Physico-chemical properties of functionally adhesive spider silk nanofibres. (2nd February 2023)
- Record Type:
- Journal Article
- Title:
- Physico-chemical properties of functionally adhesive spider silk nanofibres. (2nd February 2023)
- Main Title:
- Physico-chemical properties of functionally adhesive spider silk nanofibres
- Authors:
- Joel, Anna-Christin
Rawal, Aditya
Yao, Yin
Jenner, Andrew
Ariotti, Nicholas
Weissbach, Margret
Adler, Lewis
Stafstrom, Jay
Blamires, Sean J. - Abstract:
- Abstract : In nano-scale spider silk fibres, typically secondary protein structures are lost and the silk becomes very compliant. Additionally, due to a changed amino acid composition, a suit of new functionalities can be gained. Abstract : Currently, synthetic fibre production focuses primarily on high performance materials. For high performance fibrous materials, such as silks, this involves interpreting the structure–function relationship and downsizing to a smaller scale to then harness those properties within synthetic products. Spiders create an array of fibres that range in size from the micrometre to nanometre scale. At about 20 nm diameter spider cribellate silk, the smallest of these silks, is too small to contain any of the typical secondary protein structures of other spider silks, let alone a hierarchical skin-core-type structure. Here, we performed a multitude of investigations to elucidate the structure of cribellate spider silk. These confirmed our hypothesis that, unlike all other types of spider silk, it has a disordered molecular structure. Alanine and glycine, the two amino acids predominantly found in other spider silks, were much less abundant and did not form the usual α-helices and β-sheet secondary structural arrangements. Correspondingly, we characterized the cribellate silk nanofibre to be very compliant. This characterization matches its function as a dry adhesive within the capture threads of cribellate spiders. Our results imply that atAbstract : In nano-scale spider silk fibres, typically secondary protein structures are lost and the silk becomes very compliant. Additionally, due to a changed amino acid composition, a suit of new functionalities can be gained. Abstract : Currently, synthetic fibre production focuses primarily on high performance materials. For high performance fibrous materials, such as silks, this involves interpreting the structure–function relationship and downsizing to a smaller scale to then harness those properties within synthetic products. Spiders create an array of fibres that range in size from the micrometre to nanometre scale. At about 20 nm diameter spider cribellate silk, the smallest of these silks, is too small to contain any of the typical secondary protein structures of other spider silks, let alone a hierarchical skin-core-type structure. Here, we performed a multitude of investigations to elucidate the structure of cribellate spider silk. These confirmed our hypothesis that, unlike all other types of spider silk, it has a disordered molecular structure. Alanine and glycine, the two amino acids predominantly found in other spider silks, were much less abundant and did not form the usual α-helices and β-sheet secondary structural arrangements. Correspondingly, we characterized the cribellate silk nanofibre to be very compliant. This characterization matches its function as a dry adhesive within the capture threads of cribellate spiders. Our results imply that at extremely small scales there may be a limit reached below which a silk will lose its structural, but not functional, integrity. Nano-sized fibres, such as cribellate silk, thus offer a new opportunity for inspiring the creation of novel scaled-down functional adhesives and nano meta-materials. … (more)
- Is Part Of:
- Biomaterials science. Volume 11:Number 6(2023)
- Journal:
- Biomaterials science
- Issue:
- Volume 11:Number 6(2023)
- Issue Display:
- Volume 11, Issue 6 (2023)
- Year:
- 2023
- Volume:
- 11
- Issue:
- 6
- Issue Sort Value:
- 2023-0011-0006-0000
- Page Start:
- 2139
- Page End:
- 2150
- Publication Date:
- 2023-02-02
- Subjects:
- Biomedical materials -- Periodicals
610.28 - Journal URLs:
- http://pubs.rsc.org/en/journals/journalissues/bm ↗
http://www.rsc.org/ ↗ - DOI:
- 10.1039/d2bm01599d ↗
- Languages:
- English
- ISSNs:
- 2047-4830
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 2087.724000
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 26159.xml