Evidence map›Paper›PMID 29263666›Full record

ArticleInternational journal of nanomedicine2017

Development of surface-engineered PLGA nanoparticulate-delivery system of Tet1-conjugated nattokinase enzyme for inhibition of Aβ

Prakash Chandra Bhatt, Amita Verma, Fahad A Al-Abbasi, Firoz Anwar, Vikas Kumar, Bibhu Prasad Panda

Open access · goldAbstract read
In one paragraph

Article in International journal of nanomedicine, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

23 citing papers in PubMed, 68 citations in OpenAlex.

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  16. TweenNanomaterials (Basel, Switzerland) · 2021
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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

6 authors at 3 institutions in 2 countries.

Prakash Chandra BhattMicrobial and Pharmaceutical Biotechnology Laboratory, Centre for Advanced Research in Pharmaceutical Science, Faculty of Pharmacy, Jamia Hamdard, New Delhi, India.
Amita VermaBioorganic & Medicinal Chemistry Research Laboratory, Department of Pharmaceutical Sciences, Faculty of Health Sciences, Sam Higginbottom University of Agriculture, Technology and Sciences, Allahabad, Uttar Pradesh, India.
Fahad A Al-AbbasiDepartment of Biochemistry, Faculty of Science, King Abdulaziz University, Jeddah, Saudi Arabia.
Firoz AnwarDepartment of Biochemistry, Faculty of Science, King Abdulaziz University, Jeddah, Saudi Arabia.
Vikas KumarNatural Product Drug Discovery Laboratory, Department of Pharmaceutical Sciences, Faculty of Health Sciences, Sam Higginbottom University of Agriculture, Technology and Sciences, Allahabad, Uttar Pradesh, India.
Bibhu Prasad PandaMicrobial and Pharmaceutical Biotechnology Laboratory, Centre for Advanced Research in Pharmaceutical Science, Faculty of Pharmacy, Jamia Hamdard, New Delhi, India.
Jamia Hamdard · INKing Abdulaziz University · SASam Higginbottom Institute of Agriculture · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

According to the World Health Organization, globally there are around 18 million patients suffering from Alzheimer's disease (AD), and this number is expected to double by 2025. The pathophysiology of AD includes selective deposition of Aβ peptide in the mitochondria of cells, which inhibits uptake of glucose by neurons and key enzyme functions. Current drug treatments for AD are unable to rectify the underlying pathology of the disease; they only provide short-term symptomatic relief, so there is a need for the development of newer treatment regimes. The antiamyloid activity, antifibrinolytic activity, and antithrombotic activity of nattokinase holds potential for the treatment of AD. As nattokinase is a protein, its stability restricts its usage to a greater extent, but this limitation can be overcome by nanoencapsulation. In this work, we successfully synthesized polymeric nanoparticles of nattokinase and characterized its use by different techniques: transmission electron microscopy, scanning electron microscopy, DTS Nano, differential scanning calorimetry, Fourier-transform infrared spectroscopy, thioflavin T-binding assay, in vitro drug release, antifibrinolytic activity, and in vivo antiamyloid activity. As brain targeting of hydrophilic drugs is complicated due to the stringent nature of blood-brain barrier, in the current experimental study, we conjugated poly(lactic-

Indexed as

Alzheimer DiseaseAmyloid beta-PeptidesAntifibrinolytic AgentsCalorimetry, Differential ScanningDrug Delivery SystemsDrug LiberationFibrinolytic AgentsHumansLactic AcidMicroscopy, Electron, ScanningMicroscopy, Electron, TransmissionMixed Function OxygenasesNanoparticlesPeptide FragmentsPlaque, AmyloidPolyglycolic AcidAmyloid beta-Peptidesamyloid beta-protein (1-40)Antifibrinolytic AgentsFibrinolytic AgentsLactic AcidMixed Function OxygenasesnattokinasePeptide FragmentsPolyglycolic AcidPolylactic Acid-Polyglycolic Acid CopolymerProto-Oncogene ProteinsSubtilisinsTET1 protein, humanAlzheimer’s diseaseAβ40nattokinasePLGAsurface modificationTEMTet1 peptide

Identifiers

PMID29263666
PMCPMC5732557
OpenAlexW2771911282

What OpenQuestion holds

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LicenceCC BY-NC
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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 OpenQuestion graph.