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Multimerization of a rationally designed nanobody for enhanced avidity toward Aβ42 oligomers.

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Τίτλος: Multimerization of a rationally designed nanobody for enhanced avidity toward Aβ42 oligomers.
Συγγραφείς: Nowinska M; Centre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Cambridge, UK., Suh E; Centre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Cambridge, UK., Mogilevsky C; Centre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Cambridge, UK., Vendruscolo M; Centre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Cambridge, UK.
Πηγή: Protein science : a publication of the Protein Society [Protein Sci] 2026 Sep; Vol. 35 (9), pp. e70754.
Τύπος έκδοσης: Journal Article
Γλώσσα: English
Στοιχεία περιοδικού: Publisher: Cold Spring Harbor Laboratory Press Country of Publication: United States NLM ID: 9211750 Publication Model: Print Cited Medium: Internet ISSN: 1469-896X (Electronic) Linking ISSN: 09618368 NLM ISO Abbreviation: Protein Sci Subsets: MEDLINE
Imprint Name(s): Publication: 2001- : Woodbury, NY : Cold Spring Harbor Laboratory Press
Original Publication: New York, N.Y. : Cambridge University Press, c1992-
Ιατρικοί όροι (MeSH): Amyloid beta-Peptides*/chemistry , Amyloid beta-Peptides*/immunology , Amyloid beta-Peptides*/metabolism , Peptide Fragments*/chemistry , Peptide Fragments*/immunology , Peptide Fragments*/metabolism , Single-Domain Antibodies*/chemistry , Single-Domain Antibodies*/genetics , Single-Domain Antibodies*/immunology , Protein Multimerization*, Humans ; Alzheimer Disease
Περίληψη: Alzheimer's disease affects tens of millions of people worldwide and is associated with the self-assembly of the Aβ42 peptide into amyloid aggregates. Among the species formed during this process, soluble oligomeric intermediates are the most closely linked to neurotoxicity and are therefore an attractive target for both therapeutic and diagnostic strategies. Their conformational heterogeneity and transient nature, however, have so far hindered the development of reagents that recognize them selectively, and no fully quantitative biomarker of Aβ42 oligomers is widely available. To address this problem, we use a rationally designed conformation-specific single-domain antibody, DesAbO, which binds selectively to Aβ42 oligomers. By using enzyme-linked immunosorbent assay, we show that encoding self-assembling multimerization domains in the DesAbO plasmid yields multimeric variants with increased avidity toward Aβ42 oligomers. In aggregation assays, the multimeric variants inhibited Aβ42 aggregation at concentrations at which the monomeric form was no longer effective, with the SB175 trimer performing best. These results show how multimerization can be used to enhance the recognition of Aβ42 oligomers and offer a route toward diagnostic and therapeutic agents for Alzheimer's disease and other protein misfolding disorders.
(© 2026 The Author(s). Protein Science published by Wiley Periodicals LLC on behalf of The Protein Society.)
References: Alzheimers Dement. 2018 Apr;14(4):535-562. (PMID: 29653606)
Protein Sci. 2026 Sep;35(9):e70754. (PMID: 42615560)
JAMA. 2023 Aug 8;330(6):512-527. (PMID: 37459141)
Mol Psychiatry. 2021 Oct;26(10):5481-5503. (PMID: 34456336)
Mol Cell Neurosci. 2024 Sep;130:103949. (PMID: 38906341)
PLoS Pathog. 2025 Dec 8;21(12):e1013744. (PMID: 41359663)
