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Multi-target-directed coumarin derivatives: hAChE and BACE1 inhibitors as potential anti-Alzheimer compounds
Piazzi L, Cavalli A, Colizzi F, Belluti F, Bartolini M, Mancini F, Recanatini M, Andrisano V et al.. Bioorganic & medicinal chemistry letters, 2007-10-04
Topic: Amyloid, tau and blood-test diagnosis
The complex etiology of Alzheimer's disease (AD) prompts scientists to develop multifunctional compounds to combat causes and symptoms of such neurodegeneration. To this aim we designed, synthesized, and tested a series of compounds by introducing halophenylalkylamidic functions on the scaffold of AP2238, which is a dual binding site acetylcholinesterase inhibitor. The inhibitory activity was successfully extended to the beta-site amyloid precursor protein cleavage enzyme, leading to the discovery of a potent inhibitor of this enzyme (3) and affording multifunctional compounds (2, 6, 8) for the treatment of AD.
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APA 7th
Piazzi, L., Cavalli, A., Colizzi, F., Belluti, F., Bartolini, M., Mancini, F., et al. (2008). Multi-target-directed coumarin derivatives: hAChE and BACE1 inhibitors as potential anti-Alzheimer compounds. Bioorganic & medicinal chemistry letters. https://doi.org/10.1016/j.bmcl.2007.09.100
Vancouver
Piazzi L, Cavalli A, Colizzi F, Belluti F, Bartolini M, Mancini F, et al. Multi-target-directed coumarin derivatives: hAChE and BACE1 inhibitors as potential anti-Alzheimer compounds. Bioorganic & medicinal chemistry letters. 2008. doi:10.1016/j.bmcl.2007.09.100. PMID: 17998161.
BibTeX
@article{piazzi2008-17998161,
author = {Piazzi, L. and Cavalli, A. and Colizzi, F. and Belluti, F. and Bartolini, M. and Mancini, F. and Recanatini, M. and Andrisano, V. and others},
title = {{Multi-target-directed coumarin derivatives: hAChE and BACE1 inhibitors as potential anti-Alzheimer compounds}},
journal = {Bioorganic \& medicinal chemistry letters},
year = {2008},
doi = {10.1016/j.bmcl.2007.09.100},
pmid = {17998161},
url = {https://doi.org/10.1016/j.bmcl.2007.09.100}
}
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Key findings
- To this aim we designed, synthesized, and tested a series of compounds by introducing halophenylalkylamidic functions on the scaffold of AP2238, which is a dual binding site acetylcholinesterase inhibitor.
- The inhibitory activity was successfully extended to the beta-site amyloid precursor protein cleavage enzyme, leading to the discovery of a potent inhibitor of this enzyme (3) and affording multifunctional compounds (2, 6, 8) for the treatment of AD.
Why it matters
Researchers designed and tested coumarin compounds that inhibit both acetylcholinesterase and the beta-site amyloid precursor protein cleavage enzyme (BACE1) in the laboratory. These are early chemical findings and no treatment, cure or prevention in people is reported.
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Study details
- Evidence strengthLow
How this study scored 40/100
Published in a peer-reviewed journal. Scored zero for study design, sample size, effect reported, studied in people and randomised / blinded because the record does not state it.
| Component | Points | Why |
|---|---|---|
| Journal tier | 7 / 10 | Tier 3 — peer-reviewed journal (Bioorganic & medicinal chemistry letters) |
| Journal's citation record | 2 / 4 | Bioorganic & Medicinal Chemistry Letters: journal h-index 181 (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 | 2008 — within 20 year(s) of the newest study here |
| 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 | Not stated whether this was studied in people — scores zero (not stated in the record — scored 0) |
| Randomised / blinded | 0 / 2 | No randomisation or blinding stated — scores zero (not stated in the record — scored 0) |
| Times cited | 5 / 7 | Cited 214 times (OpenAlex, 2026-10-10) |
| Citations per year | 3 / 5 | 10.7 citations a year over 20 year(s) since 2008 |
| Impact for its field and year | 3 / 6 | Cited 4.1× the average for papers of its field and year (OpenAlex FWCI) |
| Cited by studies here | 1 / 6 | Cited by 1 other studies in this library |
| Still being cited | 2 / 4 | Cited 15 times in 2024–2026 (2026 still in progress; OpenAlex) |
| Senior author's track record | 2 / 4 | Last-listed author Angela Rampa: h-index 36 (OpenAlex, whole career) |
| Institution's track record | 1 / 3 | University of Bologna: institution h-index 989 (OpenAlex) |
| Multi-centre collaboration | 0 / 3 | OpenAlex lists 1 institution(s) in 1 country — scores zero (affiliation lists can be incomplete) |
| Indexed in PubMed | 2 / 2 | Indexed in PubMed (PMID 17998161) |
| Free to read | 0 / 2 | Behind a paywall — scores zero |
| Total | 40 / 100 | — |
What each of these 20 components measures, and what this score is not →
Read the original
- DOI: 10.1016/j.bmcl.2007.09.100
- PubMed: 17998161
- Original source →
- Free full text: Zenodo (CERN European Organization for Nuclear Research) →
Full text: free to read — OpenAlex lists this copy as free to read: the link above (checked 6 Feb 1020).
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