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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Self-Assembly of a 9-Residue Amyloid-Forming Peptide Fragment of <italic>SARS Corona Virus E-protein</italic>: Mechanism of Self Aggregation and Amyloid-Inhibition of hIAPP</title><author><name sortKey="Ghosh, Anirban" sort="Ghosh, Anirban" uniqKey="Ghosh A" first="Anirban" last="Ghosh">Anirban Ghosh</name><affiliation><nlm:aff id="A1">Department of Biophysics, Bose Institute, P-1/12 CIT Scheme VII (M), Kolkata 700 054, India</nlm:aff></affiliation></author><author><name sortKey="Pithadia, Amit S" sort="Pithadia, Amit S" uniqKey="Pithadia A" first="Amit S." last="Pithadia">Amit S. Pithadia</name><affiliation><nlm:aff id="A2">Department of Chemistry, University of Michigan, 930 N. University Avenue, Ann Arbor, MI 48109-1055, USA</nlm:aff></affiliation></author><author><name sortKey="Bhat, Jyotsna" sort="Bhat, Jyotsna" uniqKey="Bhat J" first="Jyotsna" last="Bhat">Jyotsna Bhat</name><affiliation><nlm:aff id="A1">Department of Biophysics, Bose Institute, P-1/12 CIT Scheme VII (M), Kolkata 700 054, India</nlm:aff></affiliation></author><author><name sortKey="Bera, Supriyo" sort="Bera, Supriyo" uniqKey="Bera S" first="Supriyo" last="Bera">Supriyo Bera</name><affiliation><nlm:aff id="A1">Department of Biophysics, Bose Institute, P-1/12 CIT Scheme VII (M), Kolkata 700 054, India</nlm:aff></affiliation></author><author><name sortKey="Midya, Anupam" sort="Midya, Anupam" uniqKey="Midya A" first="Anupam" last="Midya">Anupam Midya</name><affiliation><nlm:aff id="A3">School of Nanoscience and Technology, Indian Institute of Technology Kharagpur, Kharagpur 721302, India</nlm:aff></affiliation></author><author><name sortKey="Fierke, Carol A" sort="Fierke, Carol A" uniqKey="Fierke C" first="Carol A." last="Fierke">Carol A. Fierke</name><affiliation><nlm:aff id="A2">Department of Chemistry, University of Michigan, 930 N. University Avenue, Ann Arbor, MI 48109-1055, USA</nlm:aff></affiliation><affiliation><nlm:aff id="A4">Biophysics, University of Michigan, 930 N. University Avenue, Ann Arbor, MI 48109-1055, USA</nlm:aff></affiliation><affiliation><nlm:aff id="A5">Department of Biological Chemistry, University of Michigan, Ann Arbor, MI 48109, USA</nlm:aff></affiliation></author><author><name sortKey="Ramamoorthy, Ayyalusamy" sort="Ramamoorthy, Ayyalusamy" uniqKey="Ramamoorthy A" first="Ayyalusamy" last="Ramamoorthy">Ayyalusamy Ramamoorthy</name><affiliation><nlm:aff id="A2">Department of Chemistry, University of Michigan, 930 N. University Avenue, Ann Arbor, MI 48109-1055, USA</nlm:aff></affiliation><affiliation><nlm:aff id="A4">Biophysics, University of Michigan, 930 N. University Avenue, Ann Arbor, MI 48109-1055, USA</nlm:aff></affiliation></author><author><name sortKey="Bhunia, Anirban" sort="Bhunia, Anirban" uniqKey="Bhunia A" first="Anirban" last="Bhunia">Anirban Bhunia</name><affiliation><nlm:aff id="A1">Department of Biophysics, Bose Institute, P-1/12 CIT Scheme VII (M), Kolkata 700 054, India</nlm:aff></affiliation><affiliation><nlm:aff id="A2">Department of Chemistry, University of Michigan, 930 N. University Avenue, Ann Arbor, MI 48109-1055, USA</nlm:aff></affiliation><affiliation><nlm:aff id="A4">Biophysics, University of Michigan, 930 N. University Avenue, Ann Arbor, MI 48109-1055, USA</nlm:aff></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">25785896</idno><idno type="pmc">4903029</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4903029</idno><idno type="RBID">PMC:4903029</idno><idno type="doi">10.1021/acs.biochem.5b00061</idno><date when="2015">2015</date><idno type="wicri:Area/Pmc/Corpus">000491</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000491</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Self-Assembly of a 9-Residue Amyloid-Forming Peptide Fragment