A novel amyloid designable scaffold and potential inhibitor inspired by GAIIG of amyloid beta and the HIV‐1 V3 loop
The GAIIG sequence, common to the amyloid beta peptide (residues 29–33) and to the HIV‐1 gp120 (residues 24–28 in a typical V3 loop), self‐assembles into amyloid fibrils, as suggested by theory and the experiments presented here. The longer YATGAIIGNII sequence from the V3 loop also self‐assembles i...
Gespeichert in:
| Veröffentlicht in: | FEBS letters 2018-06, Vol.592 (11), p.1777-1788 |
|---|---|
| Hauptverfasser: | , , , , , , , , , , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 1788 |
|---|---|
| container_issue | 11 |
| container_start_page | 1777 |
| container_title | FEBS letters |
| container_volume | 592 |
| creator | Kokotidou, Chrysoula Jonnalagadda, Sai Vamshi R. Orr, Asuka A. Seoane‐Blanco, Mateo Apostolidou, Chrysanthi Pinelopi Raaij, Mark J. Kotzabasaki, Marianna Chatzoudis, Apostolos Jakubowski, Joseph M. Mossou, Estelle Forsyth, V. Trevor Mitchell, Edward P. Bowler, Matthew W. Llamas‐Saiz, Antonio L. Tamamis, Phanourios Mitraki, Anna |
| description | The GAIIG sequence, common to the amyloid beta peptide (residues 29–33) and to the HIV‐1 gp120 (residues 24–28 in a typical V3 loop), self‐assembles into amyloid fibrils, as suggested by theory and the experiments presented here. The longer YATGAIIGNII sequence from the V3 loop also self‐assembles into amyloid fibrils, of which the first three and the last two residues are outside the amyloid GAIIG core. We postulate that this sequence, with suitably selected modifications at the flexible positions, can serve as a designable scaffold for novel amyloid‐based materials. Moreover, we report the single crystal X‐ray structure of the beta‐breaker peptide GAIPIG at 1.05 Å resolution. The structural information provided in this study could serve as the basis for structure‐based design of potential inhibitors of amyloid formation. |
| doi_str_mv | 10.1002/1873-3468.13096 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_2041631065</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2041631065</sourcerecordid><originalsourceid>FETCH-LOGICAL-c3856-e6106024ba05c38c732ccbf92bc33cd616d265614ae327a1d07ed60ab12162643</originalsourceid><addsrcrecordid>eNqFkLtOwzAUQC0EouUxsyGPLCl-JE4zlqovCYkFWC0_bqiRG4c4BXXjE_hGvoSUlq5Mtq_OPZYOQleUDCgh7JYOc57wVAwHlJNCHKH-YXKM-oTQNMnygvfQWYyvpHsPaXGKeqzIcyYI76P1CFfhHTxWq40PzmIL0b1USnvA0aiyDN5iVVlchxaq1imPXbV02rWh6W6xdg1YrDd4NlosZjiUB5GGVv1utkvA88Xz9-cXxc8c-xDqC3RSKh_hcn-eo6fp5HE8T-4fZovx6D4xfJiJBAQlgrBUK5J1E5NzZowuC6YN58YKKiwTmaCpAs5yRS3JwQqiNGVUMJHyc3Sz89ZNeFtDbOXKRQPeqwrCOkpGUip490nWobc71DQhxgZKWTdupZqNpERuW8ttWbktK39bdxvXe_lar8Ae-L-4HSB2wIfzsPnPJ6eTO7Yz_wAgOYg-</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2041631065</pqid></control><display><type>article</type><title>A novel amyloid designable scaffold and potential inhibitor inspired by GAIIG of amyloid beta and the HIV‐1 V3 loop</title><source>MEDLINE</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><source>Access via Wiley Online Library</source><source>Wiley Online Library (Open Access Collection)</source><source>Alma/SFX Local Collection</source><creator>Kokotidou, Chrysoula ; Jonnalagadda, Sai Vamshi R. ; Orr, Asuka A. ; Seoane‐Blanco, Mateo ; Apostolidou, Chrysanthi Pinelopi ; Raaij, Mark