A folding transition underlies the emergence of membrane affinity in amyloid-β.
Identifieur interne : 002091 ( Main/Merge ); précédent : 002090; suivant : 002092A folding transition underlies the emergence of membrane affinity in amyloid-β.
Auteurs : Suman Nag [Inde] ; Bidyut Sarkar ; Muralidharan Chandrakesan ; Rajiv Abhyanakar ; Debanjan Bhowmik ; Mamata Kombrabail ; Sucheta Dandekar ; Eitan Lerner ; Elisha Haas ; Sudipta MaitiSource :
- Physical chemistry chemical physics : PCCP [ 1463-9084 ] ; 2013.
Descripteurs français
- KwdFr :
- Fluorescéine (), Fragments peptidiques (), Fragments peptidiques (métabolisme), Fragments peptidiques (synthèse chimique), Peptides bêta-amyloïdes (), Peptides bêta-amyloïdes (métabolisme), Peptides bêta-amyloïdes (synthèse chimique), Phosphatidylcholines (), Pliage des protéines, Structure secondaire des protéines, Transfert d'énergie par résonance de fluorescence.
- MESH :
- métabolisme : Fragments peptidiques, Peptides bêta-amyloïdes.
- synthèse chimique : Fragments peptidiques, Peptides bêta-amyloïdes.
- Fluorescéine, Fragments peptidiques, Peptides bêta-amyloïdes, Phosphatidylcholines, Pliage des protéines, Structure secondaire des protéines, Transfert d'énergie par résonance de fluorescence.
English descriptors
- KwdEn :
- Amyloid beta-Peptides (chemical synthesis), Amyloid beta-Peptides (chemistry), Amyloid beta-Peptides (metabolism), Fluorescein (chemistry), Fluorescence Resonance Energy Transfer, Peptide Fragments (chemical synthesis), Peptide Fragments (chemistry), Peptide Fragments (metabolism), Phosphatidylcholines (chemistry), Protein Folding, Protein Structure, Secondary.
- MESH :
- chemical , chemical synthesis : Amyloid beta-Peptides, Peptide Fragments.
- chemical , chemistry : Amyloid beta-Peptides, Fluorescein, Peptide Fragments, Phosphatidylcholines.
- chemical , metabolism : Amyloid beta-Peptides, Peptide Fragments.
- Fluorescence Resonance Energy Transfer, Protein Folding, Protein Structure, Secondary.
Abstract
Small amyloid-β (Aβ) oligomers have much higher membrane affinity compared to the monomers, but the structural origin of this functional change is not understood. We show that as monomers assemble into small n-mers (n < 10), Aβ acquires a tertiary fold that is consistent with the mature fibrils. This is an early and defining transition for the aggregating peptide, and possibly underpins its altered bioactivity.
DOI: 10.1039/c3cp52732h
PubMed: 24121316
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pubmed:24121316Le document en format XML
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<term>Amyloid beta-Peptides (metabolism)</term>
<term>Fluorescein (chemistry)</term>
<term>Fluorescence Resonance Energy Transfer</term>
<term>Peptide Fragments (chemical synthesis)</term>
<term>Peptide Fragments (chemistry)</term>
<term>Peptide Fragments (metabolism)</term>
<term>Phosphatidylcholines (chemistry)</term>
<term>Protein Folding</term>
<term>Protein Structure, Secondary</term>
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<term>Fragments peptidiques ()</term>
<term>Fragments peptidiques (métabolisme)</term>
<term>Fragments peptidiques (synthèse chimique)</term>
<term>Peptides bêta-amyloïdes ()</term>
<term>Peptides bêta-amyloïdes (métabolisme)</term>
<term>Peptides bêta-amyloïdes (synthèse chimique)</term>
<term>Phosphatidylcholines ()</term>
<term>Pliage des protéines</term>
<term>Structure secondaire des protéines</term>
<term>Transfert d'énergie par résonance de fluorescence</term>
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<keywords scheme="MESH" type="chemical" qualifier="chemical synthesis" xml:lang="en"><term>Amyloid beta-Peptides</term>
<term>Peptide Fragments</term>
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<term>Fluorescein</term>
<term>Peptide Fragments</term>
<term>Phosphatidylcholines</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Amyloid beta-Peptides</term>
<term>Peptide Fragments</term>
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<term>Peptides bêta-amyloïdes</term>
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<term>Peptides bêta-amyloïdes</term>
<term>Phosphatidylcholines</term>
<term>Pliage des protéines</term>
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<front><div type="abstract" xml:lang="en">Small amyloid-β (Aβ) oligomers have much higher membrane affinity compared to the monomers, but the structural origin of this functional change is not understood. We show that as monomers assemble into small n-mers (n < 10), Aβ acquires a tertiary fold that is consistent with the mature fibrils. This is an early and defining transition for the aggregating peptide, and possibly underpins its altered bioactivity. </div>
</front>
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