Large-scale all-atom molecular dynamics alanine-scanning of IAPP octapeptides provides insights into the molecular determinants of amyloidogenicity.
Identifieur interne : 000635 ( PubMed/Corpus ); précédent : 000634; suivant : 000636Large-scale all-atom molecular dynamics alanine-scanning of IAPP octapeptides provides insights into the molecular determinants of amyloidogenicity.
Auteurs : Richa Tambi ; Gentaro Morimoto ; Satoshi Kosuda ; Makoto Taiji ; Yutaka KurodaSource :
- Scientific reports [ 2045-2322 ] ; 2019.
Abstract
In order to investigate the early phase of the amyloid formation by the short amyloidogenic octapeptide sequence ('NFGAILSS') derived from IAPP, we carried out a 100ns all-atom molecular dynamics (MD) simulations of systems that contain 27 peptides and over 30,000 water molecules. The large-scale calculations were performed for the wild type sequence and seven alanine-scanned sequences using AMBER 8.0 on RIKEN's special purpose MD-GRAPE3 supercomputer, using the all-atom point charge force field ff99, which do not favor β-structures. Large peptide clusters (size 18-26 mers) were observed for all simulations, and our calculations indicated that isoleucine at position 5 played important role in the formation of β-rich clusters. In the oligomeric state, the wild type and the S7A sequences had the highest β-structure content (~14%), as calculated by DSSP, in line with experimental observations, whereas I5A and G3A had the highest helical content (~20%). Importantly, the β-structure preferences of wild type IAPP originate from its association into clusters and are not intrinsic to its sequence. Altogether, the results of this first large-scale, multi-peptide all-atom molecular dynamics simulation appear to provide insights into the mechanism of amyloidogenic and non-amyloidogenic oligomers that mainly corroborate previous experimental observations.
DOI: 10.1038/s41598-018-38401-w
PubMed: 30792475
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Large-scale all-atom molecular dynamics alanine-scanning of IAPP octapeptides provides insights into the molecular determinants of amyloidogenicity.</title><author><name sortKey="Tambi, Richa" sort="Tambi, Richa" uniqKey="Tambi R" first="Richa" last="Tambi">Richa Tambi</name><affiliation><nlm:affiliation>Department of Biotechnology and Life Sciences, Graduate School of Engineering, Tokyo University of Agriculture and Technology, 2-24-16, Nakamachi, Koganei, Tokyo, 184-8588, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Morimoto, Gentaro" sort="Morimoto, Gentaro" uniqKey="Morimoto G" first="Gentaro" last="Morimoto">Gentaro Morimoto</name><affiliation><nlm:affiliation>Computational Biology Research Core, Quantitative Biology Center (QBiC), RIKEN, 6-2-3, Furuedai, Suita, Osaka, 565-0874, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Kosuda, Satoshi" sort="Kosuda, Satoshi" uniqKey="Kosuda S" first="Satoshi" last="Kosuda">Satoshi Kosuda</name><affiliation><nlm:affiliation>Department of Biotechnology and Life Sciences, Graduate School of Engineering, Tokyo University of Agriculture and Technology, 2-24-16, Nakamachi, Koganei, Tokyo, 184-8588, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Taiji, Makoto" sort="Taiji, Makoto" uniqKey="Taiji M" first="Makoto" last="Taiji">Makoto Taiji</name><affiliation><nlm:affiliation>Computational Biology Research Core, Quantitative Biology Center (QBiC), RIKEN, 6-2-3, Furuedai, Suita, Osaka, 565-0874, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Kuroda, Yutaka" sort="Kuroda, Yutaka" uniqKey="Kuroda Y" first="Yutaka" last="Kuroda">Yutaka Kuroda</name><affiliation><nlm:affiliation>Department of Biotechnology and Life Sciences, Graduate School of Engineering, Tokyo University of Agriculture and Technology, 2-24-16, Nakamachi, Koganei, Tokyo, 184-8588, Japan. ykuroda@cc.tuat.ac.jp.