J. ; Kotzabasaki, Marianna ; Chatzoudis, Apostolos ; Jakubowski, Joseph M. ; Mossou, Estelle ; Forsyth, V. Trevor ; Mitchell, Edward P. ; Bowler, Matthew W. ; Llamas‐Saiz, Antonio L. ; Tamamis, Phanourios ; Mitraki, Anna</creator><creatorcontrib>Kokotidou, Chrysoula ; Jonnalagadda, Sai Vamshi R. ; Orr, Asuka A. ; Seoane‐Blanco, Mateo ; Apostolidou, Chrysanthi Pinelopi ; Raaij, Mark J. ; Kotzabasaki, Marianna ; Chatzoudis, Apostolos ; Jakubowski, Joseph M. ; Mossou, Estelle ; Forsyth, V. Trevor ; Mitchell, Edward P. ; Bowler, Matthew W. ; Llamas‐Saiz, Antonio L. ; Tamamis, Phanourios ; Mitraki, Anna</creatorcontrib><description>The GAIIG sequence, common to the amyloid beta peptide (residues 29–33) and to the HIV‐1 gp120 (residues 24–28 in a typical V3 loop), self‐assembles into amyloid fibrils, as suggested by theory and the experiments presented here. The longer YATGAIIGNII sequence from the V3 loop also self‐assembles into amyloid fibrils, of which the first three and the last two residues are outside the amyloid GAIIG core. We postulate that this sequence, with suitably selected modifications at the flexible positions, can serve as a designable scaffold for novel amyloid‐based materials. Moreover, we report the single crystal X‐ray structure of the beta‐breaker peptide GAIPIG at 1.05 Å resolution. The structural information provided in this study could serve as the basis for structure‐based design of potential inhibitors of amyloid formation.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1002/1873-3468.13096</identifier><identifier>PMID: 29772603</identifier><language>eng</language><publisher>England</publisher><subject>amyloid ; Amyloid beta-Peptides - chemistry ; beta‐breaker ; Crystallography, X-Ray ; HIV Envelope Protein gp120 - chemistry ; HIV-1 - chemistry ; Humans ; peptide self‐assembly ; Protein Structure, Secondary</subject><ispartof>FEBS letters, 2018-06, Vol.592 (11), p.1777-1788</ispartof><rights>2018 Federation of European Biochemical Societies</rights><rights>2018 Federation of European Biochemical Societies.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3856-e6106024ba05c38c732ccbf92bc33cd616d265614ae327a1d07ed60ab12162643</citedby><cites>FETCH-LOGICAL-c3856-e6106024ba05c38c732ccbf92bc33cd616d265614ae327a1d07ed60ab12162643</cites><orcidid>0000-0001-7686-2238 ; 0000-0001-5072-1939 ; 0000-0001-9134-0366 ; 0000-0003-0380-3477 ; 0000-0003-4704-3131 ; 0000-0002-4781-1375 ; 0000-0002-1899-4942 ; 0000-0003-4375-2272 ; 0000-0002-3342-2651 ; 0000-0003-4628-526X ; 0000-0002-8203-3791 ; 0000-0002-0496-9025 ; 0000-0001-9809-9536 ; 0000-0003-4825-9022 ; 0000-0001-7327-238X ; 0000-0003-0465-3351</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2F1873-3468.13096$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2F1873-3468.13096$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>315,781,785,1418,1434,27929,27930,45579,45580,46414,46838</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/29772603$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kokotidou, Chrysoula</creatorcontrib><creatorcontrib>Jonnalagadda, Sai Vamshi R.</creatorcontrib><creatorcontrib>Orr, Asuka A.</creatorcontrib><creatorcontrib>Seoane‐Blanco, Mateo</creatorcontrib><creatorcontrib>Apostolidou, Chrysanthi Pinelopi</creatorcontrib><creatorcontrib>Raaij, Mark J.