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Alpha 1-antichymotrypsin binding to Alzheimer A beta peptides is sequence specific and induces fibril disaggregation in vitro
Fraser PE, Nguyen JT, McLachlan DR, Abraham CR, Kirschner DA.. Journal of neurochemistry, 1993-07-01
Topic: Brain proteins, microglia and lab models
The serine protease inhibitor alpha 1-antichymotrypsin (ACT) consistently colocalizes with amyloid deposits of Alzheimer's disease (AD) and may contribute to the generation of amyloid proteins and/or physically affect fibril assembly. AD amyloid fibrils are composed primarily of A beta, which is a proteolytic fragment of the larger beta-amyloid precursor protein. Using negative-stain and immunochemical electron microscopy, we have investigated the binding of ACT to the fibrils formed by four synthetic A beta analogues corresponding to the wild-type human 1-40 sequence [Hwt(1-40)], a 1-40 peptide [HDu(1-40)] containing the Glu22-->Gln mutation found in hereditary cerebral hemorrhage with amyloidosis of the Dutch type, the N-terminal 1-28 residues [beta(1-28)], and an internal fragment of A beta containing residues 11-28 [beta(11-28)].
Cite this study APA, Vancouver, BibTeX · download .bib or .ris
APA 7th
Fraser, P. E., Nguyen, J. T., McLachlan, D. R., Abraham, C. R., & Kirschner, D. A. (1993). Alpha 1-antichymotrypsin binding to Alzheimer A beta peptides is sequence specific and induces fibril disaggregation in vitro. Journal of neurochemistry. https://doi.org/10.1111/j.1471-4159.1993.tb03568.x
Vancouver
Fraser PE, Nguyen JT, McLachlan DR, Abraham CR, Kirschner DA. Alpha 1-antichymotrypsin binding to Alzheimer A beta peptides is sequence specific and induces fibril disaggregation in vitro. Journal of neurochemistry. 1993. doi:10.1111/j.1471-4159.1993.tb03568.x. PMID: 8515277.
BibTeX
@article{fraser1993-8515277,
author = {Fraser, P. E. and Nguyen, J. T. and McLachlan, D. R. and Abraham, C. R. and Kirschner, D. A.},
title = {{Alpha 1-antichymotrypsin binding to Alzheimer A beta peptides is sequence specific and induces fibril disaggregation in vitro}},
journal = {Journal of neurochemistry},
year = {1993},
doi = {10.1111/j.1471-4159.1993.tb03568.x},
pmid = {8515277},
url = {https://doi.org/10.1111/j.1471-4159.1993.tb03568.x}
}
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Key findings
- AD amyloid fibrils are composed primarily of A beta, which is a proteolytic fragment of the larger beta-amyloid precursor protein.
- Using negative-stain and immunochemical electron microscopy, we have investigated the binding of ACT to the fibrils formed by four synthetic A beta analogues corresponding to the wild-type human 1-40 sequence [Hwt(1-40)], a 1-40 peptide [HDu(1-40)] containing the Glu22-->Gln mutation found in hereditary cerebral hemorrhage with amyloidosis of the Dutch type, the N-terminal 1-28 residues [beta(1-28)], and an internal fragment of A beta containing residues 11-28 [beta(11-28)].
- Each of these peptide analogues assembled into 70-90-A-diameter fibrils resembling native amyloid and, except for beta(11-28), bound ACT, as indicated by the appearance of 80-100-A globular particles that adhered to preformed fibrils and that could be decorated with anti-ACT antibodies.
- Under the conditions used, ACT binding destabilized the in vitro fibrils and produced a gradual dissolution of the macromolecular assemblies into constituent filaments and shorter fragments.
Why it matters
In laboratory experiments, alpha 1-antichymotrypsin bound to synthetic amyloid-beta peptides and caused fibril disaggregation in vitro. This is a test-tube study and does not show any treatment, cure, or prevention for Alzheimer's disease in people.
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Study details
- Evidence strengthLow
How this study scored 43/100
Published in a peer-reviewed journal. Scored zero for study design, sample size, effect reported and randomised / blinded because the record does not state it.
| Component | Points | Why |
|---|---|---|
| Journal tier | 7 / 10 | Tier 3 — peer-reviewed journal (Journal of neurochemistry) |
| Journal's citation record | 3 / 4 | Journal of Neurochemistry: journal h-index 349 (OpenAlex, 2026-10-29) |
| Study design | 0 / 12 | No study design recorded — scores zero, not guessed (not stated in the record — scored 0) |
| Strength of evidence | 1 / 5 | Rated “low” in our summary |
| Peer-review validation | 10 / 10 | Peer-reviewed. Published as an article in a named peer-reviewed journal. |
| How recent | 1 / 5 | 1993 — older than 20 years, still counted |
| Sample size | 0 / 4 | Participant count not stated — scores zero (not stated in the record — scored 0) |
| Effect reported | 0 / 3 | No effect size reported — scores zero (not stated in the record — scored 0) |
| Studied in people | 0 / 3 | Laboratory or animal study (title names “in vitro”) — scores zero |
| Randomised / blinded | 0 / 2 | No randomisation or blinding stated — scores zero (not stated in the record — scored 0) |
| Times cited | 5 / 7 | Cited 139 times (OpenAlex, 2026-10-10) |
| Citations per year | 2 / 5 | 4.0 citations a year over 35 year(s) since 1993 |
| Impact for its field and year | 3 / 6 | Cited 6.2× the average for papers of its field and year (OpenAlex FWCI) |
| Cited by studies here | 2 / 6 | Cited by 4 other studies in this library |
| Still being cited | 0 / 4 | Cited 1 times in 2024–2026 (2026 still in progress; OpenAlex) |
| Senior author's track record | 3 / 4 | Last-listed author Daniel A. Kirschner: h-index 54 (OpenAlex, whole career) |
| Institution's track record | 3 / 3 | Harvard University: institution h-index 3,235 (OpenAlex) |
| Multi-centre collaboration | 1 / 3 | OpenAlex lists 3 institution(s) in 2 countries |
| Indexed in PubMed | 2 / 2 | Indexed in PubMed (PMID 8515277) |
| Free to read | 0 / 2 | Behind a paywall — scores zero |
| Total | 43 / 100 | — |
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