Cell. 2019 Oct 3;179(2):312-339. (PMID: 31564456)
Commun Biol. 2026 Mar 27;9(1):. (PMID: 41896453)
Proc Natl Acad Sci U S A. 2013 Jun 11;110(24):9758-63. (PMID: 23703910)
Nat Rev Chem. 2021 Apr;5(4):277-294. (PMID: 37117282)
BioDrugs. 2024 Jan;38(1):5-22. (PMID: 37955845)
Nat Biotechnol. 2017 Nov;35(11):1026-1028. (PMID: 29035372)
Bioconjug Chem. 2022 Aug 17;33(8):1494-1504. (PMID: 35875886)
N Engl J Med. 2021 May 6;384(18):1691-1704. (PMID: 33720637)
Methods Mol Biol. 2020;2141:731-754. (PMID: 32696387)
Nat Rev Dis Primers. 2021 May 13;7(1):33. (PMID: 33986301)
Nat Methods. 2022 Jun;19(6):679-682. (PMID: 35637307)
Proc Natl Acad Sci U S A. 2020 Jun 16;117(24):13509-13518. (PMID: 32493749)
Nature. 2016 Aug 31;537(7618):50-6. (PMID: 27582220)
Nat Neurosci. 2012 Jan 29;15(3):349-57. (PMID: 22286176)
Science. 2002 Jul 19;297(5580):353-6. (PMID: 12130773)
Nat Biotechnol. 2011 Mar;29(3):245-54. (PMID: 21390033)
Ann Neurol. 2019 Aug;86(2):215-224. (PMID: 31168802)
Nat Med. 2008 Aug;14(8):837-42. (PMID: 18568035)
Nat Commun. 2016 Feb 19;7:10759. (PMID: 26892305)
BioDrugs. 2020 Feb;34(1):11-26. (PMID: 31686399)
Lancet. 2021 Apr 24;397(10284):1577-1590. (PMID: 33667416)
Nat Rev Mol Cell Biol. 2007 Feb;8(2):101-12. (PMID: 17245412)
Nat Rev Drug Discov. 2008 Jan;7(1):21-39. (PMID: 18097458)
Nature. 2021 Aug;596(7873):583-589. (PMID: 34265844)
Alzheimers Res Ther. 2024 Jan 18;16(1):13. (PMID: 38238842)
Nat Struct Mol Biol. 2020 Dec;27(12):1125-1133. (PMID: 32989305)
N Engl J Med. 2023 Jan 5;388(1):9-21. (PMID: 36449413)
Int J Nanomedicine. 2023 Jan 19;18:353-367. (PMID: 36700149)
Annu Rev Immunol. 1994;12:433-55. (PMID: 8011287)
Bioinformatics. 2023 Jul 1;39(7):. (PMID: 37405868)
Science. 2003 Apr 18;300(5618):486-9. (PMID: 12702875)
Alzheimers Dement (N Y). 2024 Apr 24;10(2):e12465. (PMID: 38659717)
Nat Chem. 2020 May;12(5):445-451. (PMID: 32284577)
Sci Transl Med. 2022 May 25;14(646):eabn1252. (PMID: 35412328)
Mol Neurodegener. 2024 Feb 20;19(1):20. (PMID: 38378578)
Proc Natl Acad Sci U S A. 2005 Feb 15;102(7):2273-6. (PMID: 15695586)
Grant Information: 10059436 UK Research and Innovation; 10061100 UK Research and Innovation
Contributed Indexing: Keywords: Alzheimer’s disease; Aβ42 oligomers; avidity; multivalency; nanobodies; protein aggregation
Substance Nomenclature: 0 (Amyloid beta-Peptides)
0 (Peptide Fragments)
0 (amyloid beta-protein (1-42))
0 (Single-Domain Antibodies)
Entry Date(s): Date Created: 20260819 Date Completed: 20260819 Latest Revision: 20260926
Update Code: 20260926
PubMed Central ID: PMC13488367
DOI: 10.1002/pro.70754
PMID: 42615560
Βάση Δεδομένων: MEDLINE
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  Data: Multimerization of a rationally designed nanobody for enhanced avidity toward Aβ42 oligomers.
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  Data: <searchLink fieldCode="AU" term="%22Nowinska+M%22">Nowinska M</searchLink>; Centre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Cambridge, UK.<br /><searchLink fieldCode="AU" term="%22Suh+E%22">Suh E</searchLink>; Centre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Cambridge, UK.<br /><searchLink fieldCode="AU" term="%22Mogilevsky+C%22">Mogilevsky C</searchLink>; Centre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Cambridge, UK.<br /><searchLink fieldCode="AU" term="%22Vendruscolo+M%22">Vendruscolo M</searchLink>; Centre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Cambridge, UK.