</creatorcontrib><creatorcontrib>Kotzabasaki, Marianna</creatorcontrib><creatorcontrib>Chatzoudis, Apostolos</creatorcontrib><creatorcontrib>Jakubowski, Joseph M.</creatorcontrib><creatorcontrib>Mossou, Estelle</creatorcontrib><creatorcontrib>Forsyth, V. Trevor</creatorcontrib><creatorcontrib>Mitchell, Edward P.</creatorcontrib><creatorcontrib>Bowler, Matthew W.</creatorcontrib><creatorcontrib>Llamas‐Saiz, Antonio L.</creatorcontrib><creatorcontrib>Tamamis, Phanourios</creatorcontrib><creatorcontrib>Mitraki, Anna</creatorcontrib><title>A novel amyloid designable scaffold and potential inhibitor inspired by GAIIG of amyloid beta and the HIV‐1 V3 loop</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>The GAIIG sequence, common to the amyloid beta peptide (residues 29–33) and to the HIV‐1 gp120 (residues 24–28 in a typical V3 loop), self‐assembles into amyloid fibrils, as suggested by theory and the experiments presented here. The longer YATGAIIGNII sequence from the V3 loop also self‐assembles into amyloid fibrils, of which the first three and the last two residues are outside the amyloid GAIIG core. We postulate that this sequence, with suitably selected modifications at the flexible positions, can serve as a designable scaffold for novel amyloid‐based materials. Moreover, we report the single crystal X‐ray structure of the beta‐breaker peptide GAIPIG at 1.05 Å resolution. The structural information provided in this study could serve as the basis for structure‐based design of potential inhibitors of amyloid formation.</description><subject>amyloid</subject><subject>Amyloid beta-Peptides - chemistry</subject><subject>beta‐breaker</subject><subject>Crystallography, X-Ray</subject><subject>HIV Envelope Protein gp120 - chemistry</subject><subject>HIV-1 - chemistry</subject><subject>Humans</subject><subject>peptide self‐assembly</subject><subject>Protein Structure, Secondary</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkLtOwzAUQC0EouUxsyGPLCl-JE4zlqovCYkFWC0_bqiRG4c4BXXjE_hGvoSUlq5Mtq_OPZYOQleUDCgh7JYOc57wVAwHlJNCHKH-YXKM-oTQNMnygvfQWYyvpHsPaXGKeqzIcyYI76P1CFfhHTxWq40PzmIL0b1USnvA0aiyDN5iVVlchxaq1imPXbV02rWh6W6xdg1YrDd4NlosZjiUB5GGVv1utkvA88Xz9-cXxc8c-xDqC3RSKh_hcn-eo6fp5HE8T-4fZovx6D4xfJiJBAQlgrBUK5J1E5NzZowuC6YN58YKKiwTmaCpAs5yRS3JwQqiNGVUMJHyc3Sz89ZNeFtDbOXKRQPeqwrCOkpGUip490nWobc71DQhxgZKWTdupZqNpERuW8ttWbktK39bdxvXe_lar8Ae-L-4HSB2wIfzsPnPJ6eTO7Yz_wAgOYg-</recordid><startdate>201806</startdate><enddate>201806</enddate><creator>Kokotidou, Chrysoula</creator><creator>Jonnalagadda, Sai Vamshi R.</creator><creator>Orr, Asuka A.</creator><creator>Seoane‐Blanco, Mateo</creator><creator>Apostolidou, Chrysanthi Pinelopi</creator><creator>Raaij, Mark J.</creator><creator>Kotzabasaki, Marianna</creator><creator>Chatzoudis, Apostolos</creator><creator>Jakubowski, Joseph M.</creator><creator>Mossou, Estelle</creator><creator>Forsyth, V. Trevor</creator><creator>Mitchell, Edward P.</creator><creator>Bowler, Matthew W.</creator><creator>Llamas‐Saiz, Antonio L.