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Aβ40 Oligomers Identified as a Potential Biomarker for the Diagnosis of Alzheimer's Disease
Open accessAbstract
Alzheimer's Disease (AD) is the most prevalent form of dementia worldwide, yet the development of therapeutics has been hampered by the absence of suitable biomarkers to diagnose the disease in its early stages prior to the formation of amyloid plaques and the occurrence of irreversible neuronal damage. Since oligomeric Aβ species have been implicated in the pathophysiology of AD, we reasoned that they may correlate with the onset of disease. As such, we have developed a novel misfolded protein assay for the detection of soluble oligomers composed of Aβ x-40 and x-42 peptide (hereafter Aβ40 and Aβ42) from cerebrospinal fluid (CSF). Preliminary validation of this assay with 36 clinical samples demonstrated the presence of aggregated Aβ40 in the CSF of AD patients. Together with measurements of total Aβ42, diagnostic sensitivity and specificity greater than 95% and 90%, respectively, were achieved. Although larger sample populations will be needed to confirm this diagnostic sensitivity, our studies demonstrate a sensitive method of detecting circulating Aβ40 oligomers from AD CSF and suggest that these oligomers could be a powerful new biomarker for the early detection of AD.
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“These assays, which can be many orders of magnitude more sensitive than ELISAs, have established an AD-dependent accumulation of oligomers in human CSF (Fukumoto et al., 2010; Gao et al., 2010; Georganopoulou et al., 2005; Haes et al., 2005).”
From The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer’s disease (2011) · cites this paper as Gao et al., 2010
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1 retracted
RETRACTED ARTICLE: A specific amyloid-β protein assembly in the brain impairs memory
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“and the criteria of probable AD defined by NINCDS-ADRDA”
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“It is the most prevalent form of dementia, estimated to affect 13 million people worldwide [1].”
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Haass, C., & Selkoe, D. J. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2101 · Cited by 4,744 · cited 1×
“Its chemical composition is also poorly defined, although several lines of evidence suggest that AD-associated oligomers are primarily composed of Ab42 [3].”
BackgroundCommon structure of soluble amyloid oligomers implies common mechanism of pathogenesis
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“As amyloid aggregates are characterized by similar cross-beta sheet structure, they share conformational epitopes that are recognized by amyloid-binding molecules such as Congo Red and thioflavin T [15,16] as well as conformation-specific antibodies [17,18].”
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“While the precise conformation of in vivo oligomers is unknown, several lines of evidence suggest that aggregated proteins share a number of structural properties. For instance, amyloid fibrils composed of different proteins have similar cross beta sheet structure, allowing binding and detection by a number of compoun…”
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“interpretation of these results is that aggregation of the less soluble Ab42 would precede and recruit subsequent aggregation of Ab40, as has been previously suggested [12,35].”
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“In addition, Ab42 appears to be more amyloidogenic than Ab40 and is found more frequently in plaques despite existing at much lower physiological concentrations [13].”
Background
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The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer’s disease
Ferreira, S. T., & Klein, W. L. (2011) · Neurobiology of Learning and Memory · doi:10.1016/j.nlm.2011.08.003 · Cited by 442
Olivares, D., K. Deshpande, V., Shi, Y., K. Lahiri, D., H. Greig, N., T. Rogers, J., & Huang, X. (2012) · Current Alzheimer Research · doi:10.2174/156720512801322564 · Cited by 407
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Morales, R., Moreno‐González, I., & Soto, C. A. (2013) · PLoS Pathogens · doi:10.1371/journal.ppat.1003537 · Cited by 225
“Although the presence of misfolded aggregates at different organs throughout the body complicates the possibility of a crossseeding in this specific case, it is important to highlight that there is evidence for soluble oligomers circulating in biological fluids [28,29].”
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Rosén, C., Hansson, O., Blennow, K., & Zetterberg, H. (2013) · Molecular Neurodegeneration · doi:10.1186/1750-1326-8-20 · Cited by 221
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“A few reports of the detection of apparent Ab oligomers in CSF and plasma have appeared (Fukumoto et al., 2010; Gao et al., 2010; Klyubin et al., 2008; Villemagne et al., 2010); however, the interpretation of these reports has been clouded by failure to define the precise oligomeric unit the assays are detecting, an i…”
Detection of Misfolded Aβ Oligomers for Sensitive Biochemical Diagnosis of Alzheimer’s Disease
Salvadores, N., Shahnawaz, M., Scarpini, E. A., Tagliavini, F., & Soto, C. A. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.02.031 · Cited by 205
“Recent studies have shown that Ab oligomers are naturally secreted by cells and circulate in AD biological fluids (Gao et al., 2010; Head et al., 2010; Walsh et al., 2002; Klyubin et al., 2008; Georganopoulou et al., 2005; Fukumoto et al., 2010).”
