Dodecylphosphocholine Micelles Induce Amyloid Formation of the PrP(110-136) Peptide via an α-Helical Metastable Conformation.
A peptide encompassing the conserved hydrophobic region and the first β-strand of the prion protein (PrP(110-136)) shown to interact with the surface of dodecylphosphocholine micelles adopts an α-helical conformation that is localized below the head-group layer. This surface-bound peptide has a half...
| Main Authors: | , |
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2016-01-01
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| Series: | PLoS ONE |
| Online Access: | http://europepmc.org/articles/PMC5145231?pdf=render |
| _version_ | 1818129501461151744 |
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| author | Simon Sauvé Yves Aubin |
| author_facet | Simon Sauvé Yves Aubin |
| author_sort | Simon Sauvé |
| collection | DOAJ |
| description | A peptide encompassing the conserved hydrophobic region and the first β-strand of the prion protein (PrP(110-136)) shown to interact with the surface of dodecylphosphocholine micelles adopts an α-helical conformation that is localized below the head-group layer. This surface-bound peptide has a half-life of one day, and readily initiates the formation of amyloid fibrils. The presence of the latter was confirmed using birefringence microscopy upon Congo red binding and thioflavin T-binding induced fluorescence. The observation of this metastable α-helical conformer provides a unique snapshot of the early steps of the inter-conversion pathway. These findings together with the body of evidence from the prion literature allowed us to propose a mechanism for the conversion of PrPC to amyloid material. |
| first_indexed | 2024-12-11T07:50:09Z |
| format | Article |
| id | doaj.art-0db62a69d12a43e1af7dbbfa01ba1cc5 |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-11T07:50:09Z |
| publishDate | 2016-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-0db62a69d12a43e1af7dbbfa01ba1cc52022-12-22T01:15:22ZengPublic Library of Science (PLoS)PLoS ONE1932-62032016-01-011112e016802110.1371/journal.pone.0168021Dodecylphosphocholine Micelles Induce Amyloid Formation of the PrP(110-136) Peptide via an α-Helical Metastable Conformation.Simon SauvéYves AubinA peptide encompassing the conserved hydrophobic region and the first β-strand of the prion protein (PrP(110-136)) shown to interact with the surface of dodecylphosphocholine micelles adopts an α-helical conformation that is localized below the head-group layer. This surface-bound peptide has a half-life of one day, and readily initiates the formation of amyloid fibrils. The presence of the latter was confirmed using birefringence microscopy upon Congo red binding and thioflavin T-binding induced fluorescence. The observation of this metastable α-helical conformer provides a unique snapshot of the early steps of the inter-conversion pathway. These findings together with the body of evidence from the prion literature allowed us to propose a mechanism for the conversion of PrPC to amyloid material.http://europepmc.org/articles/PMC5145231?pdf=render |
| spellingShingle | Simon Sauvé Yves Aubin Dodecylphosphocholine Micelles Induce Amyloid Formation of the PrP(110-136) Peptide via an α-Helical Metastable Conformation. PLoS ONE |
| title | Dodecylphosphocholine Micelles Induce Amyloid Formation of the PrP(110-136) Peptide via an α-Helical Metastable Conformation. |
| title_full | Dodecylphosphocholine Micelles Induce Amyloid Formation of the PrP(110-136) Peptide via an α-Helical Metastable Conformation. |
| title_fullStr | Dodecylphosphocholine Micelles Induce Amyloid Formation of the PrP(110-136) Peptide via an α-Helical Metastable Conformation. |
| title_full_unstemmed | Dodecylphosphocholine Micelles Induce Amyloid Formation of the PrP(110-136) Peptide via an α-Helical Metastable Conformation. |
| title_short | Dodecylphosphocholine Micelles Induce Amyloid Formation of the PrP(110-136) Peptide via an α-Helical Metastable Conformation. |
| title_sort | dodecylphosphocholine micelles induce amyloid formation of the prp 110 136 peptide via an α helical metastable conformation |
| url | http://europepmc.org/articles/PMC5145231?pdf=render |
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