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Spidroin N-terminal...
Spidroin N-terminal domain forms amyloid-like fibril based hydrogels and provides a protein immobilization platform
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Arndt, Tina (author)
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Jaudzems, Kristaps (author)
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- Shilkova, Olga (author)
- Karolinska Institutet
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Francis, Juanita (author)
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- Johansson, Mathias (author)
- Swedish University of Agricultural Sciences,Sveriges lantbruksuniversitet,Institutionen för Molekylära vetenskaper,Department of Molecular Sciences
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Laity, Peter R. (author)
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- Sahin, Cagla (author)
- Karolinska Institutet
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- Chatterjee, Urmimala (author)
- Karolinska Institutet
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- Kronqvist, Nina (author)
- Karolinska Institutet
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Barajas-Ledesma, Edgar (author)
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- Kumar, Rakesh (author)
- Karolinska Institutet
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- Chen, Gefei (author)
- Karolinska Institutet
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Strömberg, Roger (author)
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- Abelein, Axel (author)
- Karolinska Institutet
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- Langton, Maud (author)
- Swedish University of Agricultural Sciences,Sveriges lantbruksuniversitet,Institutionen för Molekylära vetenskaper,Department of Molecular Sciences
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- Landreh, Michael (author)
- Karolinska Institutet
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- Barth, Andreas (author)
- Stockholms universitet,Institutionen för biokemi och biofysik
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Holland, Chris (author)
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- Johansson, Jan (author)
- Karolinska Institutet
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- Rising, Anna (author)
- Swedish University of Agricultural Sciences,Sveriges lantbruksuniversitet,Institutionen för anatomi, fysiologi och biokemi,Department of Anatomy, Physiology and Biochemistry (AFB),Karolinska Institutet
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(creator_code:org_t)
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- 2022-08-15
- 2022
- English.
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In: Nature Communications. - : Springer Science and Business Media LLC. - 2041-1723. ; 13
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https://doi.org/10.1...
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https://pub.epsilon.... (primary) (Raw object) (free)
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https://urn.kb.se/re...
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https://doi.org/10.1...
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Abstract
Subject headings
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- Recombinant spider silk proteins (spidroins) have multiple potential applications in development of novel biomaterials, but their multimodal and aggregation-prone nature have complicated production and straightforward applications. Here, we report that recombinant miniature spidroins, and importantly also the N-terminal domain (NT) on its own, rapidly form self-supporting and transparent hydrogels at 37 °C. The gelation is caused by NT α-helix to β-sheet conversion and formation of amyloid-like fibrils, and fusion proteins composed of NT and green fluorescent protein or purine nucleoside phosphorylase form hydrogels with intact functions of the fusion moieties. Our findings demonstrate that recombinant NT and fusion proteins give high expression yields and bestow attractive properties to hydrogels, e.g., transparency, cross-linker free gelation and straightforward immobilization of active proteins at high density.
Subject headings
- NATURVETENSKAP -- Biologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences (hsv//eng)
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
Publication and Content Type
- ref (subject category)
- art (subject category)
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To the university's database
- By the author/editor
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Arndt, Tina
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Jaudzems, Krista ...
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Shilkova, Olga
-
Francis, Juanita
-
Johansson, Mathi ...
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Laity, Peter R.
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show more...
-
Sahin, Cagla
-
Chatterjee, Urmi ...
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Kronqvist, Nina
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Barajas-Ledesma, ...
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Kumar, Rakesh
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Chen, Gefei
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Strömberg, Roger
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Abelein, Axel
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Langton, Maud
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Landreh, Michael
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Barth, Andreas
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Holland, Chris
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Johansson, Jan
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Rising, Anna
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show less...
- About the subject
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- NATURAL SCIENCES
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NATURAL SCIENCES
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and Biological Scien ...
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- NATURAL SCIENCES
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NATURAL SCIENCES
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and Biological Scien ...
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and Biochemistry and ...
- Articles in the publication
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Nature Communica ...
- By the university
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Stockholm University
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Karolinska Institutet
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Swedish University of Agricultural Sciences