Evidence map›Paper›PMID 34878460›Full record

ArticlePhysical chemistry chemical physics : PCCP2021

Graphene quantum dots obstruct the membrane axis of Alzheimer's amyloid beta.

Huayuan Tang, Yuhuan Li, Aleksandr Kakinen, Nicholas Andrikopoulos, Yunxiang Sun, Eunbi Kwak, Thomas P Davis, Feng Ding, Pu Chun Ke

Open access · greenAbstract read
In one paragraph

Article in Physical chemistry chemical physics : PCCP, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
2.9field-weighted citation impact, top 8% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

8 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Spike Protein Fragments Promote Alzheimer's Amyloidogenesis.ACS applied materials & interfaces · 2023
    Article
  6. Article
  7. Review
  8. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors at 6 institutions in 3 countries.

Huayuan TangDepartment of Physics and Astronomy, Clemson University, Clemson, SC 29634, USA. fding@clemson.edu.
Yuhuan LiLiver Cancer Institute, Zhongshan Hospital, Key Laboratory of Carcinogenesis and Cancer Invasion, Ministry of Education, Fudan University, Shanghai, 200032, China.
Aleksandr KakinenAustralian Institute for Bioengineering and Nanotechnology, The University of Queensland, Brisbane, QLD 4072, Australia.
Nicholas AndrikopoulosDrug Delivery, Disposition and Dynamics, Monash Institute of Pharmaceutical Sciences, Monash University, 381 Royal Parade, Parkville, VIC 3052, Australia. pu-chun.ke@monash.edu.
Yunxiang SunSchool of Physical Science and Technology, Ningbo University, Ningbo 315211, China.ORCID http://orcid.org/0000-0001-9799-7131
Eunbi KwakDrug Delivery, Disposition and Dynamics, Monash Institute of Pharmaceutical Sciences, Monash University, 381 Royal Parade, Parkville, VIC 3052, Australia. pu-chun.ke@monash.edu.
Thomas P DavisDrug Delivery, Disposition and Dynamics, Monash Institute of Pharmaceutical Sciences, Monash University, 381 Royal Parade, Parkville, VIC 3052, Australia. pu-chun.ke@monash.edu.
Feng DingDepartment of Physics and Astronomy, Clemson University, Clemson, SC 29634, USA. fding@clemson.edu.ORCID http://orcid.org/0000-0003-1850-6336
Pu Chun KeDrug Delivery, Disposition and Dynamics, Monash Institute of Pharmaceutical Sciences, Monash University, 381 Royal Parade, Parkville, VIC 3052, Australia. pu-chun.ke@monash.edu.ORCID http://orcid.org/0000-0003-2134-0859
The University of Queensland · AUClemson University · USFudan University · CNMonash University · AUNational Engineering Research Center for Nanotechnology · CNNingbo University · CN

Funding

Inhibition of Human Islet Amyloid Polypeptide AggregationR35GM119691 · NIGMS · CLEMSON UNIVERSITY · PI DING, FENG · 2016 to 2020
$1.9M
NIGMS NIH HHS R35 GM119691
6 · The paper itself

Abstract

Alzheimer's disease (AD) is a primary form of dementia with debilitating consequences, but no effective cure is available. While the pathophysiology of AD remains multifactorial, the aggregation of amyloid beta (Aβ) mediated by the cell membrane is known to be the cause for the neurodegeneration associated with AD. Here we examined the effects of graphene quantum dots (GQDs) on the obstruction of the membrane axis of Aβ in its three representative forms of monomers (Aβ-m), oligomers (Aβ-o), and amyloid fibrils (Aβ-f). Specifically, we determined the membrane fluidity of neuroblastoma SH-SY5Y cells perturbed by the Aβ species, especially by the most toxic Aβ-o, and demonstrated their recovery by GQDs using confocal fluorescence microscopy. Our computational data through discrete molecular dynamics simulations further revealed energetically favorable association of the Aβ species with the GQDs in overcoming peptide-peptide aggregation. Overall, this study positively implicated GQDs as an effective agent in breaking down the membrane axis of Aβ, thereby circumventing adverse downstream events and offering a potential therapeutic solution for AD.

Indexed as

Alzheimer DiseaseAmyloid beta-PeptidesCell MembraneGraphiteHumansMolecular Dynamics SimulationProtein AggregatesQuantum DotsAmyloid beta-PeptidesGraphiteProtein Aggregates

Identifiers

PMID34878460
PMCPMC8771921
OpenAlexW3215432890

What Socratic holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.