Evidence map›Paper›PMID 36235232›Full record

ArticleMolecules (Basel, Switzerland)2022

Revealing Angiopep-2/LRP1 Molecular Interaction for Optimal Delivery to Glioblastoma (GBM).

Angela Costagliola di Polidoro, Andrea Cafarchio, Donatella Vecchione, Paola Donato, Francesco De Nola, Enza Torino

Open access · goldAbstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed, 1 pooled it
2.4field-weighted citation impact, top 11% 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, 1 synthesis or guideline pooled it, 33 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Review
  4. Review
  5. Review
  6. Review
  7. Review
  8. Article
  9. Review
  10. Review
  11. Review
  12. Review
  13. Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Advancements in nanotheranostics for glioma therapy.Naunyn-Schmiedeberg's archives of pharmacology · 2025
    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

6 authors at 2 institutions in 1 country.

Angela Costagliola di PolidoroDepartment of Chemical, Materials and Production Engineering (DICMaPI), University of Naples Federico II, 80125 Naples, Italy.
Andrea CafarchioDepartment of Chemical, Materials and Production Engineering (DICMaPI), University of Naples Federico II, 80125 Naples, Italy.ORCID 0000-0002-1720-8778
Donatella VecchioneTeoresi Spa-Via F. Imparato, 198 CM2, 80146 Napoli, Italy.
Paola DonatoTeoresi Spa-Via F. Imparato, 198 CM2, 80146 Napoli, Italy.
Francesco De NolaTeoresi Spa-Via F. Imparato, 198 CM2, 80146 Napoli, Italy.
Enza TorinoDepartment of Chemical, Materials and Production Engineering (DICMaPI), University of Naples Federico II, 80125 Naples, Italy.ORCID 0000-0002-8905-1925
Center for Advanced Biomaterials for Healthcare · ITUniversity of Molise · IT

Funding

Ministry of Education, Universities and Research 2017MHJJ55
6 · The paper itself

Abstract

backgroundThe family of synthetic peptide angiopeps, and particularly angiopep-2 (ANG-2) demonstrated the ability preclinically and clinically to shuttle active molecules across the blood-brain barrier (BBB) and selectively toward brain tumor cells. The literature has also proved that the transport occurs through a specific receptor-mediated transcytosis of the peptide by LRP-1 receptors present both on BBB and tumor cell membranes. However, contradictory results about exploiting this promising mechanism to engineer complex delivery systems, such as nanoparticles, are being obtained. METHODOLOGY: For this reason, we applied a molecular docking (MD)-based strategy to investigate the molecular interaction of ANG-2 and the LRP-1 ligand-binding moieties (CR56 and CR17), clarifying the impact of peptide conjugation on its transport mechanism.

resultsMD results proved that ANG-2/LRP-1 binding involves the majority of ANG-2 residues, is characterized by high binding energies, and that it is site-specific for CR56 where the binding to 929ASP recalls a transcytosis mechanism, resembling the binding of the receptor to the receptor-associated protein. On the other hand, ANG-2 binding to CR17 is less site-specific but, as proved for apolipoprotein internalization in physiological conditions, it involves the ANG-2 lysin residue.

conclusionsOverall, our results proved that ANG-2 energetic interaction with the LRP-1 receptor is not hindered if specific residues of the peptide are chemically crosslinked to simple or complex engineered delivery systems.

Indexed as

Brain NeoplasmsGlioblastomaBlood-Brain BarrierCell Line, TumorDrug Delivery SystemsHumansLigandsLow Density Lipoprotein Receptor-Related Protein-1Molecular Docking SimulationPeptidesAngiopep-2LigandsLow Density Lipoprotein Receptor-Related Protein-1LRP1 protein, humanPeptidesangiopep-2glioblastomamolecular dockingoptimal design

Identifiers

PMID36235232
PMCPMC9572160
OpenAlexW4303958900

What OpenQuestion holds

Textmetadata
LicenceCC BY
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 OpenQuestion graph.