CovidV1, Main, Exploration, bibRecord, 000917

Self-Assembly of a 9-Residue Amyloid-Forming Peptide Fragment of SARS Corona Virus E-protein: Mechanism of Self Aggregation and Amyloid-Inhibition of hIAPP

Identifieur interne : 000917 ( Main/Exploration ); précédent : 000916; suivant : 000918

Self-Assembly of a 9-Residue Amyloid-Forming Peptide Fragment of SARS Corona Virus E-protein: Mechanism of Self Aggregation and Amyloid-Inhibition of hIAPP

Auteurs : Anirban Ghosh [Inde] ; Amit S. Pithadia [États-Unis] ; Jyotsna Bhat [Inde] ; Supriyo Bera [Inde] ; Anupam Midya [Inde] ; Carol A. Fierke [États-Unis] ; Ayyalusamy Ramamoorthy [États-Unis] ; Anirban Bhunia [Inde, États-Unis]

Source :

Biochemistry [ 0006-2960 ] ; 2015.

RBID : PMC:4903029

Descripteurs français

English descriptors

KwdEn :
- Amyloid (chemistry), Amyloid (metabolism), Circular Dichroism, Humans, Hydrophobic and Hydrophilic Interactions, Islet Amyloid Polypeptide (antagonists & inhibitors), Islet Amyloid Polypeptide (metabolism), Molecular Dynamics Simulation, Nuclear Magnetic Resonance, Biomolecular, Peptide Fragments (chemistry), Peptide Fragments (metabolism), Peptide Fragments (pharmacology), Protein Folding, Protein Structure, Secondary, Spectrometry, Fluorescence, Viral Envelope Proteins (chemistry), Viral Envelope Proteins (metabolism).
MESH :
- chemical , antagonists & inhibitors : Islet Amyloid Polypeptide.
- chemical , chemistry : Amyloid, Peptide Fragments, Viral Envelope Proteins.
- chemical , metabolism : Amyloid, Islet Amyloid Polypeptide, Peptide Fragments, Viral Envelope Proteins.
- chemical , pharmacology : Peptide Fragments.
- Circular Dichroism, Humans, Hydrophobic and Hydrophilic Interactions, Molecular Dynamics Simulation, Nuclear Magnetic Resonance, Biomolecular, Protein Folding, Protein Structure, Secondary, Spectrometry, Fluorescence.

Abstract

Molecular self-assembly, a phenomenon widely observed in nature, has been exploited through organic molecules, proteins, DNA and peptides to study complex biological systems. These self-assembly systems may also be used in understanding the molecular and structural biology which can inspire the design and synthesis of increasingly complex biomaterials. Specifically, use of these building blocks to investigate protein folding and misfolding has been of particular value since it can provide tremendous insights into peptide aggregation related to a variety of protein misfolding diseases, or amyloid diseases (e.g. Alzheimer’s disease, Parkinson’s disease, type-II diabetes). Herein, the self-assembly of TK9, a 9 residue peptide of the extra membrane C-terminal tail of the SARS Corona virus envelope, and its variants were characterized through biophysical, spectroscopic and simulated studies, and it was confirmed that the structure of these peptides influence their aggregation propensity, hence, mimicking amyloid proteins. TK9, which forms a beta-sheet rich fibril, contains a key sequence motif that may be critical for beta-sheet formation, thus making it an interesting system to study amyloid fibrillation. TK9 aggregates were further examined through simulations to evaluate the possible intra- and inter peptide interactions at the molecular level. These self-assembly peptides can also serve as amyloid inhibitors through hydrophobic and electrophilic recognition interactions. Our results show that TK9 inhibits the fibrillation of hIAPP, a 37 amino acid peptide implicated in the pathology of type-II diabetes. Thus, biophysical and NMR experimental results have revealed a molecular level understanding of peptide folding events, as well as the inhibition of amyloid-protein aggregation are reported.

Url:

http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4903029

DOI: 10.1021/acs.biochem.5b00061
PubMed: 25785896
PubMed Central: 4903029

Affiliations:

