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Book chapter2022Peer reviewedOpen access

A Novel Approach for the Production of Aggregation-Prone Proteins Using the Spidroin-Derived NT* Tag

Kronqvist, N.; Rising, A.; Johansson, J.


Spiders have evolved proteins that can be kept in a highly concentrated soluble form in the silk gland yet rapidly assemble into stable silk fibers under certain environmental conditions. The transition between soluble and fibrillar states is partly regulated by the pH-sensitive N-terminal (NT) domain which has emerged as nature’s own solubility-enhancing domain. NT has an inherent capacity to keep the silk proteins’ partly hydrophobic and very aggregation-prone regions from premature fibrillation in spite of storage at enormous concentrations. The genetically engineered double-mutant NT* shows increased solubility and stability and has arisen as a powerful tool for the production of aggregation-prone as well as other recombinant proteins. Here we describe a robust and highly efficient protocol for improved soluble expression of peptides and proteins by fusion to the NT* tag.


Aggregation-prone; Amyloid; NT domain; Recombinant production; Solubility tag; Spider silk protein; Surfactant protein; Transmembrane peptide

Published in

Methods in Molecular Biology
2022, Volume: 2406, number: 2406, pages: 113-130 Title: Insoluble Proteins : Methods and Protocols
ISBN: 978-1-0716-1858-5, eISBN: 978-1-0716-1859-2
Publisher: Springer

    UKÄ Subject classification

    Biochemistry and Molecular Biology

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