Silica Nanostructures Produced Using Diatom Peptides with Designed Post‐Translational Modifications. (3rd June 2020)
- Record Type:
- Journal Article
- Title:
- Silica Nanostructures Produced Using Diatom Peptides with Designed Post‐Translational Modifications. (3rd June 2020)
- Main Title:
- Silica Nanostructures Produced Using Diatom Peptides with Designed Post‐Translational Modifications
- Authors:
- Wallace, Andrea K.
Chanut, Nicolas
Voigt, Christopher A. - Abstract:
- Abstract: Diatoms produce intricately patterned silica structures under ambient conditions, a process initiated by post‐translationally modified silaffin peptides that nucleate silicic acid. Designing these peptides would enable the production of silica nanostructures with desired properties; however, the functional effects of modifications are poorly understood. Here, Escherichia coli is used to express and modify recombinant silaffin R5 peptide from the diatom Cylindrotheca fusiformis . A library of 38 enzymes is tested for R5 modifications in vitro, from which active methyltransferases, kinases, acetyltransferases, oxidases, and myristoyltransferases are identified from diatoms, humans, yeast, and bacteria. Modified R5 peptides are used for silica precipitation and the impacts on particle size, shape, porosity, and surface area are quantified. In vivo pathways are designed to coexpress R5 and a modifying enzyme and the resulting peptide is used to nucleate silica nanostructures with controlled size (100–3500 nm), porosity (20–635 m 2 g −1 ), or embedded with melanin. It is found that phosphorylation reduces the need for inorganic phosphate during silica synthesis. The simultaneous methylation and phosphorylation of R5 leads to smaller particles requiring less inorganic phosphate. Inspired by diatoms, the use of post‐translationally modified peptides will enable the control of silica morphology under ambient conditions, with potential applications in electronics andAbstract: Diatoms produce intricately patterned silica structures under ambient conditions, a process initiated by post‐translationally modified silaffin peptides that nucleate silicic acid. Designing these peptides would enable the production of silica nanostructures with desired properties; however, the functional effects of modifications are poorly understood. Here, Escherichia coli is used to express and modify recombinant silaffin R5 peptide from the diatom Cylindrotheca fusiformis . A library of 38 enzymes is tested for R5 modifications in vitro, from which active methyltransferases, kinases, acetyltransferases, oxidases, and myristoyltransferases are identified from diatoms, humans, yeast, and bacteria. Modified R5 peptides are used for silica precipitation and the impacts on particle size, shape, porosity, and surface area are quantified. In vivo pathways are designed to coexpress R5 and a modifying enzyme and the resulting peptide is used to nucleate silica nanostructures with controlled size (100–3500 nm), porosity (20–635 m 2 g −1 ), or embedded with melanin. It is found that phosphorylation reduces the need for inorganic phosphate during silica synthesis. The simultaneous methylation and phosphorylation of R5 leads to smaller particles requiring less inorganic phosphate. Inspired by diatoms, the use of post‐translationally modified peptides will enable the control of silica morphology under ambient conditions, with potential applications in electronics and photonics. Abstract : Diatoms build tiny silica structures under ambient conditions with intricate structural and optical properties. Here, the diatom peptide (R5) is produced in E. coli with enzymes from many sources, including humans, that modify the peptide structures. These are found to precipitate silica into structures of diverse size, shape, surface area, and porosity that have applications spanning photonics to catalysis. … (more)
- Is Part Of:
- Advanced functional materials. Volume 30:Number 30(2020)
- Journal:
- Advanced functional materials
- Issue:
- Volume 30:Number 30(2020)
- Issue Display:
- Volume 30, Issue 30 (2020)
- Year:
- 2020
- Volume:
- 30
- Issue:
- 30
- Issue Sort Value:
- 2020-0030-0030-0000
- Page Start:
- n/a
- Page End:
- n/a
- Publication Date:
- 2020-06-03
- Subjects:
- melanin -- metabolic engineering -- retrosynthesis -- ribosomally synthesized and post‐translationally modified peptides (RiPPs) -- synthetic biology
Materials -- Periodicals
Chemical vapor deposition -- Periodicals
620.11 - Journal URLs:
- http://onlinelibrary.wiley.com/journal/10.1002/(ISSN)1616-3028 ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1002/adfm.202000849 ↗
- Languages:
- English
- ISSNs:
- 1616-301X
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 0696.853900
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 13693.xml