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A spidroin-derived ...
A spidroin-derived solubility tag enables controlled aggregation of a designed amyloid protein
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- Sarr, Medoune (författare)
- Karolinska Institutet
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- Kronqvist, Nina (författare)
- Karolinska Institutet
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- Chen, Gefei (författare)
- Karolinska Institutet
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- Aleksis, Rihards (författare)
- Latvian Inst Organ Synth, Dept Phys Organ Chem, Riga, Latvia.
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- Purhonen, Pasi (författare)
- Karolinska Institutet,KTH,Skolan för kemi, bioteknologi och hälsa (CBH),Karolinska Inst, Dept Biosci & Nutr, Huddinge, Sweden
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- Hebert, Hans (författare)
- KTH,Skolan för kemi, bioteknologi och hälsa (CBH),Karolinska Inst, Dept Biosci & Nutr, Huddinge, Sweden
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- Jaudzems, Kristaps (författare)
- Latvian Inst Organ Synth, Dept Phys Organ Chem, Riga, Latvia.
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- Rising, Anna (författare)
- Swedish University of Agricultural Sciences,Sveriges lantbruksuniversitet,Karolinska Institutet,Institutionen för anatomi, fysiologi och biokemi,Department of Anatomy, Physiology and Biochemistry (AFB),Karolinska Institute
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- Johansson, Jan (författare)
- Karolinska Institutet,Karolinska Institute
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Karolinska Institutet Latvian Inst Organ Synth, Dept Phys Organ Chem, Riga, Latvia (creator_code:org_t)
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- 2018-04-14
- 2018
- Engelska.
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Ingår i: The FEBS Journal. - : WILEY. - 1742-464X .- 1742-4658. ; 285:10, s. 1873-1885
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https://urn.kb.se/re...
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https://doi.org/10.1...
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Abstract
Ämnesord
Stäng
- 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.
Ämnesord
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
Nyckelord
- amyloid disease
- fibril formation
- model protein
- protein assembly
- protein domain
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
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