ArticleMethods in molecular biology (Clifton, N.J.)2022
A Novel Approach for the Production of Aggregation-Prone Proteins Using the Spidroin-Derived NT* Tag.
Article in Methods in molecular biology (Clifton, N.J.), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- The inhibitory action of the chaperone BRICHOS against the α-Synuclein secondary nucleation pathway.Nature communications · 2024Article
- The dimerization mechanism of the N-terminal domain of spider silk proteins is conserved despite extensive sequence divergence.The Journal of biological chemistry · 2022Article
- Solution Structure of Tubuliform Spidroin N-Terminal Domain and Implications for pH Dependent Dimerization.Frontiers in molecular biosciences · 2022Article
- The collectin SP-A and its trimeric recombinant fragment protect alveolar epithelial cells from the cytotoxic and proinflammatory effects of human cathelicidinFrontiers in immunology · 2022Article
- Cooperative action of SP-A and its trimeric recombinant fragment with polymyxins against Gram-negative respiratory bacteria.Frontiers in immunology · 2022Article
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Authors and funding
3 authors.
Funding
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Abstract
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.
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