</creator><creator>Tamamis, Phanourios</creator><creator>Mitraki, Anna</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0001-7686-2238</orcidid><orcidid>https://orcid.org/0000-0001-5072-1939</orcidid><orcidid>https://orcid.org/0000-0001-9134-0366</orcidid><orcidid>https://orcid.org/0000-0003-0380-3477</orcidid><orcidid>https://orcid.org/0000-0003-4704-3131</orcidid><orcidid>https://orcid.org/0000-0002-4781-1375</orcidid><orcidid>https://orcid.org/0000-0002-1899-4942</orcidid><orcidid>https://orcid.org/0000-0003-4375-2272</orcidid><orcidid>https://orcid.org/0000-0002-3342-2651</orcidid><orcidid>https://orcid.org/0000-0003-4628-526X</orcidid><orcidid>https://orcid.org/0000-0002-8203-3791</orcidid><orcidid>https://orcid.org/0000-0002-0496-9025</orcidid><orcidid>https://orcid.org/0000-0001-9809-9536</orcidid><orcidid>https://orcid.org/0000-0003-4825-9022</orcidid><orcidid>https://orcid.org/0000-0001-7327-238X</orcidid><orcidid>https://orcid.org/0000-0003-0465-3351</orcidid></search><sort><creationdate>201806</creationdate><title>A novel amyloid designable scaffold and potential inhibitor inspired by GAIIG of amyloid beta and the HIV‐1 V3 loop</title><author>Kokotidou, Chrysoula ; Jonnalagadda, Sai Vamshi R. ; Orr, Asuka A. ; Seoane‐Blanco, Mateo ; Apostolidou, Chrysanthi Pinelopi ; Raaij, Mark J. ; Kotzabasaki, Marianna ; Chatzoudis, Apostolos ; Jakubowski, Joseph M. ; Mossou, Estelle ; Forsyth, V. Trevor ; Mitchell, Edward P. ; Bowler, Matthew W. ; Llamas‐Saiz, Antonio L. ; Tamamis, Phanourios ; Mitraki, Anna</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3856-e6106024ba05c38c732ccbf92bc33cd616d265614ae327a1d07ed60ab12162643</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2018</creationdate><topic>amyloid</topic><topic>Amyloid beta-Peptides - chemistry</topic><topic>beta‐breaker</topic><topic>Crystallography, X-Ray</topic><topic>HIV Envelope Protein gp120 - chemistry</topic><topic>HIV-1 - chemistry</topic><topic>Humans</topic><topic>peptide self‐assembly</topic><topic>Protein Structure, Secondary</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kokotidou, Chrysoula</creatorcontrib><creatorcontrib>Jonnalagadda, Sai Vamshi R.</creatorcontrib><creatorcontrib>Orr, Asuka A.</creatorcontrib><creatorcontrib>Seoane‐Blanco, Mateo</creatorcontrib><creatorcontrib>Apostolidou, Chrysanthi Pinelopi</creatorcontrib><creatorcontrib>Raaij, Mark J.</creatorcontrib><creatorcontrib>Kotzabasaki, Marianna</creatorcontrib><creatorcontrib>Chatzoudis, Apostolos</creatorcontrib><creatorcontrib>Jakubowski, Joseph M.</creatorcontrib><creatorcontrib>Mossou, Estelle</creatorcontrib><creatorcontrib>Forsyth, V. Trevor</creatorcontrib><creatorcontrib>Mitchell, Edward P.</creatorcontrib><creatorcontrib>Bowler, Matthew W.</creatorcontrib><creatorcontrib>Llamas‐Saiz, Antonio L.</creatorcontrib><creatorcontrib>Tamamis, Phanourios</creatorcontrib><creatorcontrib>Mitraki, Anna</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kokotidou, Chrysoula</au><au>Jonnalagadda, Sai Vamshi R.</au><au>Orr, Asuka A.</au><au>Seoane‐Blanco, Mateo</au><au>Apostolidou, Chrysanthi Pinelopi</au><au>Raaij, Mark J.</au><au>Kotzabasaki, Marianna</au><au>Chatzoudis, Apostolos</au><au>Jakubowski, Joseph M.</au><au>Mossou, Estelle</au><au>Forsyth, V. Trevor</au><au>Mitchell, Edward P.</au><au>Bowler, Matthew W.</au><au>Llamas‐Saiz, Antonio L.