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A spidroin-derived solubility tag enables controlled aggregation of a designed amyloid protein
Karolinska Inst, Dept Neurobiol Care Sci & Soc, Div Neurogeriatr, Huddinge, Sweden..
Karolinska Inst, Dept Neurobiol Care Sci & Soc, Div Neurogeriatr, Huddinge, Sweden..
Karolinska Inst, Dept Neurobiol Care Sci & Soc, Div Neurogeriatr, Huddinge, Sweden..
Latvian Inst Organ Synth, Dept Phys Organ Chem, Riga, Latvia..
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2018 (English)In: The FEBS Journal, ISSN 1742-464X, E-ISSN 1742-4658, Vol. 285, no 10, p. 1873-1885Article in journal (Refereed) Published
Abstract [en]

Amyloidogenesis is associated with more than 30 diseases, but the molecular mechanisms involved in cell toxicity and fibril formation remain largely unknown. The inherent tendency of amyloid-forming proteins to aggregate renders expression, purification, and experimental studies challenging. NT* is a solubility tag derived from a spider silk protein that was recently introduced for the production of several aggregation-prone peptides and proteins at high yields. Herein, we investigate whether fusion to NT* can prevent amyloid fibril formation and enable controlled aggregation for experimental studies. As an example of an amyloidogenic protein, we chose the de novo-designed polypeptide 17. The fusion protein NT*-17 was recombinantly expressed in Escherichia coli to produce high amounts of soluble and mostly monomeric protein. Structural analysis showed that 17 is kept in a largely unstructured conformation in fusion with NT*. After proteolytic release, 17 adopts a -sheet conformation in a pH- and salt-dependent manner and assembles into amyloid-like fibrils. The ability of NT* to prevent premature aggregation and to enable structural studies of prefibrillar states may facilitate investigation of proteins involved in amyloid diseases.

Place, publisher, year, edition, pages
WILEY , 2018. Vol. 285, no 10, p. 1873-1885
Keywords [en]
amyloid disease, fibril formation, model protein, protein assembly, protein domain
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:kth:diva-231232DOI: 10.1111/febs.14451ISI: 000434177700010PubMedID: 29604175Scopus ID: 2-s2.0-85045301719OAI: oai:DiVA.org:kth-231232DiVA, id: diva2:1228138
Note

QC 20180627

Available from: 2018-06-27 Created: 2018-06-27 Last updated: 2018-06-27Bibliographically approved

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Purhonen, PasiHebert, Hans

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