Non-Esterified Fatty Acids Generate Distinct Low-Molecular Weight Amyloid-β (Aβ42) Oligomers along Pathway Different from Fibril Formation
Identifieur interne : 002445 ( Main/Exploration ); précédent : 002444; suivant : 002446Non-Esterified Fatty Acids Generate Distinct Low-Molecular Weight Amyloid-β (Aβ42) Oligomers along Pathway Different from Fibril Formation
Auteurs : Amit Kumar [États-Unis] ; Rebekah L. Bullard [États-Unis] ; Pritesh Patel [États-Unis] ; Lea C. Paslay [États-Unis] ; Dipti Singh [États-Unis] ; Ewa A. Bienkiewicz [États-Unis] ; Sarah E. Morgan [États-Unis] ; Vijayaraghavan Rangachari [États-Unis]Source :
- PLoS ONE [ 1932-6203 ] ; 2011.
Descripteurs français
- KwdFr :
- Acide gras libre (pharmacologie), Benzothiazoles, Dichroïsme circulaire, Dénaturation des protéines (), Fluorescence, Guanidine (pharmacologie), Masse moléculaire, Micelles, Modèles biologiques, Peptides bêta-amyloïdes (), Peptides bêta-amyloïdes (isolement et purification), Structure quaternaire des protéines, Structure secondaire des protéines, Technique de Western, Thermodynamique, Thiazoles (métabolisme).
- MESH :
- isolement et purification : Peptides bêta-amyloïdes.
- métabolisme : Thiazoles.
- pharmacologie : Acide gras libre, Guanidine.
- Benzothiazoles, Dichroïsme circulaire, Dénaturation des protéines, Fluorescence, Masse moléculaire, Micelles, Modèles biologiques, Peptides bêta-amyloïdes, Structure quaternaire des protéines, Structure secondaire des protéines, Technique de Western, Thermodynamique.
English descriptors
- KwdEn :
- Amyloid beta-Peptides (chemistry), Amyloid beta-Peptides (isolation & purification), Benzothiazoles, Blotting, Western, Circular Dichroism, Fatty Acids, Nonesterified (pharmacology), Fluorescence, Guanidine (pharmacology), Micelles, Models, Biological, Molecular Weight, Protein Denaturation (drug effects), Protein Structure, Quaternary, Protein Structure, Secondary, Thermodynamics, Thiazoles (metabolism).
- MESH :
- chemical , chemistry : Amyloid beta-Peptides.
- chemical , isolation & purification : Amyloid beta-Peptides.
- chemical , metabolism : Thiazoles.
- chemical , pharmacology : Fatty Acids, Nonesterified, Guanidine.
- chemical : Benzothiazoles, Micelles.
- drug effects : Protein Denaturation.
- Blotting, Western, Circular Dichroism, Fluorescence, Models, Biological, Molecular Weight, Protein Structure, Quaternary, Protein Structure, Secondary, Thermodynamics.
Abstract
Amyloid-β (Aβ) peptide aggregation is known to play a central role in the etiology of Alzheimer’s disease (AD). Among various aggregates, low-molecular weight soluble oligomers of Aβ are increasingly believed to be the primary neurotoxic agents responsible for memory impairment. Anionic interfaces are known to influence the Aβ aggregation process significantly. Here, we report the effects of interfaces formed by medium-chain (C9–C12), saturated non-esterified fatty acids (NEFAs) on Aβ42 aggregation. NEFAs uniquely affected Aβ42 aggregation rates that depended on both the ratio of Aβ:NEFA as well the critical micelle concentration (CMC) of the NEFAs. More importantly, irrespective of the kind of NEFA used, we observed that two distinct oligomers, 12–18 mers and 4–5 mers were formed via different pathway of aggregation under specific experimental conditions: (
Url:
DOI: 10.1371/journal.pone.0018759
PubMed: 21526230
PubMed Central: 3079704
Affiliations:
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Le document en format XML
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Bullard</name><affiliation wicri:level="2"><nlm:aff id="aff1"><addr-line>Department of Chemistry and Biochemistry, University of Southern Mississippi, Hattiesburg, Mississippi, United States of America</addr-line></nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Chemistry and Biochemistry, University of Southern Mississippi, Hattiesburg, Mississippi</wicri:regionArea><placeName><region type="state">État du Mississippi</region></placeName></affiliation></author><author><name sortKey="Patel, Pritesh" sort="Patel, Pritesh" uniqKey="Patel P" first="Pritesh" last="Patel">Pritesh Patel</name><affiliation wicri:level="2"><nlm:aff id="aff1"><addr-line>Department of Chemistry and Biochemistry, University of Southern Mississippi, Hattiesburg, Mississippi, United States of America</addr-line></nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Chemistry and Biochemistry, University of Southern Mississippi, Hattiesburg, Mississippi</wicri:regionArea><placeName><region type="state">État du Mississippi</region></placeName></affiliation></author><author><name sortKey="Paslay, Lea C" sort="Paslay, Lea C" uniqKey="Paslay L" first="Lea C." last="Paslay">Lea C. Paslay</name><affiliation wicri:level="2"><nlm:aff id="aff2"><addr-line>School of Polymers and High Performance Materials, University of Southern Mississippi, Hattiesburg, Mississippi, United States of America</addr-line></nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>School