</nlm:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2019">2019</date><idno type="RBID">pubmed:30792475</idno><idno type="pmid">30792475</idno><idno type="doi">10.1038/s41598-018-38401-w</idno><idno type="wicri:Area/PubMed/Corpus">000635</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000635</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Large-scale all-atom molecular dynamics alanine-scanning of IAPP octapeptides provides insights into the molecular determinants of amyloidogenicity.</title><author><name sortKey="Tambi, Richa" sort="Tambi, Richa" uniqKey="Tambi R" first="Richa" last="Tambi">Richa Tambi</name><affiliation><nlm:affiliation>Department of Biotechnology and Life Sciences, Graduate School of Engineering, Tokyo University of Agriculture and Technology, 2-24-16, Nakamachi, Koganei, Tokyo, 184-8588, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Morimoto, Gentaro" sort="Morimoto, Gentaro" uniqKey="Morimoto G" first="Gentaro" last="Morimoto">Gentaro Morimoto</name><affiliation><nlm:affiliation>Computational Biology Research Core, Quantitative Biology Center (QBiC), RIKEN, 6-2-3, Furuedai, Suita, Osaka, 565-0874, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Kosuda, Satoshi" sort="Kosuda, Satoshi" uniqKey="Kosuda S" first="Satoshi" last="Kosuda">Satoshi Kosuda</name><affiliation><nlm:affiliation>Department of Biotechnology and Life Sciences, Graduate School of Engineering, Tokyo University of Agriculture and Technology, 2-24-16, Nakamachi, Koganei, Tokyo, 184-8588, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Taiji, Makoto" sort="Taiji, Makoto" uniqKey="Taiji M" first="Makoto" last="Taiji">Makoto Taiji</name><affiliation><nlm:affiliation>Computational Biology Research Core, Quantitative Biology Center (QBiC), RIKEN, 6-2-3, Furuedai, Suita, Osaka, 565-0874, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Kuroda, Yutaka" sort="Kuroda, Yutaka" uniqKey="Kuroda Y" first="Yutaka" last="Kuroda">Yutaka Kuroda</name><affiliation><nlm:affiliation>Department of Biotechnology and Life Sciences, Graduate School of Engineering, Tokyo University of Agriculture and Technology, 2-24-16, Nakamachi, Koganei, Tokyo, 184-8588, Japan. ykuroda@cc.tuat.ac.jp.</nlm:affiliation></affiliation></author></analytic><series><title level="j">Scientific reports</title><idno type="eISSN">2045-2322</idno><imprint><date when="2019" type="published">2019</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">In order to investigate the early phase of the amyloid formation by the short amyloidogenic octapeptide sequence ('NFGAILSS') derived from IAPP, we carried out a 100ns all-atom molecular dynamics (MD) simulations of systems that contain 27 peptides and over 30,000 water molecules. The large-scale calculations were performed for the wild type sequence and seven alanine-scanned sequences using AMBER 8.0 on RIKEN's special purpose MD-GRAPE3 supercomputer, using the all-atom point charge force field ff99, which do not favor β-structures. Large peptide clusters (size 18-26 mers) were observed for all simulations, and our calculations indicated that isoleucine at position 5 played important role in the formation of β-rich clusters. In the oligomeric state, the wild type and the S7A sequences had the highest β-structure content (~14%), as calculated by DSSP, in line with experimental observations, whereas I5A and G3A had the highest helical content (~20%). Importantly, the β-structure preferences of wild type IAPP originate from its association into clusters and are not intrinsic to its sequence. Altogether, the results of this first large-scale, multi-peptide all-atom molecular dynamics simulation appear to provide insights into the mechanism of amyloidogenic and non-amyloidogenic oligomers that mainly corroborate previous experimental observations.