of <italic>SARS Corona Virus E-protein</italic>: Mechanism of Self Aggregation and Amyloid-Inhibition of hIAPP</title><author><name sortKey="Ghosh, Anirban" sort="Ghosh, Anirban" uniqKey="Ghosh A" first="Anirban" last="Ghosh">Anirban Ghosh</name><affiliation><nlm:aff id="A1">Department of Biophysics, Bose Institute, P-1/12 CIT Scheme VII (M), Kolkata 700 054, India</nlm:aff></affiliation></author><author><name sortKey="Pithadia, Amit S" sort="Pithadia, Amit S" uniqKey="Pithadia A" first="Amit S." last="Pithadia">Amit S. Pithadia</name><affiliation><nlm:aff id="A2">Department of Chemistry, University of Michigan, 930 N. University Avenue, Ann Arbor, MI 48109-1055, USA</nlm:aff></affiliation></author><author><name sortKey="Bhat, Jyotsna" sort="Bhat, Jyotsna" uniqKey="Bhat J" first="Jyotsna" last="Bhat">Jyotsna Bhat</name><affiliation><nlm:aff id="A1">Department of Biophysics, Bose Institute, P-1/12 CIT Scheme VII (M), Kolkata 700 054, India</nlm:aff></affiliation></author><author><name sortKey="Bera, Supriyo" sort="Bera, Supriyo" uniqKey="Bera S" first="Supriyo" last="Bera">Supriyo Bera</name><affiliation><nlm:aff id="A1">Department of Biophysics, Bose Institute, P-1/12 CIT Scheme VII (M), Kolkata 700 054, India</nlm:aff></affiliation></author><author><name sortKey="Midya, Anupam" sort="Midya, Anupam" uniqKey="Midya A" first="Anupam" last="Midya">Anupam Midya</name><affiliation><nlm:aff id="A3">School of Nanoscience and Technology, Indian Institute of Technology Kharagpur, Kharagpur 721302, India</nlm:aff></affiliation></author><author><name sortKey="Fierke, Carol A" sort="Fierke, Carol A" uniqKey="Fierke C" first="Carol A." last="Fierke">Carol A. Fierke</name><affiliation><nlm:aff id="A2">Department of Chemistry, University of Michigan, 930 N. University Avenue, Ann Arbor, MI 48109-1055, USA</nlm:aff></affiliation><affiliation><nlm:aff id="A4">Biophysics, University of Michigan, 930 N. University Avenue, Ann Arbor, MI 48109-1055, USA</nlm:aff></affiliation><affiliation><nlm:aff id="A5">Department of Biological Chemistry, University of Michigan, Ann Arbor, MI 48109, USA</nlm:aff></affiliation></author><author><name sortKey="Ramamoorthy, Ayyalusamy" sort="Ramamoorthy, Ayyalusamy" uniqKey="Ramamoorthy A" first="Ayyalusamy" last="Ramamoorthy">Ayyalusamy Ramamoorthy</name><affiliation><nlm:aff id="A2">Department of Chemistry, University of Michigan, 930 N. University Avenue, Ann Arbor, MI 48109-1055, USA</nlm:aff></affiliation><affiliation><nlm:aff id="A4">Biophysics, University of Michigan, 930 N. University Avenue, Ann Arbor, MI 48109-1055, USA</nlm:aff></affiliation></author><author><name sortKey="Bhunia, Anirban" sort="Bhunia, Anirban" uniqKey="Bhunia A" first="Anirban" last="Bhunia">Anirban Bhunia</name><affiliation><nlm:aff id="A1">Department of Biophysics, Bose Institute, P-1/12 CIT Scheme VII (M), Kolkata 700 054, India</nlm:aff></affiliation><affiliation><nlm:aff id="A2">Department of Chemistry, University of Michigan, 930 N. University Avenue, Ann Arbor, MI 48109-1055, USA</nlm:aff></affiliation><affiliation><nlm:aff id="A4">Biophysics, University of Michigan, 930 N. University Avenue, Ann Arbor, MI 48109-1055, USA</nlm:aff></affiliation></author></analytic><series><title level="j">Biochemistry</title><idno type="ISSN">0006-2960</idno><idno type="eISSN">1520-4995</idno><imprint><date when="2015">2015</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><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><pmc article-type="research-article"><pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
<pmc-dir>properties manuscript</pmc-dir>