of Polymers and High Performance Materials, University of Southern Mississippi, Hattiesburg, Mississippi</wicri:regionArea><placeName><region type="state">État du Mississippi</region></placeName></affiliation></author><author><name sortKey="Singh, Dipti" sort="Singh, Dipti" uniqKey="Singh D" first="Dipti" last="Singh">Dipti Singh</name><affiliation wicri:level="2"><nlm:aff id="aff2"><addr-line>School of Polymers and High Performance Materials, University of Southern Mississippi, Hattiesburg, Mississippi, United States of America</addr-line></nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>School of Polymers and High Performance Materials, University of Southern Mississippi, Hattiesburg, Mississippi</wicri:regionArea><placeName><region type="state">État du Mississippi</region></placeName></affiliation></author><author><name sortKey="Bienkiewicz, Ewa A" sort="Bienkiewicz, Ewa A" uniqKey="Bienkiewicz E" first="Ewa A." last="Bienkiewicz">Ewa A. Bienkiewicz</name><affiliation wicri:level="2"><nlm:aff id="aff3"><addr-line>Department of Biomedical Sciences, College of Medicine, Florida State University, Tallahassee, Florida, United States of America</addr-line></nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biomedical Sciences, College of Medicine, Florida State University, Tallahassee, Florida</wicri:regionArea><placeName><region type="state">Floride</region></placeName></affiliation></author><author><name sortKey="Morgan, Sarah E" sort="Morgan, Sarah E" uniqKey="Morgan S" first="Sarah E." last="Morgan">Sarah E. Morgan</name><affiliation wicri:level="2"><nlm:aff id="aff2"><addr-line>School of Polymers and High Performance Materials, University of Southern Mississippi, Hattiesburg, Mississippi, United States of America</addr-line></nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>School of Polymers and High Performance Materials, University of Southern Mississippi, Hattiesburg, Mississippi</wicri:regionArea><placeName><region type="state">État du Mississippi</region></placeName></affiliation></author><author><name sortKey="Rangachari, Vijayaraghavan" sort="Rangachari, Vijayaraghavan" uniqKey="Rangachari V" first="Vijayaraghavan" last="Rangachari">Vijayaraghavan Rangachari</name><affiliation wicri:level="2"><nlm:aff id="aff1"><addr-line>Department of Chemistry and Biochemistry, University of Southern Mississippi, Hattiesburg, Mississippi, United States of America</addr-line></nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Chemistry and Biochemistry, University of Southern Mississippi, Hattiesburg, Mississippi</wicri:regionArea><placeName><region type="state">État du Mississippi</region></placeName></affiliation></author></analytic><series><title level="j">PLoS ONE</title><idno type="eISSN">1932-6203</idno><imprint><date when="2011">2011</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amyloid beta-Peptides (chemistry)</term><term>Amyloid beta-Peptides (isolation & purification)</term><term>Benzothiazoles</term><term>Blotting, Western</term><term>Circular Dichroism</term><term>Fatty Acids, Nonesterified (pharmacology)</term><term>Fluorescence</term><term>Guanidine (pharmacology)</term><term>Micelles</term><term>Models, Biological</term><term>Molecular Weight</term><term>Protein Denaturation (drug effects)</term><term>Protein Structure, Quaternary</term><term>Protein Structure, Secondary</term><term>Thermodynamics</term><term>Thiazoles (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Acide gras libre (pharmacologie)</term><term>Benzothiazoles</term><term>Dichroïsme circulaire</term><term>Dénaturation des protéines ()</term><term>Fluorescence</term><term>Guanidine (pharmacologie)</term><term>Masse moléculaire</term><term>Micelles</term><term>Modèles biologiques</term><term>Peptides bêta-amyloïdes ()</term><term>Peptides bêta-amyloïdes (isolement et purification)</term><term>Structure quaternaire des protéines</term><term>Structure secondaire des protéines</term><term>Technique de Western</term><term>Thermodynamique</term><term>Thiazoles (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Amyloid beta-Peptides</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Amyloid beta-Peptides</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Thiazoles</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Fatty Acids, Nonesterified</term><term>Guanidine</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Benzothiazoles</term><term>Micelles</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Protein Denaturation</term></keywords><keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Peptides bêta-amyloïdes</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Thiazoles</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Acide gras libre</term><term>Guanidine</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Blotting, Western</term><term>Circular Dichroism</term><term>Fluorescence</term><term>Models, Biological</term><term>Molecular