Evidence map›Paper›PMID 35628247›Full record

ArticleInternational journal of molecular sciences2022

Lactoferrin Inhibition of the Complex Formation between ACE2 Receptor and SARS CoV-2 Recognition Binding Domain.

Roberta Piacentini, Laura Centi, Mattia Miotto, Edoardo Milanetti, Lorenzo Di Rienzo, Martina Pitea, Paolo Piazza, Giancarlo Ruocco, Alberto Boffi, Giacomo Parisi

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.3field-weighted citation impact, top 10% 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

17 citing papers in PubMed, 23 citations in OpenAlex.

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  11. Lactoferrin, the Moonlighting Protein of Innate Immunity.International journal of molecular sciences · 2023
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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

10 authors at 2 institutions in 1 country.

Roberta PiacentiniDepartment of Biochemistry, Sapienza University, Piazzale Aldo Moro 5, 00185 Rome, Italy.ORCID 0000-0003-1381-9560
Laura CentiDepartment of Biochemistry, Sapienza University, Piazzale Aldo Moro 5, 00185 Rome, Italy.ORCID 0000-0002-8253-940X
Mattia MiottoCenter of Life Nano and Neuro Science, Institute of Italian Technology, Viale Regina Elena 291, 00181 Rome, Italy.ORCID 0000-0002-0043-8921
Edoardo MilanettiCenter of Life Nano and Neuro Science, Institute of Italian Technology, Viale Regina Elena 291, 00181 Rome, Italy.
Lorenzo Di RienzoCenter of Life Nano and Neuro Science, Institute of Italian Technology, Viale Regina Elena 291, 00181 Rome, Italy.
Martina PiteaCenter of Life Nano and Neuro Science, Institute of Italian Technology, Viale Regina Elena 291, 00181 Rome, Italy.ORCID 0000-0002-3982-4141
Paolo PiazzaEDIF Instruments s.r.l., Via Ardeatina 132, 00147 Rome, Italy.
Giancarlo RuoccoCenter of Life Nano and Neuro Science, Institute of Italian Technology, Viale Regina Elena 291, 00181 Rome, Italy.ORCID 0000-0002-2762-9533
Alberto BoffiDepartment of Biochemistry, Sapienza University, Piazzale Aldo Moro 5, 00185 Rome, Italy.
Giacomo ParisiCenter of Life Nano and Neuro Science, Institute of Italian Technology, Viale Regina Elena 291, 00181 Rome, Italy.ORCID 0000-0002-3064-0928
Italian Institute of Technology · ITSapienza University of Rome · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The present investigation focuses on the analysis of the interactions among human lactoferrin (LF), SARS-CoV-2 receptor-binding domain (RBD) and human angiotensin-converting enzyme 2 (ACE2) receptor in order to assess possible mutual interactions that could provide a molecular basis of the reported preventative effect of lactoferrin against CoV-2 infection. In particular, kinetic and thermodynamic parameters for the pairwise interactions among the three proteins were measured via two independent techniques, biolayer interferometry and latex nanoparticle-enhanced turbidimetry. The results obtained clearly indicate that LF is able to bind the ACE2 receptor ectodomain with significantly high affinity, whereas no binding to the RBD was observed up to the maximum "physiological" lactoferrin concentration range. Lactoferrin, above 1 µM concentration, thus appears to directly interfere with RBD-ACE2 binding, bringing about a measurable, up to 300-fold increase of the K

Indexed as

Angiotensin-Converting Enzyme 2COVID-19LactoferrinSARS-CoV-2HumansPeptidyl-Dipeptidase AProtein Interaction Domains and MotifsSpike Glycoprotein, CoronavirusACE2 protein, humanAngiotensin-Converting Enzyme 2LactoferrinPeptidyl-Dipeptidase ASpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2angiotensin-converting enzyme 2 (ACE2)biolayer interferometrykinetic analysislactoferrinnanoparticle enhanced turbidimetrySARS-CoV-2 receptor-binding domain (RBD)

Identifiers

PMID35628247
PMCPMC9141661
OpenAlexW4280568295

What OpenQuestion holds

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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.