Evidence map›Paper›PMID 31991749›Full record

ArticleBiomolecules2020

Structure-Activity Relationship of HER2 Receptor Targeting Peptide and Its Derivatives in Targeted Tumor Therapy.

Beáta Biri-Kovács, Afrodité Adorján, Ildikó Szabó, Bálint Szeder, Szilvia Bősze, Gábor Mező

Open access · goldAbstract read
In one paragraph

Article in Biomolecules, 2020. 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
0.9field-weighted citation impact, top 24% 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, 19 citations in OpenAlex.

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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 2 institutions in 1 country.

Beáta Biri-KovácsEötvös Loránd University (ELTE), Faculty of Science, Institute of Chemistry, Budapest 1117, Hungary.
Afrodité AdorjánEötvös Loránd University (ELTE), Faculty of Science, Institute of Chemistry, Budapest 1117, Hungary.
Ildikó SzabóMTA-ELTE Research Group of Peptide Chemistry, Budapest, Hungary, Budapest 1117, Hungary.
Bálint SzederResearch Centre for Natural Sciences, Institute of Enzymology, Hungarian Academy of Sciences, Budapest 1117, Hungary.
Szilvia BőszeMTA-ELTE Research Group of Peptide Chemistry, Budapest, Hungary, Budapest 1117, Hungary.
Gábor MezőEötvös Loránd University (ELTE), Faculty of Science, Institute of Chemistry, Budapest 1117, Hungary.
Eötvös Loránd University · HUInstitute of Molecular Life Sciences · HU

Funding

European Union and the State of Hungary, co-financed by the European Regional Development Fund VEKOP-2.3.3-15-2017-00020Nemzeti Kutatási Fejlesztési és Innovációs Hivatal K119552, NVKP_16-1-2016-0036, NKFIH-1157-8/2019-DT
6 · The paper itself

Abstract

Human epidermal growth factor (HER2) is a transmembrane tyrosine kinase receptor that is frequently overexpressed in breast cancer. Its increased level prognoses a poor patient outcome and a high mortality rate. Despite the widening spectrum of therapies that are becoming available to treat HER2+ breast cancer, its side effects and resistance still make this protein a valuable object of research in targeted tumor therapy. The role of tumor-targeting peptides has become more and more prominent in the last few decades due to their simple synthesis and pharmakokinetic properties. Here, we examine two fluorescently-labeled HER2-specific peptides and their combined analogues that are developed to target the extracellular region of HER2. The peptides are investigated on breast cancer cell lines with different HER2 expression profiles. Moreover, their extracellular localization and specificity are confirmed by flow cytometry and confocal microscopy. Therefore, a new, combined HER2 binding conjugate is obtained that interacts with HER2-overexpressing cells with high affinity and specificity. Furthermore, secondary structure prediction reveals that the α-helical content of the peptides is associated with their receptor recognition. This highly specific conjugate can be used as a starting point for diagnostical or drug-targeting purposes in upcoming studies.

Indexed as

Molecular Targeted TherapyBreast NeoplasmsDrug Delivery SystemsErb-b2 Receptor Tyrosine KinasesFemaleGene Expression Regulation, NeoplasticHumansMCF-7 CellsPeptidesPrognosisProtein BindingProtein Structure, SecondaryStructure-Activity RelationshipERBB2 protein, humanErb-b2 Receptor Tyrosine KinasesPeptidesbreast cancerHER2HER2 diagnosistargeted tumor therapytargeting peptide

Identifiers

PMID31991749
PMCPMC7072344
OpenAlexW3001211234

What OpenQuestion holds

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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.