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“Soluble Aβ oligomers have been isolated from extracts of postmortem AD brain tissue and from transgenic AD animal models [37,52,117-119] and have been reported to be elevated in human AD brain relative to non-demented older patients [59,61,62,65,119-124].”
BackgroundA Sensitive Aβ Oligomer Assay Discriminates Alzheimer's and Aged Control Cerebrospinal Fluid
Savage, M. J., Kalinina, J., Wolfe, A. L., Tugusheva, K., Korn, R., Cash-Mason, T., Maxwell, J. W., Hatcher, N. G., Haugabook, S. J., Wu, G., et al. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.1675-13.2014 · Cited by 187
“It is notable that oligomers consistently increase in AD (Pitschke et al., 1998; Georganopoulou et al., 2005; Fukumoto et al., 2010; Gao et al., 2010; Sancesario et al., 2012; Santos et al., 2012; Hölttä et al., 2013; Herskovits et al., 2013), unlike A 42 monomer (Jack et al., 2010).”
BackgroundInfluentialAmyloid β oligomers (AβOs) in Alzheimer’s disease
Mroczko, B., Groblewska, M., Litman‐Zawadzka, A., Kornhuber, J., & Lewczuk, P. (2017) · Journal of Neural Transmission · doi:10.1007/s00702-017-1820-x · Cited by 150
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“compared the diagnostic potential of the Aβ40 oligomer to that of the Aβ42 monomer and found Aβ42 monomers to be superior (63).”
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“Although Ab42 is more toxic than Ab40, Ab40 is the predominant form of Ab, accounting for > 90% of total Ab (Donmez et al., 2010; Gao et al., 2010; Kuperstein et al., 2010; Seppala et al., 2010; Rabe et al., 2011; Sato et al., 2012).”
BackgroundPreoperative cerebrospinal fluid β‐Amyloid/Tau ratio and postoperative delirium
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Amyloid cross-seeding raises new dimensions to understanding of amyloidogenesis mechanism
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“…such as fluorescence correlation spectroscopy (Pitschke et al., 1998), biobarcode assay (Georganopoulou et al., 2005), misfolded protein assay (Gao et al., 2010), ELISA with the same monoclonal antibody both for capture and detection (Fukumoto et al., 2010), flow cytometry based assays…”
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“These peptides have been localized in amyloid plaques and can form oligomers and protofibrils, although Aβ42 is more hydrophobic and fibrillogenic (Selkoe, 2001).”
BackgroundInfluentialCSF Biomarkers for Amyloid and Tau Pathology in Alzheimer's Disease
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“Additionally, the application of a Misfolded Protein Assay (MPA) for the detection of soluble oligomers allows specific detection of Ab40 and Ab42 oligomers in the CSF; this is important as Ab40 but not Ab42 oligomers are increased in the CSF in AD patients (Gao et al., 2010).”
BackgroundProtein misfolding cyclic amplification (PMCA): Current status and future directions
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“Interestingly, similar results were not found for A 42 aggregates [33].”
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“…value of Aβ oligomers for early diagnosis and as a possible surrogate biomarker in clinical trials (Sian et al., 2000; Austen et al., 2008; Gao et al., 2010; Yam et al., 2011; Herskovits et al., 2013; Lesne et al., 2013), Aβ has yet to be validated as a clinically acceptedmarker for AD…”
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Correlation of Aβ oligomer levels in matched cerebrospinal fluid and serum samples
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“Interestingly, in CSF samples of 26 AD patients, higher amounts of Aβ1-40 aggregates could be detected than in the samples of 10 agematched controls [29].”
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“Novel assays of misfolded protein for the detection of soluble Aβ1–40 and Aβ1–42 oligomers in CSF have shown promise in terms of greater accuracy in differentiating patients with MCI and AD from normal controls, as compared with the usual methods based on fibrillar forms of the peptide [15,78].”
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How many biomarkers to discriminate neurodegenerative dementia?
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Cerebrospinal fluid biomarkers of Alzheimer’s disease
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“Nevertheless Gao and coworkers, using a novel misfolded protein assay, found an enrichment of Aβ40containing oligomers in AD CSF [78] and suggested these assemblies as biomarker for early diagnosis of AD.”
BackgroundField amplified sample stacking of amyloid beta (1-42) oligomers using capillary electrophoresis
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“Furthermore, in the case of the clinical trial, the levels of AβO in AD patients were also found to be significantly higher than in healthy individuals [7, 8].”
