A folding transition underlies the emergence of membrane affinity in amyloid-β.
Identifieur interne : 002067 ( Main/Exploration ); précédent : 002066; suivant : 002068A 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
Affiliations:
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Le document en format XML
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uniqKey="Chandrakesan M" first="Muralidharan" last="Chandrakesan">Muralidharan Chandrakesan</name></author><author><name sortKey="Abhyanakar, Rajiv" sort="Abhyanakar, Rajiv" uniqKey="Abhyanakar R" first="Rajiv" last="Abhyanakar">Rajiv Abhyanakar</name></author><author><name sortKey="Bhowmik, Debanjan" sort="Bhowmik, Debanjan" uniqKey="Bhowmik D" first="Debanjan" last="Bhowmik">Debanjan Bhowmik</name></author><author><name sortKey="Kombrabail, Mamata" sort="Kombrabail, Mamata" uniqKey="Kombrabail M" first="Mamata" last="Kombrabail">Mamata Kombrabail</name></author><author><name sortKey="Dandekar, Sucheta" sort="Dandekar, Sucheta" uniqKey="Dandekar S" first="Sucheta" last="Dandekar">Sucheta Dandekar</name></author><author><name sortKey="Lerner, Eitan" sort="Lerner, Eitan" uniqKey="Lerner E" first="Eitan" last="Lerner">Eitan Lerner</name></author><author><name sortKey="Haas, Elisha" sort="Haas, Elisha" uniqKey="Haas E" first="Elisha" last="Haas">Elisha Haas</name></author><author><name sortKey="Maiti, Sudipta" sort="Maiti, Sudipta" uniqKey="Maiti S" first="Sudipta" last="Maiti">Sudipta Maiti</name></author></analytic><series><title level="j">Physical chemistry chemical physics : PCCP</title><idno type="eISSN">1463-9084</idno><imprint><date when="2013" type="published">2013</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amyloid beta-Peptides (chemical synthesis)</term><term>Amyloid beta-Peptides (chemistry)</term><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></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Fluorescéine ()</term><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></keywords><keywords scheme="MESH" type="chemical" qualifier="chemical synthesis" xml:lang="en"><term>Amyloid beta-Peptides</term><term>Peptide Fragments</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Amyloid beta-Peptides</term><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></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Fragments peptidiques</term><term>Peptides bêta-amyloïdes</term></keywords><keywords scheme="MESH" qualifier="synthèse chimique" xml:lang="fr"><term>Fragments peptidiques</term><term>Peptides bêta-amyloïdes</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Fluorescence Resonance Energy Transfer</term><term>Protein Folding</term><term>Protein Structure, Secondary</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Fluorescéine</term><term>Fragments peptidiques</term><term>Peptides bêta-amyloïdes</term><term>Phosphatidylcholines</term><term>Pliage des protéines</term><term>Structure secondaire des protéines</term><term>Transfert d'énergie par résonance de fluorescence</term></keywords></textClass></profileDesc></teiHeader><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></TEI><affiliations><list><country><li>Inde</li></country></list><tree><noCountry><name sortKey="Abhyanakar, Rajiv" sort="Abhyanakar, Rajiv" uniqKey="Abhyanakar R" first="Rajiv" last="Abhyanakar">Rajiv Abhyanakar</name><name sortKey="Bhowmik, Debanjan" sort="Bhowmik, Debanjan" uniqKey="Bhowmik D" first="Debanjan" last="Bhowmik">Debanjan Bhowmik</name><name sortKey="Chandrakesan, Muralidharan" sort="Chandrakesan, Muralidharan" uniqKey="Chandrakesan M" first="Muralidharan" last="Chandrakesan">Muralidharan Chandrakesan</name><name sortKey="Dandekar, Sucheta" sort="Dandekar, Sucheta" uniqKey="Dandekar S" first="Sucheta" last="Dandekar">Sucheta Dandekar</name><name sortKey="Haas, Elisha" sort="Haas, Elisha" uniqKey="Haas E" first="Elisha" last="Haas">Elisha Haas</name><name sortKey="Kombrabail, Mamata" sort="Kombrabail, Mamata" uniqKey="Kombrabail M" first="Mamata" last="Kombrabail">Mamata Kombrabail</name><name sortKey="Lerner, Eitan" sort="Lerner, Eitan" uniqKey="Lerner E" first="Eitan" last="Lerner">Eitan Lerner</name><name sortKey="Maiti, Sudipta" sort="Maiti, Sudipta" uniqKey="Maiti S" first="Sudipta" last="Maiti">Sudipta Maiti</name><name sortKey="Sarkar, Bidyut" sort="Sarkar, Bidyut" uniqKey="Sarkar B" first="Bidyut" last="Sarkar">Bidyut Sarkar</name></noCountry><country name="Inde"><noRegion><name sortKey="Nag, Suman" sort="Nag, Suman" uniqKey="Nag S" first="Suman" last="Nag">Suman Nag</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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