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Synthetic NAC 71-82...
Synthetic NAC 71-82 Peptides Designed to Produce Fibrils with Different Protofilament Interface Contacts
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- Näsström, Thomas (author)
- Linnéuniversitetet,Institutionen för kemi och biomedicin (KOB),Avancerade material,PPL;Linnaeus Ctr Biomat Chem, BMC,Linnaeus Univ, Ctr Biomat Chem, Phys Pharm Lab, SE-39231 Kalmar, Sweden.
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- Dahlberg, Tobias (author)
- Umeå universitet,Institutionen för fysik,Umeå University, Sweden,The Biophysics and Biophotonics Group,Umeå Univ, Biophys & Biophoton Grp, Dept Phys, SE-90187 Umeå, Sweden.
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- Malyshev, Dmitry (author)
- Umeå universitet,Institutionen för fysik,Umeå University, Sweden,The Biophysics and Biophotonics Group,Umeå Univ, Biophys & Biophoton Grp, Dept Phys, SE-90187 Umeå, Sweden.
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- Ådén, Jörgen, 1980- (author)
- Umeå universitet,Kemiska institutionen,Umeå University, Sweden,Umeå Univ, Dept Chem, SE-90187 Umeå, Sweden.
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- Andersson, Per-Ola (author)
- Uppsala universitet,Tillämpad materialvetenskap
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- Andersson, Magnus (author)
- Umeå universitet,Institutionen för fysik,The Biophysics and Biophotonics group,Umeå University, Sweden,Umeå Univ, Biophys & Biophoton Grp, Dept Phys, SE-90187 Umeå, Sweden.
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- Karlsson, Björn C. G., Docent, 1977- (author)
- Linnéuniversitetet,Institutionen för kemi och biomedicin (KOB),Avancerade material,Linnaeus Ctr Biomat Chem, BMC;PPL,Linnaeus Univ, Ctr Biomat Chem, Phys Pharm Lab, SE-39231 Kalmar, Sweden.
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(creator_code:org_t)
- 2021-08-28
- 2021
- English.
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In: International Journal of Molecular Sciences. - : MDPI. - 1661-6596 .- 1422-0067. ; 22:17
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Abstract
Subject headings
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- Alpha-synucleinopathies are featured by fibrillar inclusions in brain cells. Although α-synuclein fibrils display structural diversity, the origin of this diversity is not fully understood. We used molecular dynamics simulations to design synthetic peptides, based on the NAC 71-82 amino acid fragment of α-synuclein, that govern protofilament contacts and generation of twisted fibrillar polymorphs. Four peptides with structures based on either single or double fragments and capped or non-capped ends were selected for further analysis. We determined the fibrillar yield and the structures from these peptides found in the solution after fibrillisation using protein concentration determination assay and circular dichroism spectroscopy. In addition, we characterised secondary structures formed by individual fibrillar complexes using laser-tweezers Raman spectroscopy. Results suggest less mature fibrils, based on the lower relative β-sheet content for double- than single-fragment peptide fibrils. We confirmed this structural difference by TEM analysis which revealed, in addition to short protofibrils, more elongated, twisted and rod-like fibril structures in non-capped and capped double-fragment peptide systems, respectively. Finally, time-correlated single-photon counting demonstrated a difference in the Thioflavin T fluorescence lifetime profiles upon fibril binding. It could be proposed that this difference originated from morphological differences in the fibril samples. Altogether, these results highlight the potential of using peptide models for the generation of fibrils that share morphological features relevant for disease, e.g., twisted and rod-like polymorphs.
Subject headings
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
- NATURVETENSKAP -- Fysik -- Annan fysik (hsv//swe)
- NATURAL SCIENCES -- Physical Sciences -- Other Physics Topics (hsv//eng)
- NATURVETENSKAP -- Biologi -- Biofysik (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biophysics (hsv//eng)
- NATURVETENSKAP -- Kemi -- Fysikalisk kemi (hsv//swe)
- NATURAL SCIENCES -- Chemical Sciences -- Physical Chemistry (hsv//eng)
Keyword
- α-synuclein
- NAC 71-82 peptides
- fibril polymorphs
- Biokemi
Publication and Content Type
- ref (subject category)
- art (subject category)
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