BackgroundNew developments and concepts related to biomarker application to vaccines
Ahmed, S., BLACK, S. B., & Ulmer, J. B. (2011) · Microbial Biotechnology · doi:10.1111/j.1751-7915.2011.00277.x · Cited by 9
“In Alzheimer’s disease, a potential biomarker (Ab40) has been discovered that may facilitate earlier diagnosis of Alzheimer’s disease (Gao et al., 2010).”
BackgroundChallenges in understanding the structure/activity relationship of Aβ oligomers
Pilkington, A. W., & Legleiter, J. A. (2019) · AIMS Biophysics · doi:10.3934/biophy.2019.1.1 · Cited by 7
Multivalent foldamer-based affinity assay for selective recognition of Aβ oligomers
Olajos, G., Bartus, É., Schuster, I., Lautner, G., Gyurcsányi, R. E., Szögi, T., Fülöp, L., & Martinek, T. A. (2017) · Analytica Chimica Acta · doi:10.1016/j.aca.2017.01.013 · Cited by 7
Direct and selective nanosensor for amyloid-β oligomers in serum for Alzheimer's disease diagnosis
Song, Q., Zhang, H., Lan, Y., Kong, J., Wong, M. S., & Li, H. (2025) · RSC Advances · doi:10.1039/d5ra01020a · Cited by 6
Clinical significance of plasma candidate biomarkers of Alzheimer’s Disease
Lewczuk, P., Łukaszewicz‐Zając, M., Kornhuber, J., & Mroczko, B. (2024) · Neurologia i Neurochirurgia Polska · doi:10.5603/pjnns.100675 · Cited by 7
Protein Misfolding in Neurodegenerative Diseases: The Key Pending Questions
Soto, C. A., & Mitchell, C. (2013) · Cited by 6
Interactions between gold nanoparticles and amyloid β 25–35 peptide
Peng, J., Weng, J., Ren, L., & Sun, L. (2014) · IET Nanobiotechnology · doi:10.1049/iet-nbt.2013.0071 · Cited by 6
Peptoid self-assembly and opportunities for creating protein-mimetic biomaterials and biointerfaces
yaagoubi, M. E., Tewari, K. M., & Lau, K. H. A. (2018) · Elsevier eBooks · doi:10.1016/b978-0-08-102015-9.00006-x · Cited by 5
Webb, S. J. N., Chitta, S., Magden, E. R., & Simmons, J. H. (2025) · PLoS ONE · doi:10.1371/journal.pone.0318173 · Cited by 4
Biomarkers of Alzheimer’s Disease
Saeed, U., Swardfager, W., Black, S. E., & Masellis, M. (2017) · Mental health and illness worldwide · doi:10.1007/978-981-10-2414-6_8 · Cited by 4
Neuropathological Basis of Alzheimer’s Disease and Alzheimer’s Disease Diagnosis
Schneider, J. A., Montine, T. J., Sperling, R. A., & Bennett, D. A. (2012) · Advances in biological psychiatry · doi:10.1159/000335384 · Cited by 4
Amyloid-β in the Cerebrospinal Fluid of APP Transgenic Mice Does not Show Prion-like Properties
Skachokova, Z. K., Sprenger, F., Breu, K., Abramowski, D., Clavaguera, F., Hench, J., Staufenbiel, M., Tolnay, M., & Winkler, D. T. (2015) · Current Alzheimer Research · doi:10.2174/1567205012666150710115022 · Cited by 4
Alzheimer’s Disease and Other Neurodegenerative Disorders
Rosén, C., Zetterberg, H., & Blennow, K. (2015) · Springer eBooks · doi:10.1007/978-3-319-01225-4_20 · Cited by 2
Fluid Biomarkers in Alzheimer’s Disease and Frontotemporal Dementia
Mattsson, N., Grigoriou, S., & Zetterberg, H. (2018) · Springer eBooks · doi:10.1007/978-3-319-72938-1_11 · Cited by 2
In vitro screening on amyloid beta modulation of aqueous extracts from plant seeds
Okada, Y., & Okada, M. (2015) · Journal of Pharmacy And Bioallied Sciences · doi:10.4103/0975-7406.171688 · Cited by 2
“Yield was expressed as a gram of dry matter/mL. Yield was in the range of 0.137–0.246 g/mL. TPC was expressed as mg of chlorogenic acid equiv/g of dry matter [Table 1].”
