Spidroin N-terminal domain forms amyloid-like fibril based hydrogels and provides a protein immobili...
Spidroin N-terminal domain forms amyloid-like fibril based hydrogels and provides a protein immobilization platform
About this item
Full title
Author / Creator
Arndt, Tina , Jaudzems, Kristaps , Shilkova, Olga , Francis, Juanita , Johansson, Mathias , Laity, Peter R. , Sahin, Cagla , Chatterjee, Urmimala , Kronqvist, Nina , Barajas-Ledesma, Edgar , Kumar, Rakesh , Chen, Gefei , Strömberg, Roger , Abelein, Axel , Langton, Maud , Landreh, Michael , Barth, Andreas , Holland, Chris , Johansson, Jan , Rising, Anna and Sveriges lantbruksuniversitet
Publisher
London: Nature Publishing Group UK
Journal title
Language
English
Formats
Publication information
Publisher
London: Nature Publishing Group UK
Subjects
More information
Scope and Contents
Contents
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, rapi...
Alternative Titles
Full title
Spidroin N-terminal domain forms amyloid-like fibril based hydrogels and provides a protein immobilization platform
Authors, Artists and Contributors
Author / Creator
Jaudzems, Kristaps
Shilkova, Olga
Francis, Juanita
Johansson, Mathias
Laity, Peter R.
Sahin, Cagla
Chatterjee, Urmimala
Kronqvist, Nina
Barajas-Ledesma, Edgar
Kumar, Rakesh
Chen, Gefei
Strömberg, Roger
Abelein, Axel
Langton, Maud
Landreh, Michael
Barth, Andreas
Holland, Chris
Johansson, Jan
Rising, Anna
Sveriges lantbruksuniversitet
Identifiers
Primary Identifiers
Record Identifier
TN_cdi_doaj_primary_oai_doaj_org_article_797818a67a6f4d898230e24aa54af69c
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_797818a67a6f4d898230e24aa54af69c
Other Identifiers
ISSN
2041-1723
E-ISSN
2041-1723
DOI
10.1038/s41467-022-32093-7