</div></front></TEI><pubmed><MedlineCitation Status="In-Process" Owner="NLM"><PMID Version="1">30792475</PMID><DateRevised><Year>2020</Year><Month>03</Month><Day>17</Day></DateRevised><Article PubModel="Electronic"><Journal><ISSN IssnType="Electronic">2045-2322</ISSN><JournalIssue CitedMedium="Internet"><Volume>9</Volume><Issue>1</Issue><PubDate><Year>2019</Year><Month>02</Month><Day>21</Day></PubDate></JournalIssue><Title>Scientific reports</Title><ISOAbbreviation>Sci Rep</ISOAbbreviation></Journal><ArticleTitle>Large-scale all-atom molecular dynamics alanine-scanning of IAPP octapeptides provides insights into the molecular determinants of amyloidogenicity.</ArticleTitle><Pagination><MedlinePgn>2530</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1038/s41598-018-38401-w</ELocationID><Abstract><AbstractText>In order to investigate the early phase of the amyloid formation by the short amyloidogenic octapeptide sequence ('NFGAILSS') derived from IAPP, we carried out a 100ns all-atom molecular dynamics (MD) simulations of systems that contain 27 peptides and over 30,000 water molecules. The large-scale calculations were performed for the wild type sequence and seven alanine-scanned sequences using AMBER 8.0 on RIKEN's special purpose MD-GRAPE3 supercomputer, using the all-atom point charge force field ff99, which do not favor β-structures. Large peptide clusters (size 18-26 mers) were observed for all simulations, and our calculations indicated that isoleucine at position 5 played important role in the formation of β-rich clusters. In the oligomeric state, the wild type and the S7A sequences had the highest β-structure content (~14%), as calculated by DSSP, in line with experimental observations, whereas I5A and G3A had the highest helical content (~20%). Importantly, the β-structure preferences of wild type IAPP originate from its association into clusters and are not intrinsic to its sequence. Altogether, the results of this first large-scale, multi-peptide all-atom molecular dynamics simulation appear to provide insights into the mechanism of amyloidogenic and non-amyloidogenic oligomers that mainly corroborate previous experimental observations.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Tambi</LastName><ForeName>Richa</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>Department of Biotechnology and Life Sciences, Graduate School of Engineering, Tokyo University of Agriculture and Technology, 2-24-16, Nakamachi, Koganei, Tokyo, 184-8588, Japan.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>College of Medicine, Mohammed Bin Rashid University of Medicine and Health Sciences, Dubai, 505055, UAE.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Morimoto</LastName><ForeName>Gentaro</ForeName><Initials>G</Initials><AffiliationInfo><Affiliation>Computational Biology Research Core, Quantitative Biology Center (QBiC), RIKEN, 6-2-3, Furuedai, Suita, Osaka, 565-0874, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kosuda</LastName><ForeName>Satoshi</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Department of Biotechnology and Life Sciences, Graduate School of Engineering, Tokyo University of Agriculture and Technology, 2-24-16, Nakamachi, Koganei, Tokyo, 184-8588, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Taiji</LastName><ForeName>Makoto</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Computational Biology Research Core, Quantitative Biology Center (QBiC), RIKEN, 6-2-3, Furuedai, Suita, Osaka, 565-0874, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kuroda</LastName><ForeName>Yutaka</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>Department of Biotechnology and Life Sciences, Graduate School of Engineering, Tokyo University of Agriculture and Technology, 2-24-16, Nakamachi, Koganei, Tokyo, 184-8588, Japan. ykuroda@cc.tuat.ac.jp.