InfluentialArtificial DnaJ Protein for protein production and conformational diseases
Hishiya, A., & Koya, K. (2017) · Scientific Reports · doi:10.1038/s41598-017-09067-7 · Cited by 2
Neuroimaging and molecular biomarkers of dementia
Polyakova, T., & Араблинский, А. В. (2017) · S S Korsakov Journal of Neurology and Psychiatry · doi:10.17116/jnevro20171176216-22 · Cited by 1
Bioinspired Polymers for Regenerative Medicine
Khajehmohammadi, M., Tolabi, H., Kabbani, L., & Ashammakhi, N. A. (2025) · Springer eBooks · doi:10.1007/978-3-031-87744-5_2 · Cited by 1
Sancesario, G. (2012) · Journal of Molecular Biomarkers & Diagnosis · doi:10.4172/2155-9929.1000e107 · Cited by 1
“[7] developed a complex method using a synthetic ligand, the Aggregate Specific Reagent 1 (ASR1) that preferentially binds aggregated proteins over monomeric proteins.”
MethodAdvances in Alzheimer’s Disease Management
Gauthier, S. G., & Rosa‐Neto, P. (2012) · doi:10.2217/9781780840840 · Cited by 1
Sahoo, S., Balireddygari, L. R., Padhy, A. A., Kumari, S., Hegde, P., & Mishra, P. (2024) · Elsevier eBooks · doi:10.1016/b978-0-443-21809-5.00003-x · Cited by 1
Martone, R. L., Snyder, R. H., Xu, A. S. L., & Reams, R. Y. (2012) · Current Translational Geriatrics and Experimental Gerontology Reports · doi:10.1007/s13670-012-0015-4
“ent platforms have been developed to interrogate the ability of a test therapeutic compound to cause ostensibly therapeutic reductions in Aβ or Aβ oligomers [35, 36].”
BackgroundSPECIFIC AMYLOID-BETA OLIGOMERS IN HUMAN CEREBROSPINAL FLUID
Handoko, M. (2012) · University of Minnesota Digital Conservancy (University of Minnesota)
New Frontiers in Alzheimer's Disease Diagnosis
Llorens, F., Nuhn, S., Peter, C., Zerr, I., & Stoeck, K. (2015) · InTech eBooks · doi:10.5772/59652 · Cited by 1
Fluid biomarkers in Alzheimer's disease - current
Rosén, C., Hansson, O., Blennow, K., & Zetterberg, H. (2013)
Fluid Biomarkers and Diagnostics
Zetterberg, H., & Blennow, K. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-802173-6.00021-6
Biomarkers of Alzheimer’s Disease
Saeed, U., Swardfager, W., Black, S. E., & Masellis, M. (2017) · Mental health and illness worldwide · doi:10.1007/978-981-10-0370-7_8-1
Metadata
- Authors
- Gao, C. M., Yam, A. Y., Wang, X., Magdangal, E., Salisbury, C., Peretz, D., Zuckermann, R. N., Connolly, M. D., Hansson, O., Minthon, L., Zetterberg, H., Blennow, K., Fedynyshyn, J. P., & Allauzen, S.
- Affiliations
- Lund University (SE)
- Sahlgrenska University Hospital (SE)
- Corresponding author
- Fedynyshyn, Joseph P.
- ORCID
- Venue
- PLoS ONE
- Publisher
- Public Library of Science (PLoS)
- Published
- 2010-12-30
- Volume
- 5
- Issue
- 12
- Pages
- e15725
- ISSN
- 1932-6203 (ISSN-L)
- PMC
- PMC3012719
- OpenAlex
- W2135057867
- Cited by
- 105
- References
- 39
- Citations by year
- 2026: 2 · 2025: 3 · 2024: 2 · 2023: 1 · 2022: 3 · 2021: 2 · 2020: 2 · 2019: 8 · 2018: 4 · 2017: 11 · 2016: 9 · 2015: 10 · 2014: 17 · 2013: 13 · 2012: 12
- FWCI
- 6.72
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- PLoS ONE (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- UCL Discovery (University College London) (submittedVersion)
- Lund University Publications (Lund University) (submittedVersion, other-oa)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- Alzheimer's disease, Aβ40, amyloid-beta 42, cerebrospinal fluid biomarkers, early diagnosis, amyloid plaques, sensitivity and specificity
- MeSH terms
- Aged, Alzheimer Disease, Epitopes, Brain, Enzyme-Linked Immunosorbent Assay, Gene Expression Regulation, Humans, Middle Aged, Models, Chemical, Molecular Conformation, Peptide Fragments, Peptides, Protein Conformation, Sensitivity and Specificity, Biomarkers, Amyloid beta-Peptides
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