formation of ∼20 nm particles, which aggregated into spheres. Excess of the peptide stabilized surface Si-OH groups that prevented spontaneous Si-O-Si bonding between aggregates. Under Si concentrations relevant to plant sap, the peptide and possibly Siliplant1, could catalyze nucleation of silica particles that aggregate into spherical aggregates.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Ácido Silícico / Dióxido de Silicio Idioma: En Revista: Colloids Surf B Biointerfaces Asunto de la revista: QUIMICA Año: 2023 Tipo del documento: Article País de afiliación: Israel Pais de publicación: Países Bajos
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Ácido Silícico / Dióxido de Silicio Idioma: En Revista: Colloids Surf B Biointerfaces Asunto de la revista: QUIMICA Año: 2023 Tipo del documento: Article País de afiliación: Israel Pais de publicación: Países Bajos