Inde, États-Unis

Le document en format XML

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: Mechanism of Self Aggregation and Amyloid-Inhibition of hIAPP</title>
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<term>Islet Amyloid Polypeptide (metabolism)</term>
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<term>Peptide Fragments (metabolism)</term>
<term>Peptide Fragments (pharmacology)</term>
<term>Protein Folding</term>
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<term>Spectrometry, Fluorescence</term>
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<term>Viral Envelope Proteins (metabolism)</term>
</keywords>
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<term>Amyloïde (métabolisme)</term>
<term>Dichroïsme circulaire</term>
<term>Fragments peptidiques ()</term>
<term>Fragments peptidiques (métabolisme)</term>
<term>Fragments peptidiques (pharmacologie)</term>
<term>Humains</term>
<term>Interactions hydrophobes et hydrophiles</term>
<term>Pliage des protéines</term>
<term>Polypeptide amyloïde des ilots (antagonistes et inhibiteurs)</term>
<term>Polypeptide amyloïde des ilots (métabolisme)</term>
<term>Protéines de l'enveloppe virale ()</term>
<term>Protéines de l'enveloppe virale (métabolisme)</term>
<term>Résonance magnétique nucléaire biomoléculaire</term>
<term>Simulation de dynamique moléculaire</term>
<term>Spectrométrie de fluorescence</term>
<term>Structure secondaire des protéines</term>
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<term>Islet Amyloid Polypeptide</term>
<term>Peptide Fragments</term>
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</keywords>
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</keywords>
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<term>Protéines de l'enveloppe virale</term>
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</keywords>
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<term>Molecular Dynamics Simulation</term>
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<term>Protein Structure, Secondary</term>
<term>Spectrometry, Fluorescence</term>
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<term>Dichroïsme circulaire</term>
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<term>Humains</term>
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<front><div type="abstract" xml:lang="en"><p id="P1">Molecular self-assembly, a phenomenon widely observed in nature, has been exploited through organic molecules, proteins, DNA and peptides to study complex biological systems. These self-assembly systems may also be used in understanding the molecular and structural biology which can inspire the design and synthesis of increasingly complex biomaterials. Specifically, use of these building blocks to investigate protein folding and misfolding has been of particular value since it can provide tremendous insights into peptide aggregation related to a variety of protein misfolding diseases, or amyloid diseases (e.g. Alzheimer’s disease, Parkinson’s disease, type-II diabetes). Herein, the self-assembly of <bold>TK9</bold>
, a 9 residue peptide of the extra membrane C-terminal tail of the SARS Corona virus envelope, and its variants were characterized through biophysical, spectroscopic and simulated studies, and it was confirmed that the structure of these peptides influence their aggregation propensity, hence, mimicking amyloid proteins. <bold>TK9</bold>
, which forms a beta-sheet rich fibril, contains a key sequence motif that may be critical for beta-sheet formation, thus making it an interesting system to study amyloid fibrillation. <bold>TK9</bold>
 aggregates were further examined through simulations to evaluate the possible intra- and inter peptide interactions at the molecular level. These self-assembly peptides can also serve as amyloid inhibitors through hydrophobic and electrophilic recognition interactions. Our results show that <bold>TK9</bold>
 inhibits the fibrillation of hIAPP, a 37 amino acid peptide implicated in the pathology of type-II diabetes. Thus, biophysical and NMR experimental results have revealed a molecular level understanding of peptide folding events, as well as the inhibition of amyloid-protein aggregation are reported.</p>
</div>
</front>
</TEI>
<affiliations><list><country><li>Inde</li>
<li>États-Unis</li>
</country>
</list>
<tree><country name="Inde"><noRegion><name sortKey="Ghosh, Anirban" sort="Ghosh, Anirban" uniqKey="Ghosh A" first="Anirban" last="Ghosh">Anirban Ghosh</name>
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<name sortKey="Bhat, Jyotsna" sort="Bhat, Jyotsna" uniqKey="Bhat J" first="Jyotsna" last="Bhat">Jyotsna Bhat</name>
<name sortKey="Bhunia, Anirban" sort="Bhunia, Anirban" uniqKey="Bhunia A" first="Anirban" last="Bhunia">Anirban Bhunia</name>
<name sortKey="Midya, Anupam" sort="Midya, Anupam" uniqKey="Midya A" first="Anupam" last="Midya">Anupam Midya</name>
</country>
<country name="États-Unis"><noRegion><name sortKey="Pithadia, Amit S" sort="Pithadia, Amit S" uniqKey="Pithadia A" first="Amit S." last="Pithadia">Amit S. Pithadia</name>
</noRegion>
<name sortKey="Bhunia, Anirban" sort="Bhunia, Anirban" uniqKey="Bhunia A" first="Anirban" last="Bhunia">Anirban Bhunia</name>
<name sortKey="Bhunia, Anirban" sort="Bhunia, Anirban" uniqKey="Bhunia A" first="Anirban" last="Bhunia">Anirban Bhunia</name>
<name sortKey="Fierke, Carol A" sort="Fierke, Carol A" uniqKey="Fierke C" first="Carol A." last="Fierke">Carol A. Fierke</name>
<name sortKey="Fierke, Carol A" sort="Fierke, Carol A" uniqKey="Fierke C" first="Carol A." last="Fierke">Carol A. Fierke</name>
<name sortKey="Fierke, Carol A" sort="Fierke, Carol A" uniqKey="Fierke C" first="Carol A." last="Fierke">Carol A. Fierke</name>
<name sortKey="Ramamoorthy, Ayyalusamy" sort="Ramamoorthy, Ayyalusamy" uniqKey="Ramamoorthy A" first="Ayyalusamy" last="Ramamoorthy">Ayyalusamy Ramamoorthy</name>
<name sortKey="Ramamoorthy, Ayyalusamy" sort="Ramamoorthy, Ayyalusamy" uniqKey="Ramamoorthy A" first="Ayyalusamy" last="Ramamoorthy">Ayyalusamy Ramamoorthy</name>
</country>
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</affiliations>
</record>

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Self-Assembly of a 9-Residue Amyloid-Forming Peptide Fragment of SARS Corona Virus E-protein: Mechanism of Self Aggregation and Amyloid-Inhibition of hIAPP

Self-Assembly of a 9-Residue Amyloid-Forming Peptide Fragment of SARS Corona Virus E-protein: Mechanism of Self Aggregation and Amyloid-Inhibition of hIAPP

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