Weight</term><term>Protein Structure, Quaternary</term><term>Protein Structure, Secondary</term><term>Thermodynamics</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Benzothiazoles</term><term>Dichroïsme circulaire</term><term>Dénaturation des protéines</term><term>Fluorescence</term><term>Masse moléculaire</term><term>Micelles</term><term>Modèles biologiques</term><term>Peptides bêta-amyloïdes</term><term>Structure quaternaire des protéines</term><term>Structure secondaire des protéines</term><term>Technique de Western</term><term>Thermodynamique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>Amyloid-β (Aβ) peptide aggregation is known to play a central role in the etiology of Alzheimer’s disease (AD). Among various aggregates, low-molecular weight soluble oligomers of Aβ are increasingly believed to be the primary neurotoxic agents responsible for memory impairment. Anionic interfaces are known to influence the Aβ aggregation process significantly. Here, we report the effects of interfaces formed by medium-chain (C9–C12), saturated non-esterified fatty acids (NEFAs) on Aβ42 aggregation. NEFAs uniquely affected Aβ42 aggregation rates that depended on both the ratio of Aβ:NEFA as well the critical micelle concentration (CMC) of the NEFAs. More importantly, irrespective of the kind of NEFA used, we observed that two distinct oligomers, 12–18 mers and 4–5 mers were formed via different pathway of aggregation under specific experimental conditions: (<italic>i</italic>) 12–18 mers were generated near the CMC in which NEFAs augment the rate of Aβ42 aggregation towards fibril formation, and, (<italic>ii</italic>) 4–5 mers were formed above the CMC, where NEFAs inhibit fibril formation. The data indicated that both 12–18 mers and 4–5 mers are formed along an alternate pathway called ‘off-pathway’ that did not result in fibril formation and yet have subtle structural and morphological differences that distinguish their bulk molecular behavior. These observations, (<italic>i</italic>) reflect the possible mechanism of Aβ aggregation in physiological lipid-rich environments, and (ii) reiterate the fact that all oligomeric forms of Aβ need not be obligatory intermediates of the fibril formation pathway.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Hardy, Ja" uniqKey="Hardy J">JA Hardy</name></author><author><name sortKey="Higgins, Ga" uniqKey="Higgins G">GA Higgins</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Terry, Rd" uniqKey="Terry R">RD Terry</name></author><author><name sortKey="Masliah, E" uniqKey="Masliah E">E Masliah</name></author><author><name sortKey="Salmon, Dp" uniqKey="Salmon D">DP Salmon</name></author><author><name sortKey="Butters, N" uniqKey="Butters N">N Butters</name></author><author><name sortKey="Deteresa, R" uniqKey="Deteresa R">R 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Bailey</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Wang, F" uniqKey="Wang F">F Wang</name></author><author><name sortKey="Yang, F" uniqKey="Yang F">F Yang</name></author><author><name sortKey="Hu, Y" uniqKey="Hu Y">Y Hu</name></author><author><name sortKey="Wang, X" uniqKey="Wang X">X Wang</name></author><author><name sortKey="Jin, C" uniqKey="Jin C">C Jin</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Wang, F" uniqKey="Wang F">F Wang</name></author><author><name sortKey="Wang, X" uniqKey="Wang X">X Wang</name></author><author><name sortKey="Yuan, Cg" uniqKey="Yuan C">CG Yuan</name></author><author><name sortKey="Ma, J" uniqKey="Ma J">J Ma</name></author></analytic></biblStruct></listBibl></div1></back></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>Floride</li><li>État du Mississippi</li></region></list><tree><country name="États-Unis"><region name="État du Mississippi"><name sortKey="Kumar, Amit" sort="Kumar, Amit" uniqKey="Kumar A" first="Amit" last="Kumar">Amit Kumar</name></region><name sortKey="Bienkiewicz, Ewa A" sort="Bienkiewicz, Ewa A" uniqKey="Bienkiewicz E" first="Ewa A." last="Bienkiewicz">Ewa A. Bienkiewicz</name><name sortKey="Bullard, Rebekah L" sort="Bullard, Rebekah L" uniqKey="Bullard R" first="Rebekah L." last="Bullard">Rebekah L. Bullard</name><name sortKey="Morgan, Sarah E" sort="Morgan, Sarah E" uniqKey="Morgan S" first="Sarah E." last="Morgan">Sarah E. Morgan</name><name sortKey="Paslay, Lea C" sort="Paslay, Lea C" uniqKey="Paslay L" first="Lea C." last="Paslay">Lea C. Paslay</name><name sortKey="Patel, Pritesh" sort="Patel, Pritesh" uniqKey="Patel P" first="Pritesh" last="Patel">Pritesh Patel</name><name sortKey="Rangachari, Vijayaraghavan" sort="Rangachari, Vijayaraghavan" uniqKey="Rangachari V" first="Vijayaraghavan" last="Rangachari">Vijayaraghavan Rangachari</name><name sortKey="Singh, Dipti" sort="Singh, Dipti" uniqKey="Singh D" first="Dipti" last="Singh">Dipti Singh</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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