Probing differences among Aβ oligomers with two triangular trimers derived from Aβ
The assembly of the β-amyloid peptide (Aβ) to form oligomers and fibrils is closely associated with the pathogenesis and progression of Alzheimer's disease. Aβ is a shape-shifting peptide capable of adopting many conformations and folds within the multitude of oligomers and fibrils the peptide...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2023-05, Vol.120 (22), p.e2219216120 |
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| creator | Kreutzer, Adam G Guaglianone, Gretchen Yoo, Stan Parrocha, Chelsea Marie T Ruttenberg, Sarah M Malonis, Ryan J Tong, Karen Lin, Yu-Fu Nguyen, Jennifer T Howitz, William J Diab, Michelle N Hamza, Imane L Lai, Jonathan R Wysocki, Vicki H Nowick, James S |
| description | The assembly of the β-amyloid peptide (Aβ) to form oligomers and fibrils is closely associated with the pathogenesis and progression of Alzheimer's disease. Aβ is a shape-shifting peptide capable of adopting many conformations and folds within the multitude of oligomers and fibrils the peptide forms. These properties have precluded detailed structural elucidation and biological characterization of homogeneous, well-defined Aβ oligomers. In this paper, we compare the structural, biophysical, and biological characteristics of two different covalently stabilized isomorphic trimers derived from the central and
-terminal regions Aβ. X-ray crystallography reveals the structures of the trimers and shows that each trimer forms a ball-shaped dodecamer. Solution-phase and cell-based studies demonstrate that the two trimers exhibit markedly different assembly and biological properties. One trimer forms small soluble oligomers that enter cells through endocytosis and activate capase-3/7-mediated apoptosis, while the other trimer forms large insoluble aggregates that accumulate on the outer plasma membrane and elicit cellular toxicity through an apoptosis-independent mechanism. The two trimers also exhibit different effects on the aggregation, toxicity, and cellular interaction of full-length Aβ, with one trimer showing a greater propensity to interact with Aβ than the other. The studies described in this paper indicate that the two trimers share structural, biophysical, and biological characteristics with oligomers of full-length Aβ. The varying structural, assembly, and biological characteristics of the two trimers provide a working model for how different Aβ trimers can assemble and lead to different biological effects, which may help shed light on the differences among Aβ oligomers. |
| doi_str_mv | 10.1073/pnas.2219216120 |
| format | Article |
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-terminal regions Aβ. X-ray crystallography reveals the structures of the trimers and shows that each trimer forms a ball-shaped dodecamer. Solution-phase and cell-based studies demonstrate that the two trimers exhibit markedly different assembly and biological properties. One trimer forms small soluble oligomers that enter cells through endocytosis and activate capase-3/7-mediated apoptosis, while the other trimer forms large insoluble aggregates that accumulate on the outer plasma membrane and elicit cellular toxicity through an apoptosis-independent mechanism. The two trimers also exhibit different effects on the aggregation, toxicity, and cellular interaction of full-length Aβ, with one trimer showing a greater propensity to interact with Aβ than the other. The studies described in this paper indicate that the two trimers share structural, biophysical, and biological characteristics with oligomers of full-length Aβ. The varying structural, assembly, and biological characteristics of the two trimers provide a working model for how different Aβ trimers can assemble and lead to different biological effects, which may help shed light on the differences among Aβ oligomers.</description><identifier>ISSN: 0027-8424</identifier><identifier>ISSN: 1091-6490</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.2219216120</identifier><identifier>PMID: 37216514</identifier><language>eng</language><publisher>United States: National Academy of Sciences</publisher><subject>Alzheimer Disease ; Alzheimer's disease ; Amyloid beta-Peptides - metabolism ; Apoptosis ; Assembly ; Biological effects ; Biological properties ; Biological Sciences ; Cell Membrane - metabolism ; Crystallography ; Crystallography, X-Ray ; Endocytosis ; Fibrils ; Humans ; Neurodegenerative diseases ; Oligomers ; Pathogenesis ; Peptide Fragments - chemistry ; Peptides ; Physical Sciences ; Protein Conformation ; Structural analysis ; Toxicity ; Trimers ; X-ray crystallography ; β-Amyloid</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 2023-05, Vol.120 (22), p.e2219216120</ispartof><rights>Copyright National Academy of Sciences May 30, 2023</rights><rights>Copyright © 2023 the Author(s). Published by PNAS. 2023</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c422t-59735bf9ae2be5fef6b4348d0a7be5babb92c3a504b1ad056492270c97671f783</citedby><cites>FETCH-LOGICAL-c422t-59735bf9ae2be5fef6b4348d0a7be5babb92c3a504b1ad056492270c97671f783</cites><orcidid>0000-0002-2273-1029 ; 0000-0003-0495-2538 ; 0009-0004-9748-4378 ; 0000-0002-9724-6298 ; 0000-0003-4739-0619 ; 0000-0002-5759-3180 ; 0000-0003-0476-5193 ; 0000-0001-6323-7126 ; 0000-0002-5189-2550 ; 0000-0002-4863-0015</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC10235986/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC10235986/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,881,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/37216514$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kreutzer, Adam G</creatorcontrib><creatorcontrib>Guaglianone, Gretchen</creatorcontrib><creatorcontrib>Yoo, Stan</creatorcontrib><creatorcontrib>Parrocha, Chelsea Marie T</creatorcontrib><creatorcontrib>Ruttenberg, Sarah M</creatorcontrib><creatorcontrib>Malonis, Ryan J</creatorcontrib><creatorcontrib>Tong, Karen</creatorcontrib><creatorcontrib>Lin, Yu-Fu</creatorcontrib><creatorcontrib>Nguyen, Jennifer T</creatorcontrib><creatorcontrib>Howitz, William J</creatorcontrib><creatorcontrib>Diab, Michelle N</creatorcontrib><creatorcontrib>Hamza, Imane L</creatorcontrib><creatorcontrib>Lai, Jonathan R</creatorcontrib><creatorcontrib>Wysocki, Vicki H</creatorcontrib><creatorcontrib>Nowick, James S</creatorcontrib><title>Probing differences among Aβ oligomers with two triangular trimers derived from Aβ</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>The assembly of the β-amyloid peptide (Aβ) to form oligomers and fibrils is closely associated with the pathogenesis and progression of Alzheimer's disease. 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-terminal regions Aβ. X-ray crystallography reveals the structures of the trimers and shows that each trimer forms a ball-shaped dodecamer. Solution-phase and cell-based studies demonstrate that the two trimers exhibit markedly different assembly and biological properties. One trimer forms small soluble oligomers that enter cells through endocytosis and activate capase-3/7-mediated apoptosis, while the other trimer forms large insoluble aggregates that accumulate on the outer plasma membrane and elicit cellular toxicity through an apoptosis-independent mechanism. The two trimers also exhibit different effects on the aggregation, toxicity, and cellular interaction of full-length Aβ, with one trimer showing a greater propensity to interact with Aβ than the other. The studies described in this paper indicate that the two trimers share structural, biophysical, and biological characteristics with oligomers of full-length Aβ. The varying structural, assembly, and biological characteristics of the two trimers provide a working model for how different Aβ trimers can assemble and lead to different biological effects, which may help shed light on the differences among Aβ oligomers.</description><subject>Alzheimer Disease</subject><subject>Alzheimer's disease</subject><subject>Amyloid beta-Peptides - metabolism</subject><subject>Apoptosis</subject><subject>Assembly</subject><subject>Biological effects</subject><subject>Biological properties</subject><subject>Biological Sciences</subject><subject>Cell Membrane - metabolism</subject><subject>Crystallography</subject><subject>Crystallography, X-Ray</subject><subject>Endocytosis</subject><subject>Fibrils</subject><subject>Humans</subject><subject>Neurodegenerative diseases</subject><subject>Oligomers</subject><subject>Pathogenesis</subject><subject>Peptide Fragments - chemistry</subject><subject>Peptides</subject><subject>Physical Sciences</subject><subject>Protein Conformation</subject><subject>Structural analysis</subject><subject>Toxicity</subject><subject>Trimers</subject><subject>X-ray crystallography</subject><subject>β-Amyloid</subject><issn>0027-8424</issn><issn>1091-6490</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2023</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdkctOxSAQhonR6PGydmeauHFTHSiUsjLGeEtMdKFrAi0cMW05QqvxtXwQn0nqXVdc5pt_5s-P0DaGfQy8OFj0Ku4TggXBJSawhGYYBM5LKmAZzQAIzytK6Bpaj_EeAASrYBWtFTzxDNMZurkOXrt-njXOWhNMX5uYqc6nn6PXl8y3bu47E2L25Ia7bHjy2RCc6udjq8J0fa81JrhH02Q2-G5q20QrVrXRbH2eG-j29OTm-Dy_vDq7OD66zGtKyJAzwQumrVCGaMOssaWmBa0aUDy9tdJakLpQDKjGqgGWXBHCoRa85NjyqthAhx-6i1F3pqlNPwTVykVaS4Vn6ZWTfyu9u5Nz_ygxkIKJqkwKe58KwT-MJg6yc7E2bat648coSYUrYFTgadjuP_Tej6FP_hJFCBXJDk3UwQdVBx9jMPZ7GwxyikxOkcmfyFLHzm8T3_xXRsUb68yUxw</recordid><startdate>20230530</startdate><enddate>20230530</enddate><creator>Kreutzer, Adam