Engineering protein filaments with enhanced thermostability for nanomaterials. Issue 2 (29th November 2012)
- Record Type:
- Journal Article
- Title:
- Engineering protein filaments with enhanced thermostability for nanomaterials. Issue 2 (29th November 2012)
- Main Title:
- Engineering protein filaments with enhanced thermostability for nanomaterials
- Authors:
- Glover, Dominic J.
Giger, Lars
Kim, Jihyun R.
Clark, Douglas S. - Abstract:
- <abstract abstract-type="main" xml:lang="en"> <title>Abstract</title> <p>Self‐assembling protein templates have enormous potential as biomaterials for the fabrication of multifunctional nanostructures that require precise positioning of individual molecules in regular patterns over large surface areas. Furthermore, the development of protein templates that are stable under extreme conditions of heat or chemical denaturants will expand processing conditions and end‐use applications for biomaterials that require exceptional stability and robustness. In the present work, we characterized the high thermal stability of a filamentous protein template, the γ‐prefoldin (γPFD) from the hyperthermophile <italic>Methanocaldococcus jannaschii</italic>, and subsequently used rational design to further enhance the filament's thermal stability for application as a biotemplate in the creation of platinum nanowires. The γPFD assembles into long fibers with lengths that exceed 2 μm, which when heated to various temperatures and examined by transmission electron microscopy, revealed a <italic>T</italic><sub>m</sub> of 93°C for the quaternary filament structure. Subsequently, we increased the hydrophobicity of the α‐helices of the γPFD's coiled‐coil, which appeared to strengthen the filamentous structure, leading to filaments of greater length at elevated temperatures. These enhanced filaments functioned as templates for the synthesis of platinum nanowires at unprecedented temperatures, and may<abstract abstract-type="main" xml:lang="en"> <title>Abstract</title> <p>Self‐assembling protein templates have enormous potential as biomaterials for the fabrication of multifunctional nanostructures that require precise positioning of individual molecules in regular patterns over large surface areas. Furthermore, the development of protein templates that are stable under extreme conditions of heat or chemical denaturants will expand processing conditions and end‐use applications for biomaterials that require exceptional stability and robustness. In the present work, we characterized the high thermal stability of a filamentous protein template, the γ‐prefoldin (γPFD) from the hyperthermophile <italic>Methanocaldococcus jannaschii</italic>, and subsequently used rational design to further enhance the filament's thermal stability for application as a biotemplate in the creation of platinum nanowires. The γPFD assembles into long fibers with lengths that exceed 2 μm, which when heated to various temperatures and examined by transmission electron microscopy, revealed a <italic>T</italic><sub>m</sub> of 93°C for the quaternary filament structure. Subsequently, we increased the hydrophobicity of the α‐helices of the γPFD's coiled‐coil, which appeared to strengthen the filamentous structure, leading to filaments of greater length at elevated temperatures. These enhanced filaments functioned as templates for the synthesis of platinum nanowires at unprecedented temperatures, and may create new opportunities for other applications of nanoscale biotemplates that require exceptional thermal stability.</p> <p>See accompanying commentary by Jonathan S. Dordick DOI: <ext-link ext-link-type="doi" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink">10.1002/biot.201200338</ext-link></p> </abstract> … (more)
- Is Part Of:
- Biotechnology journal. Volume 8:Issue 2(2013:Feb.)
- Journal:
- Biotechnology journal
- Issue:
- Volume 8:Issue 2(2013:Feb.)
- Issue Display:
- Volume 8, Issue 2 (2013)
- Year:
- 2013
- Volume:
- 8
- Issue:
- 2
- Issue Sort Value:
- 2013-0008-0002-0000
- Page Start:
- 228
- Page End:
- 236
- Publication Date:
- 2012-11-29
- Subjects:
- Biotechnology -- Periodicals
660.605 - Journal URLs:
- http://onlinelibrary.wiley.com/journal/10.1002/(ISSN)1860-7314 ↗
http://www.biotechnology-journal.com ↗
http://www3.interscience.wiley.com/cgi-bin/jabout/110544531/2446%5Finfo.html ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1002/biot.201200009 ↗
- Languages:
- English
- ISSNs:
- 1860-6768
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 2089.862350
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 4252.xml