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– Name: Abstract
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  Data: Alzheimer's disease affects tens of millions of people worldwide and is associated with the self-assembly of the Aβ42 peptide into amyloid aggregates. Among the species formed during this process, soluble oligomeric intermediates are the most closely linked to neurotoxicity and are therefore an attractive target for both therapeutic and diagnostic strategies. Their conformational heterogeneity and transient nature, however, have so far hindered the development of reagents that recognize them selectively, and no fully quantitative biomarker of Aβ42 oligomers is widely available. To address this problem, we use a rationally designed conformation-specific single-domain antibody, DesAbO, which binds selectively to Aβ42 oligomers. By using enzyme-linked immunosorbent assay, we show that encoding self-assembling multimerization domains in the DesAbO plasmid yields multimeric variants with increased avidity toward Aβ42 oligomers. In aggregation assays, the multimeric variants inhibited Aβ42 aggregation at concentrations at which the monomeric form was no longer effective, with the SB175 trimer performing best. These results show how multimerization can be used to enhance the recognition of Aβ42 oligomers and offer a route toward diagnostic and therapeutic agents for Alzheimer's disease and other protein misfolding disorders.<br /> (© 2026 The Author(s). Protein Science published by Wiley Periodicals LLC on behalf of The Protein Society.)
– Name: Ref
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  Group: RefInfo
  Data: Alzheimers Dement. 2018 Apr;14(4):535-562. (PMID: <searchLink fieldCode="PM" term="%2229653606%22">29653606)</searchLink><br />Protein Sci. 2026 Sep;35(9):e70754. (PMID: <searchLink fieldCode="PM" term="%2242615560%22">42615560)</searchLink><br />JAMA. 2023 Aug 8;330(6):512-527. (PMID: <searchLink fieldCode="PM" term="%2237459141%22">37459141)</searchLink><br />Mol Psychiatry. 2021 Oct;26(10):5481-5503. (PMID: <searchLink fieldCode="PM" term="%2234456336%22">34456336)</searchLink><br />Mol Cell Neurosci. 2024 Sep;130:103949. (PMID: <searchLink fieldCode="PM" term="%2238906341%22">38906341)</searchLink><br />PLoS Pathog. 2025 Dec 8;21(12):e1013744. (PMID: <searchLink fieldCode="PM" term="%2241359663%22">41359663)</searchLink><br />Cell. 2019 Oct 3;179(2):312-339. (PMID: <searchLink fieldCode="PM" term="%2231564456%22">31564456)</searchLink><br />Commun Biol. 2026 Mar 27;9(1):. (PMID: <searchLink fieldCode="PM" term="%2241896453%22">41896453)</searchLink><br />Proc Natl Acad Sci U S A. 2013 Jun 11;110(24):9758-63. (PMID: <searchLink fieldCode="PM" term="%2223703910%22">23703910)</searchLink><br />Nat Rev Chem. 2021 Apr;5(4):277-294. (PMID: <searchLink fieldCode="PM" term="%2237117282%22">37117282)</searchLink><br />BioDrugs. 2024 Jan;38(1):5-22. (PMID: <searchLink fieldCode="PM" term="%2237955845%22">37955845)</searchLink><br />Nat Biotechnol. 2017 Nov;35(11):1026-1028. (PMID: <searchLink fieldCode="PM" term="%2229035372%22">29035372)</searchLink><br />Bioconjug Chem. 2022 Aug 17;33(8):1494-1504. (PMID: <searchLink fieldCode="PM" term="%2235875886%22">35875886)</searchLink><br />N Engl J Med. 2021 May 6;384(18):1691-1704. (PMID: <searchLink fieldCode="PM" term="%2233720637%22">33720637)</searchLink><br />Methods Mol Biol. 2020;2141:731-754. (PMID: <searchLink fieldCode="PM" term="%2232696387%22">32696387)</searchLink><br />Nat Rev Dis Primers. 