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2019</Year><Month>02</Month><Day>21</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Sci Rep</MedlineTA><NlmUniqueID>101563288</NlmUniqueID><ISSNLinking>2045-2322</ISSNLinking></MedlineJournalInfo><CitationSubset>IM</CitationSubset></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2018</Year><Month>05</Month><Day>31</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2018</Year><Month>12</Month><Day>11</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2019</Year><Month>2</Month><Day>23</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2019</Year><Month>2</Month><Day>23</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2019</Year><Month>2</Month><Day>23</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>epublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">30792475</ArticleId><ArticleId IdType="doi">10.1038/s41598-018-38401-w</ArticleId><ArticleId IdType="pii">10.1038/s41598-018-38401-w</ArticleId><ArticleId IdType="pmc">PMC6384915</ArticleId></ArticleIdList><ReferenceList><Reference><Citation>J Mol Biol. 2000 Jan 28;295(4):1055-71</Citation><ArticleIdList><ArticleId IdType="pubmed">10656810</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2001 Sep 7;276(36):34156-61</Citation><ArticleIdList><ArticleId IdType="pubmed">11445568</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochim Biophys Acta. 2001 Nov 29;1537(3):179-203</Citation><ArticleIdList><ArticleId IdType="pubmed">11731221</ArticleId></ArticleIdList></Reference><Reference><Citation>J Comput Chem. 2003 Jan 15;24(1):21-31</Citation><ArticleIdList><ArticleId IdType="pubmed">12483672</ArticleId></ArticleIdList></Reference><Reference><Citation>J Mol Med (Berl). 2003 Nov;81(11):678-99</Citation><ArticleIdList><ArticleId IdType="pubmed">12942175</ArticleId></ArticleIdList></Reference><Reference><Citation>Structure. 2004 Mar;12(3):439-55</Citation><ArticleIdList><ArticleId IdType="pubmed">15016360</ArticleId></ArticleIdList></Reference><Reference><Citation>J Chem Phys. 2004 Jul 1;121(1):415-25</Citation><ArticleIdList><ArticleId IdType="pubmed">15260562</ArticleId></ArticleIdList></Reference><Reference><Citation>Proteins. 2005 May 15;59(3):519-27</Citation><ArticleIdList><ArticleId IdType="pubmed">15778964</ArticleId></ArticleIdList></Reference><Reference><Citation>J Am Chem Soc. 2005 Oct 5;127(39):13530-7</Citation><ArticleIdList><ArticleId IdType="pubmed">16190716</ArticleId></ArticleIdList></Reference><Reference><Citation>J Comput Chem. 2005 Dec;26(16):1668-88</Citation><ArticleIdList><ArticleId IdType="pubmed">16200636</ArticleId></ArticleIdList></Reference><Reference><Citation>Biopolymers. 2007 Jan;85(1):12-8</Citation><ArticleIdList><ArticleId IdType="pubmed">16948129</ArticleId></ArticleIdList></Reference><Reference><Citation>Methods Enzymol. 2006;413:217-36</Citation><ArticleIdList><ArticleId IdType="pubmed">17046399</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochemistry. 2007 Mar 20;46(11):3255-61</Citation><ArticleIdList><ArticleId IdType="pubmed">17311418</ArticleId></ArticleIdList></Reference><Reference><Citation>J Am Chem Soc. 2007 Sep 19;129(37):11300-1</Citation><ArticleIdList><ArticleId IdType="pubmed">17722920</ArticleId></ArticleIdList></Reference><Reference><Citation>J Mol Biol. 2007 Nov 30;374(3):806-16</Citation><ArticleIdList><ArticleId IdType="pubmed">17950314</ArticleId></ArticleIdList></Reference><Reference><Citation>J Comput Chem. 2009 Jan 15;30(1):110-8</Citation><ArticleIdList><ArticleId IdType="pubmed">18524021</ArticleId></ArticleIdList></Reference><Reference><Citation>J Am Chem Soc. 2008 Nov 12;130(45):14990-5001</Citation><ArticleIdList><ArticleId IdType="pubmed">18937465</ArticleId></ArticleIdList></Reference><Reference><Citation>Curr Pharm Des. 2008;14(30):3205-18</Citation><ArticleIdList><ArticleId IdType="pubmed">19075701</ArticleId></ArticleIdList></Reference><Reference><Citation>J Mol Biol. 2009 Feb 27;386(3):878-90</Citation><ArticleIdList><ArticleId IdType="pubmed">19133274</ArticleId></ArticleIdList></Reference><Reference><Citation>Annu Rev Biophys. 2009;38:125-52</Citation><ArticleIdList><ArticleId IdType="pubmed">19416063</ArticleId></ArticleIdList></Reference><Reference><Citation>Biophys J. 2009 Jun 17;96(12):5020-9</Citation><ArticleIdList><ArticleId IdType="pubmed">19527662</ArticleId></ArticleIdList></Reference><Reference><Citation>Proteins. 