G</creator><creator>Guaglianone, Gretchen</creator><creator>Yoo, Stan</creator><creator>Parrocha, Chelsea Marie T</creator><creator>Ruttenberg, Sarah M</creator><creator>Malonis, Ryan J</creator><creator>Tong, Karen</creator><creator>Lin, Yu-Fu</creator><creator>Nguyen, Jennifer T</creator><creator>Howitz, William J</creator><creator>Diab, Michelle N</creator><creator>Hamza, Imane L</creator><creator>Lai, Jonathan R</creator><creator>Wysocki, Vicki H</creator><creator>Nowick, James S</creator><general>National Academy of Sciences</general><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>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0002-2273-1029</orcidid><orcidid>https://orcid.org/0000-0003-0495-2538</orcidid><orcidid>https://orcid.org/0009-0004-9748-4378</orcidid><orcidid>https://orcid.org/0000-0002-9724-6298</orcidid><orcidid>https://orcid.org/0000-0003-4739-0619</orcidid><orcidid>https://orcid.org/0000-0002-5759-3180</orcidid><orcidid>https://orcid.org/0000-0003-0476-5193</orcidid><orcidid>https://orcid.org/0000-0001-6323-7126</orcidid><orcidid>https://orcid.org/0000-0002-5189-2550</orcidid><orcidid>https://orcid.org/0000-0002-4863-0015</orcidid></search><sort><creationdate>20230530</creationdate><title>Probing differences among Aβ oligomers with two triangular trimers derived from Aβ</title><author>Kreutzer, Adam G ; 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Aβ is a shape-shifting peptide capable of adopting many conformations and folds within the multitude of oligomers and fibrils the peptide forms. These properties have precluded detailed structural elucidation and biological characterization of homogeneous, well-defined Aβ oligomers. In this paper, we compare the structural, biophysical, and biological characteristics of two different covalently stabilized isomorphic trimers derived from the central and
-terminal regions Aβ. X-ray crystallography reveals the structures of the trimers and shows that each trimer forms a ball-shaped dodecamer. Solution-phase and cell-based studies demonstrate that the two trimers exhibit markedly different assembly and biological properties. One trimer forms small soluble oligomers that enter cells through endocytosis and activate capase-3/7-mediated apoptosis, while the other trimer forms large insoluble aggregates that accumulate on the outer plasma membrane and elicit cellular toxicity through an apoptosis-independent mechanism. The two trimers also exhibit different effects on the aggregation, toxicity, and cellular interaction of full-length Aβ, with one trimer showing a greater propensity to interact with Aβ than the other. The studies described in this paper indicate that the two trimers share structural, biophysical, and biological characteristics with oligomers of full-length Aβ. The varying structural, assembly, and biological characteristics of the two trimers provide a working model for how different Aβ trimers can assemble and lead to different biological effects, which may help shed light on the differences among Aβ oligomers.</abstract><cop>United States</cop><pub>National Academy of Sciences</pub><pmid>37216514</pmid><doi>10.1073/pnas.2219216120</doi><orcidid>https://orcid.org/0000-0002-2273-1029</orcidid><orcidid>https://orcid.org/0000-0003-0495-2538</orcidid><orcidid>https://orcid.org/0009-0004-9748-4378</orcidid><orcidid>https://orcid.org/0000-0002-9724-6298</orcidid><orcidid>https://orcid.org/0000-0003-4739-0619</orcidid><orcidid>https://orcid.org/0000-0002-5759-3180</orcidid><orcidid>https://orcid.org/0000-0003-0476-5193</orcidid><orcidid>https://orcid.org/0000-0001-6323-7126</orcidid><orcidid>https://orcid.org/0000-0002-5189-2550</orcidid><orcidid>https://orcid.org/0000-0002-4863-0015</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Alzheimer Disease Alzheimer's disease Amyloid beta-Peptides - metabolism Apoptosis Assembly Biological effects Biological properties Biological Sciences Cell Membrane - metabolism Crystallography Crystallography, X-Ray Endocytosis Fibrils Humans Neurodegenerative diseases Oligomers Pathogenesis Peptide Fragments - chemistry Peptides Physical Sciences Protein Conformation Structural analysis Toxicity Trimers X-ray crystallography β-Amyloid |
| title | Probing differences among Aβ oligomers with two triangular trimers derived from Aβ |
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