<front><journal-meta><journal-id journal-id-type="nlm-journal-id">0370623</journal-id><journal-id journal-id-type="pubmed-jr-id">1028</journal-id><journal-id journal-id-type="nlm-ta">Biochemistry</journal-id><journal-id journal-id-type="iso-abbrev">Biochemistry</journal-id><journal-title-group><journal-title>Biochemistry</journal-title></journal-title-group><issn pub-type="ppub">0006-2960</issn><issn pub-type="epub">1520-4995</issn></journal-meta><article-meta><article-id pub-id-type="pmid">25785896</article-id><article-id pub-id-type="pmc">4903029</article-id><article-id pub-id-type="doi">10.1021/acs.biochem.5b00061</article-id><article-id pub-id-type="manuscript">NIHMS790054</article-id><article-categories><subj-group subj-group-type="heading"><subject>Article</subject></subj-group></article-categories><title-group><article-title>Self-Assembly of a 9-Residue Amyloid-Forming Peptide Fragment of <italic>SARS Corona Virus E-protein</italic>: Mechanism of Self Aggregation and Amyloid-Inhibition of hIAPP</article-title></title-group><contrib-group><contrib contrib-type="author" equal-contrib="yes"><name><surname>Ghosh</surname><given-names>Anirban</given-names></name><xref ref-type="aff" rid="A1">1</xref></contrib><contrib contrib-type="author" equal-contrib="yes"><name><surname>Pithadia</surname><given-names>Amit S.</given-names></name><xref ref-type="aff" rid="A2">2</xref></contrib><contrib contrib-type="author"><name><surname>Bhat</surname><given-names>Jyotsna</given-names></name><xref ref-type="aff" rid="A1">1</xref></contrib><contrib contrib-type="author"><name><surname>Bera</surname><given-names>Supriyo</given-names></name><xref ref-type="aff" rid="A1">1</xref></contrib><contrib contrib-type="author"><name><surname>Midya</surname><given-names>Anupam</given-names></name><xref ref-type="aff" rid="A3">3</xref></contrib><contrib contrib-type="author"><name><surname>Fierke</surname><given-names>Carol A.</given-names></name><xref ref-type="aff" rid="A2">2</xref><xref ref-type="aff" rid="A4">4</xref><xref ref-type="aff" rid="A5">5</xref></contrib><contrib contrib-type="author"><name><surname>Ramamoorthy</surname><given-names>Ayyalusamy</given-names></name><xref ref-type="aff" rid="A2">2</xref><xref ref-type="aff" rid="A4">4</xref></contrib><contrib contrib-type="author"><name><surname>Bhunia</surname><given-names>Anirban</given-names></name><xref ref-type="corresp" rid="CR1">*</xref><xref ref-type="aff" rid="A1">1</xref><xref ref-type="aff" rid="A2">2</xref><xref ref-type="aff" rid="A4">4</xref></contrib></contrib-group><aff id="A1"><label>1</label>Department of Biophysics, Bose Institute, P-1/12 CIT Scheme VII (M), Kolkata 700 054, India</aff><aff id="A2"><label>2</label>Department of Chemistry, University of Michigan, 930 N. University Avenue, Ann Arbor, MI 48109-1055, USA</aff><aff id="A3"><label>3</label>School of Nanoscience and Technology, Indian Institute of Technology Kharagpur, Kharagpur 721302, India</aff><aff id="A4"><label>4</label>Biophysics, University of Michigan, 930 N. University Avenue, Ann Arbor, MI 48109-1055, USA</aff><aff id="A5"><label>5</label>Department of Biological Chemistry, University of Michigan, Ann Arbor, MI 48109, USA</aff><author-notes><corresp id="CR1"><label>*</label><bold>Corresponding Author</bold>: Anirban Bhunia, <email>bhunia@jcbose.ac.in</email> or <email>abhunia@umich.edu</email></corresp></author-notes><pub-date pub-type="nihms-submitted"><day>27</day><month>5</month><year>2016</year></pub-date><pub-date pub-type="epub"><day>24</day><month>3</month><year>2015</year></pub-date><pub-date pub-type="ppub"><day>7</day><month>4</month><year>2015</year></pub-date><pub-date pub-type="pmc-release"><day>11</day><month>6</month><year>2016</year></pub-date><volume>54</volume><issue>13</issue><fpage>2249</fpage><lpage>2261</lpage><pmc-comment>elocation-id from pubmed: 10.1021/acs.biochem.5b00061</pmc-comment>
<abstract><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></abstract></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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