2012 Apr;80(4):1053-65</Citation><ArticleIdList><ArticleId IdType="pubmed">22253015</ArticleId></ArticleIdList></Reference><Reference><Citation>Cell. 2012 Mar 16;148(6):1188-203</Citation><ArticleIdList><ArticleId IdType="pubmed">22424229</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochemistry. 2012 Oct 9;51(40):7974-82</Citation><ArticleIdList><ArticleId IdType="pubmed">22963334</ArticleId></ArticleIdList></Reference><Reference><Citation>Curr Opin Struct Biol. 2013 Feb;23(1):82-9</Citation><ArticleIdList><ArticleId IdType="pubmed">23266002</ArticleId></ArticleIdList></Reference><Reference><Citation>Biophys Rev. 2012 Sep;4(3):205-222</Citation><ArticleIdList><ArticleId IdType="pubmed">23495357</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochim Biophys Acta. 2013 Oct;1834(10):2107-15</Citation><ArticleIdList><ArticleId IdType="pubmed">23811470</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 2013 Nov 26;110(48):19285-90</Citation><ArticleIdList><ArticleId IdType="pubmed">24218609</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochem Med (Zagreb). 2013;23(3):266-80</Citation><ArticleIdList><ArticleId IdType="pubmed">24266296</ArticleId></ArticleIdList></Reference><Reference><Citation>Nat Rev Mol Cell Biol. 2014 Jun;15(6):384-96</Citation><ArticleIdList><ArticleId IdType="pubmed">24854788</ArticleId></ArticleIdList></Reference><Reference><Citation>J Am Chem Soc. 2014 Jun 25;136(25):8947-56</Citation><ArticleIdList><ArticleId IdType="pubmed">24884889</ArticleId></ArticleIdList></Reference><Reference><Citation>FEBS Lett. 2015 Mar 12;589(6):672-9</Citation><ArticleIdList><ArticleId IdType="pubmed">25647034</ArticleId></ArticleIdList></Reference><Reference><Citation>Annu Rev Phys Chem. 2015 Apr;66:643-66</Citation><ArticleIdList><ArticleId IdType="pubmed">25648485</ArticleId></ArticleIdList></Reference><Reference><Citation>Ann Indian Acad Neurol. 2015 Apr-Jun;18(2):138-45</Citation><ArticleIdList><ArticleId IdType="pubmed">26019408</ArticleId></ArticleIdList></Reference><Reference><Citation>PLoS One. 2015 May 29;10(5):e0127865</Citation><ArticleIdList><ArticleId IdType="pubmed">26024352</ArticleId></ArticleIdList></Reference><Reference><Citation>Prog Nucl Magn Reson Spectrosc. 2015 Aug;88-89:86-104</Citation><ArticleIdList><ArticleId IdType="pubmed">26282197</ArticleId></ArticleIdList></Reference><Reference><Citation>Sci Rep. 2016 Jan 28;6:19479</Citation><ArticleIdList><ArticleId IdType="pubmed">26817663</ArticleId></ArticleIdList></Reference><Reference><Citation>FEBS Lett. 2016 Oct;590(20):3501-3509</Citation><ArticleIdList><ArticleId IdType="pubmed">27685427</ArticleId></ArticleIdList></Reference><Reference><Citation>Sci Rep. 2017 Jan 09;7:40065</Citation><ArticleIdList><ArticleId IdType="pubmed">28067252</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2017 Sep 1;292(35):14587-14602</Citation><ArticleIdList><ArticleId IdType="pubmed">28684415</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochim Biophys Acta Proteins Proteom. 2018 Feb;1866(2):366-372</Citation><ArticleIdList><ArticleId IdType="pubmed">28951312</ArticleId></ArticleIdList></Reference><Reference><Citation>Biophys Rev. 2018 Apr;10(2):473-480</Citation><ArticleIdList><ArticleId IdType="pubmed">29302914</ArticleId></ArticleIdList></Reference><Reference><Citation>Biopolymers. 1983 Dec;22(12):2577-637</Citation><ArticleIdList><ArticleId IdType="pubmed">6667333</ArticleId></ArticleIdList></Reference><Reference><Citation>J Mol Biol. 1994 May 20;238(5):777-93</Citation><ArticleIdList><ArticleId IdType="pubmed">8182748</ArticleId></ArticleIdList></Reference><Reference><Citation>J Mol Biol. 1997 Oct 31;273(3):729-39</Citation><ArticleIdList><ArticleId IdType="pubmed">9356260</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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