Evidence map›Paper›PMID 31276595›Full record

ArticleNucleic acids research2019

Insights into the G-rich VEGF-binding aptamer V7t1: when two G-quadruplexes are better than one!

Federica Moccia, Claudia Riccardi, Domenica Musumeci, Serena Leone, Rosario Oliva, Luigi Petraccone, Daniela Montesarchio

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

22 citing papers in PubMed, 43 citations in OpenAlex.

  1. Review
  2. Article
  3. Determining the Optimal Heparin Binding Domain Distance in VEGFInternational journal of molecular sciences · 2026
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  5. Review
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  10. G-quadruplex DNA: a novel target for drug design.Cellular and molecular life sciences : CMLS · 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

7 authors at 3 institutions in 1 country.

Federica MocciaDepartment of Chemical Sciences, University of Naples Federico II, Via Cintia 21, I-80126 Napoli, Italy.
Claudia RiccardiDepartment of Chemical Sciences, University of Naples Federico II, Via Cintia 21, I-80126 Napoli, Italy.
Domenica MusumeciDepartment of Chemical Sciences, University of Naples Federico II, Via Cintia 21, I-80126 Napoli, Italy.
Serena LeoneDepartment of Chemical Sciences, University of Naples Federico II, Via Cintia 21, I-80126 Napoli, Italy.
Rosario OlivaDepartment of Chemical Sciences, University of Naples Federico II, Via Cintia 21, I-80126 Napoli, Italy.
Luigi PetracconeDepartment of Chemical Sciences, University of Naples Federico II, Via Cintia 21, I-80126 Napoli, Italy.
Daniela MontesarchioDepartment of Chemical Sciences, University of Naples Federico II, Via Cintia 21, I-80126 Napoli, Italy.
University of Naples Federico II · ITInstitute for Experimental Endocrinology and Oncology · ITInstitute of Biostructure and Bioimaging · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The G-quadruplex-forming VEGF-binding aptamer V7t1 was previously found to be highly polymorphic in a K+-containing solution and, to restrict its conformational preferences to a unique, well-defined form, modified nucleotides (LNA and/or UNA) were inserted in its sequence. We here report an in-depth biophysical characterization of V7t1 in a Na+-rich medium, mimicking the extracellular environment in which VEGF targeting should occur, carried out combining several techniques to analyse the conformational behaviour of the aptamer and its binding to the protein. Our results demonstrate that, in the presence of high Na+ concentrations, V7t1 behaves in a very different way if subjected or not to annealing procedures, as evidenced by native gel electrophoresis, size exclusion chromatography and dynamic light scattering analysis. Indeed, not-annealed V7t1 forms both monomeric and dimeric G-quadruplexes, while the annealed oligonucleotide is a monomeric species. Remarkably, only the dimeric aptamer efficiently binds VEGF, showing higher affinity for the protein compared to the monomeric species. These findings provide new precious information for the development of improved V7t1 analogues, allowing more efficient binding to the cancer-related protein and the design of effective biosensors or theranostic devices based on VEGF targeting.

Indexed as

G-QuadruplexesAptamers, NucleotideBinding, CompetitiveCircular DichroismNucleic Acid ConformationOligonucleotidesPotassiumProtein BindingSodiumSpectrophotometry, UltravioletVascular Endothelial Growth Factor AAptamers, NucleotideOligonucleotidesPotassiumSodiumVascular Endothelial Growth Factor A

Identifiers

PMID31276595
PMCPMC6735921
OpenAlexW2953998231

What OpenQuestion holds

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Registered trials

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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.