</au><au>Tamamis, Phanourios</au><au>Mitraki, Anna</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A novel amyloid designable scaffold and potential inhibitor inspired by GAIIG of amyloid beta and the HIV‐1 V3 loop</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>2018-06</date><risdate>2018</risdate><volume>592</volume><issue>11</issue><spage>1777</spage><epage>1788</epage><pages>1777-1788</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>The GAIIG sequence, common to the amyloid beta peptide (residues 29–33) and to the HIV‐1 gp120 (residues 24–28 in a typical V3 loop), self‐assembles into amyloid fibrils, as suggested by theory and the experiments presented here. The longer YATGAIIGNII sequence from the V3 loop also self‐assembles into amyloid fibrils, of which the first three and the last two residues are outside the amyloid GAIIG core. We postulate that this sequence, with suitably selected modifications at the flexible positions, can serve as a designable scaffold for novel amyloid‐based materials. Moreover, we report the single crystal X‐ray structure of the beta‐breaker peptide GAIPIG at 1.05 Å resolution. The structural information provided in this study could serve as the basis for structure‐based design of potential inhibitors of amyloid formation.</abstract><cop>England</cop><pmid>29772603</pmid><doi>10.1002/1873-3468.13096</doi><tpages>12</tpages><orcidid>https://orcid.org/0000-0001-7686-2238</orcidid><orcidid>https://orcid.org/0000-0001-5072-1939</orcidid><orcidid>https://orcid.org/0000-0001-9134-0366</orcidid><orcidid>https://orcid.org/0000-0003-0380-3477</orcidid><orcidid>https://orcid.org/0000-0003-4704-3131</orcidid><orcidid>https://orcid.org/0000-0002-4781-1375</orcidid><orcidid>https://orcid.org/0000-0002-1899-4942</orcidid><orcidid>https://orcid.org/0000-0003-4375-2272</orcidid><orcidid>https://orcid.org/0000-0002-3342-2651</orcidid><orcidid>https://orcid.org/0000-0003-4628-526X</orcidid><orcidid>https://orcid.org/0000-0002-8203-3791</orcidid><orcidid>https://orcid.org/0000-0002-0496-9025</orcidid><orcidid>https://orcid.org/0000-0001-9809-9536</orcidid><orcidid>https://orcid.org/0000-0003-4825-9022</orcidid><orcidid>https://orcid.org/0000-0001-7327-238X</orcidid><orcidid>https://orcid.org/0000-0003-0465-3351</orcidid><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0014-5793 |
| ispartof | FEBS letters, 2018-06, Vol.592 (11), p.1777-1788 |
| issn | 0014-5793 1873-3468 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_2041631065 |
| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Access via Wiley Online Library; Wiley Online Library (Open Access Collection); Alma/SFX Local Collection |
| subjects | amyloid Amyloid beta-Peptides - chemistry beta‐breaker Crystallography, X-Ray HIV Envelope Protein gp120 - chemistry HIV-1 - chemistry Humans peptide self‐assembly Protein Structure, Secondary |
| title | A novel amyloid designable scaffold and potential inhibitor inspired by GAIIG of amyloid beta and the HIV‐1 V3 loop |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-15T03%3A41%3A33IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=A%20novel%20amyloid%20designable%20scaffold%20and%20potential%20inhibitor%20inspired%20by%20GAIIG%20of%20amyloid%20beta%20and%20the%20HIV%E2%80%901%20V3%20loop&rft.jtitle=FEBS%20letters&rft.au=Kokotidou,%20Chrysoula&rft.date=2018-06&rft.volume=592&rft.issue=11&rft.spage=1777&rft.epage=1788&rft.pages=1777-1788&rft.issn=0014-5793&rft.eissn=1873-3468&rft_id=info:doi/10.1002/1873-3468.13096&rft_dat=%3Cproquest_cross%3E2041631065%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=2041631065&rft_id=info:pmid/29772603&rfr_iscdi=true |