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41/100

✓ Peer-reviewed alzhub usefulness score 41 out of 100. Genetics

Topic: Amyloid, tau and blood-test diagnosis

Targeting amyloid-β peptide (Aβ) within the brain is a strategy actively sought for therapy of Alzheimer's disease (AD). We investigated the ability of liposomes bi-functionalized with phosphatidic acid and with a modified ApoE-derived peptide (mApoE-PA-LIP) to affect Aβ aggregation/disaggregation features and to cross in vitro and in vivo the blood-brain barrier (BBB). Surface plasmon resonance showed that bi-functionalized liposomes strongly bind Aβ (kD=0.6 μM), while Thioflavin-T and SDS-PAGE/WB assays show that liposomes inhibit peptide aggregation (70% inhibition after 72 h) and trigger the disaggregation of preformed aggregates (60% decrease after 120 h incubation). Moreover, experiments with dually radiolabelled LIP suggest that bi-functionalization enhances the passage of radioactivity across the BBB either in vitro (permeability=2.5×10(-5) cm/min, 5-fold higher with respect to mono-functionalized liposomes) or in vivo in healthy mice. Taken together, our results suggest that mApoE-PA-LIP are valuable nanodevices with a potential applicability in vivo for the treatment of AD. From the clinical editor: Bi-functionalized liposomes with phosphatidic acid and a modified ApoE-derived peptide were demonstrated to influence Aβ aggregation/disaggregation as a potential treatment in an Alzheimer's model. The liposomes were able to cross the blood-brain barrier in vitro and in vivo. Similar liposomes may become clinically valuable nanodevices with a potential applicability for the treatment of Alzheimer's disease.

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APA 7th

Bana, L., Minniti, S., Salvati, E., Sesana, S., Zambelli, V., Cagnotto, A., et al. (2014). Liposomes bi-functionalized with phosphatidic acid and an ApoE-derived peptide affect Aβ aggregation features and cross the blood-brain-barrier: implications for therapy of Alzheimer disease. Nanomedicine : nanotechnology, biology, and medicine. https://doi.org/10.1016/j.nano.2013.12.001

Vancouver

Bana L, Minniti S, Salvati E, Sesana S, Zambelli V, Cagnotto A, et al. Liposomes bi-functionalized with phosphatidic acid and an ApoE-derived peptide affect Aβ aggregation features and cross the blood-brain-barrier: implications for therapy of Alzheimer disease. Nanomedicine : nanotechnology, biology, and medicine. 2014. doi:10.1016/j.nano.2013.12.001. PMID: 24333591.

BibTeX

@article{bana2014-24333591,
  author  = {Bana, L. and Minniti, S. and Salvati, E. and Sesana, S. and Zambelli, V. and Cagnotto, A. and Orlando, A. and Cazzaniga, E. and others},
  title   = {{Liposomes bi-functionalized with phosphatidic acid and an ApoE-derived peptide affect Aβ aggregation features and cross the blood-brain-barrier: implications for therapy of Alzheimer disease}},
  journal = {Nanomedicine : nanotechnology, biology, and medicine},
  year    = {2014},
  doi     = {10.1016/j.nano.2013.12.001},
  pmid    = {24333591},
  url     = {https://doi.org/10.1016/j.nano.2013.12.001}
}

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Key findings

Surface plasmon resonance showed that bi-functionalized liposomes strongly bind Aβ (kD=0.6 μM), while Thioflavin-T and SDS-PAGE/WB assays show that liposomes inhibit peptide aggregation (70% inhibition after 72 h) and trigger the disaggregation of preformed aggregates (60% decrease after 120 h incubation).
Moreover, experiments with dually radiolabelled LIP suggest that bi-functionalization enhances the passage of radioactivity across the BBB either in vitro (permeability=2.5×10(-5) cm/min, 5-fold higher with respect to mono-functionalized liposomes) or in vivo in healthy mice.
Taken together, our results suggest that mApoE-PA-LIP are valuable nanodevices with a potential applicability in vivo for the treatment of AD.
From the clinical editor: Bi-functionalized liposomes with phosphatidic acid and a modified ApoE-derived peptide were demonstrated to influence Aβ aggregation/disaggregation as a potential treatment in an Alzheimer's model.

Why it matters

In laboratory and animal experiments, liposomes carrying a modified ApoE-derived peptide bound amyloid-beta, inhibited its aggregation, triggered disaggregation of preformed aggregates, and crossed the blood-brain barrier. These results suggest potential for therapy but are preliminary and have not been tested in humans.

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Study details

Evidence strengthLow

How this study scored 41/100

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. We have no data on journal's citation record, so that was left out: it earned 39 of the 96 points we could judge it on, which is 41 out of 100.

Component	Points	Why
Journal tier	7 / 10	Tier 3 — peer-reviewed journal (Nanomedicine : nanotechnology, biology, and medicine)
Journal's citation record	— / 4	No journal record from OpenAlex — left out of this score
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	2014 — 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 152 times (OpenAlex, 2026-10-10)
Citations per year	3 / 5	10.9 citations a year over 14 year(s) since 2014
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 29 times in 2024–2026 (2026 still in progress; OpenAlex)
Senior author's track record	2 / 4	Last-listed author Francesca Re: h-index 38 (OpenAlex, whole career)
Institution's track record	1 / 3	Amsterdam UMC Location University of Amsterdam: institution h-index 992 (OpenAlex)
Multi-centre collaboration	1 / 3	OpenAlex lists 3 institution(s) in 2 countries
Indexed in PubMed	2 / 2	Indexed in PubMed (PMID 24333591)
Free to read	0 / 2	Behind a paywall — scores zero
Points	39 / 96	Scored on 19 of 20 parts. We have no data for the rest, so they are left out: 39 of the 96 points we could judge it on is 41 out of 100.
Total	41 / 100	—

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