2021 May 13;7(1):33. (PMID: <searchLink fieldCode="PM" term="%2233986301%22">33986301)</searchLink><br />Nat Methods. 2022 Jun;19(6):679-682. (PMID: <searchLink fieldCode="PM" term="%2235637307%22">35637307)</searchLink><br />Proc Natl Acad Sci U S A. 2020 Jun 16;117(24):13509-13518. (PMID: <searchLink fieldCode="PM" term="%2232493749%22">32493749)</searchLink><br />Nature. 2016 Aug 31;537(7618):50-6. (PMID: <searchLink fieldCode="PM" term="%2227582220%22">27582220)</searchLink><br />Nat Neurosci. 2012 Jan 29;15(3):349-57. (PMID: <searchLink fieldCode="PM" term="%2222286176%22">22286176)</searchLink><br />Science. 2002 Jul 19;297(5580):353-6. (PMID: <searchLink fieldCode="PM" term="%2212130773%22">12130773)</searchLink><br />Nat Biotechnol. 2011 Mar;29(3):245-54. (PMID: <searchLink fieldCode="PM" term="%2221390033%22">21390033)</searchLink><br />Ann Neurol. 2019 Aug;86(2):215-224. (PMID: <searchLink fieldCode="PM" term="%2231168802%22">31168802)</searchLink><br />Nat Med. 2008 Aug;14(8):837-42. (PMID: <searchLink fieldCode="PM" term="%2218568035%22">18568035)</searchLink><br />Nat Commun. 2016 Feb 19;7:10759. (PMID: <searchLink fieldCode="PM" term="%2226892305%22">26892305)</searchLink><br />BioDrugs. 2020 Feb;34(1):11-26. (PMID: <searchLink fieldCode="PM" term="%2231686399%22">31686399)</searchLink><br />Lancet. 2021 Apr 24;397(10284):1577-1590. (PMID: <searchLink fieldCode="PM" term="%2233667416%22">33667416)</searchLink><br />Nat Rev Mol Cell Biol. 2007 Feb;8(2):101-12. (PMID: <searchLink fieldCode="PM" term="%2217245412%22">17245412)</searchLink><br />Nat Rev Drug Discov. 2008 Jan;7(1):21-39. (PMID: <searchLink fieldCode="PM" term="%2218097458%22">18097458)</searchLink><br />Nature. 2021 Aug;596(7873):583-589. (PMID: <searchLink fieldCode="PM" term="%2234265844%22">34265844)</searchLink><br />Alzheimers Res Ther. 2024 Jan 18;16(1):13. (PMID: <searchLink fieldCode="PM" term="%2238238842%22">38238842)</searchLink><br />Nat Struct Mol Biol. 2020 Dec;27(12):1125-1133. (PMID: <searchLink fieldCode="PM" term="%2232989305%22">32989305)</searchLink><br />N Engl J Med. 2023 Jan 5;388(1):9-21. (PMID: <searchLink fieldCode="PM" term="%2236449413%22">36449413)</searchLink><br />Int J Nanomedicine. 2023 Jan 19;18:353-367. (PMID: <searchLink fieldCode="PM" term="%2236700149%22">36700149)</searchLink><br />Annu Rev Immunol. 1994;12:433-55. (PMID: <searchLink fieldCode="PM" term="%228011287%22">8011287)</searchLink><br />Bioinformatics. 2023 Jul 1;39(7):. (PMID: <searchLink fieldCode="PM" term="%2237405868%22">37405868)</searchLink><br />Science. 2003 Apr 18;300(5618):486-9. (PMID: <searchLink fieldCode="PM" term="%2212702875%22">12702875)</searchLink><br />Alzheimers Dement (N Y). 2024 Apr 24;10(2):e12465. (PMID: <searchLink fieldCode="PM" term="%2238659717%22">38659717)</searchLink><br />Nat Chem. 2020 May;12(5):445-451. (PMID: <searchLink fieldCode="PM" term="%2232284577%22">32284577)</searchLink><br />Sci Transl Med. 2022 May 25;14(646):eabn1252. (PMID: <searchLink fieldCode="PM" term="%2235412328%22">35412328)</searchLink><br />Mol Neurodegener. 2024 Feb 20;19(1):20. (PMID: <searchLink fieldCode="PM" term="%2238378578%22">38378578)</searchLink><br />Proc Natl Acad Sci U S A. 2005 Feb 15;102(7):2273-6. (PMID: <searchLink fieldCode="PM" term="%2215695586%22">15695586)</searchLink>
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  Data: <i>Keywords: </i>Alzheimer’s disease; Aβ42 oligomers; avidity; multivalency; nanobodies; protein aggregation
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