Self-assembly of a nine-residue amyloid-forming peptide fragment of SARS corona virus E-protein: mechanism of self aggregation and amyloid-inhibition of hIAPP.
Identifieur interne : 000C95 ( PubMed/Curation ); précédent : 000C94; suivant : 000C96Self-assembly of a nine-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]Source :
- Biochemistry [ 1520-4995 ] ; 2015.
Descripteurs français
- KwdFr :
- Amyloïde (), Amyloïde (métabolisme), Dichroïsme circulaire, Fragments peptidiques (), Fragments peptidiques (métabolisme), Fragments peptidiques (pharmacologie), Humains, Interactions hydrophobes et hydrophiles, Pliage des protéines, Polypeptide amyloïde des ilots (antagonistes et inhibiteurs), Polypeptide amyloïde des ilots (métabolisme), Protéines de l'enveloppe virale (), Protéines de l'enveloppe virale (métabolisme), Résonance magnétique nucléaire biomoléculaire, Simulation de dynamique moléculaire, Spectrométrie de fluorescence, Structure secondaire des protéines.
- MESH :
- antagonistes et inhibiteurs : Polypeptide amyloïde des ilots.
- métabolisme : Amyloïde, Fragments peptidiques, Polypeptide amyloïde des ilots, Protéines de l'enveloppe virale.
- pharmacologie : Fragments peptidiques.
- Amyloïde, Dichroïsme circulaire, Fragments peptidiques, Humains, Interactions hydrophobes et hydrophiles, Pliage des protéines, Protéines de l'enveloppe virale, Résonance magnétique nucléaire biomoléculaire, Simulation de dynamique moléculaire, Spectrométrie de fluorescence, Structure secondaire des protéines.
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 nine-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 influences 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 interpeptide 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.
DOI: 10.1021/acs.biochem.5b00061
PubMed: 25785896
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<term>Humans</term>
<term>Hydrophobic and Hydrophilic Interactions</term>
<term>Islet Amyloid Polypeptide (antagonists & inhibitors)</term>
<term>Islet Amyloid Polypeptide (metabolism)</term>
<term>Molecular Dynamics Simulation</term>
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<term>Peptide Fragments (metabolism)</term>
<term>Peptide Fragments (pharmacology)</term>
<term>Protein Folding</term>
<term>Protein Structure, Secondary</term>
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<front><div type="abstract" xml:lang="en">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 nine-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 influences 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 interpeptide 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. </div>
</front>
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<DateCompleted><Year>2015</Year>
<Month>06</Month>
<Day>30</Day>
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<DateRevised><Year>2019</Year>
<Month>01</Month>
<Day>11</Day>
</DateRevised>
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<JournalIssue CitedMedium="Internet"><Volume>54</Volume>
<Issue>13</Issue>
<PubDate><Year>2015</Year>
<Month>Apr</Month>
<Day>07</Day>
</PubDate>
</JournalIssue>
<Title>Biochemistry</Title>
<ISOAbbreviation>Biochemistry</ISOAbbreviation>
</Journal>
<ArticleTitle>Self-assembly of a nine-residue amyloid-forming peptide fragment of SARS corona virus E-protein: mechanism of self aggregation and amyloid-inhibition of hIAPP.</ArticleTitle>
<Pagination><MedlinePgn>2249-2261</MedlinePgn>
</Pagination>
<ELocationID EIdType="doi" ValidYN="Y">10.1021/acs.biochem.5b00061</ELocationID>
<Abstract><AbstractText>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 nine-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 influences 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 interpeptide 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. </AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y" EqualContrib="Y"><LastName>Ghosh</LastName>
<ForeName>Anirban</ForeName>
<Initials>A</Initials>
<AffiliationInfo><Affiliation>Department of Biophysics, Bose Institute, P-1/12 CIT Scheme VII (M), Kolkata 700 054, India.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y" EqualContrib="Y"><LastName>Pithadia</LastName>
<ForeName>Amit S</ForeName>
<Initials>AS</Initials>
<AffiliationInfo><Affiliation>Department of Chemistry, University of Michigan, 930 N. University Avenue, Ann Arbor, MI 48109-1055, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Bhat</LastName>
<ForeName>Jyotsna</ForeName>
<Initials>J</Initials>
<AffiliationInfo><Affiliation>Department of Biophysics, Bose Institute, P-1/12 CIT Scheme VII (M), Kolkata 700 054, India.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Bera</LastName>
<ForeName>Supriyo</ForeName>
<Initials>S</Initials>
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</AffiliationInfo>
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<ForeName>Anupam</ForeName>
<Initials>A</Initials>
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</AffiliationInfo>
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<ForeName>Carol A</ForeName>
<Initials>CA</Initials>
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</AffiliationInfo>
<AffiliationInfo><Affiliation>Biophysics, University of Michigan, 930 N. University Avenue, Ann Arbor, MI 48109-1055, USA.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Department of Biological Chemistry, University of Michigan, Ann Arbor, MI 48109, USA.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Ramamoorthy</LastName>
<ForeName>Ayyalusamy</ForeName>
<Initials>A</Initials>
<AffiliationInfo><Affiliation>Department of Chemistry, University of Michigan, 930 N. University Avenue, Ann Arbor, MI 48109-1055, USA.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Biophysics, University of Michigan, 930 N. University Avenue, Ann Arbor, MI 48109-1055, USA.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Bhunia</LastName>
<ForeName>Anirban</ForeName>
<Initials>A</Initials>
<AffiliationInfo><Affiliation>Department of Biophysics, Bose Institute, P-1/12 CIT Scheme VII (M), Kolkata 700 054, India.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Department of Chemistry, University of Michigan, 930 N. University Avenue, Ann Arbor, MI 48109-1055, USA.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Biophysics, University of Michigan, 930 N. University Avenue, Ann Arbor, MI 48109-1055, USA.</Affiliation>
</AffiliationInfo>
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<Language>eng</Language>
<GrantList CompleteYN="Y"><Grant><GrantID>R01 GM040602</GrantID>
<Acronym>GM</Acronym>
<Agency>NIGMS NIH HHS</Agency>
<Country>United States</Country>
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