Evidence map›Paper›PMID 30698447›Full record

ArticleThe journal of physical chemistry. B2019

Role of Ligand Conformation on Nanoparticle-Protein Interactions.

Federica Simonelli, Giulia Rossi, Luca Monticelli

Open access · greenAbstract read
In one paragraph

Article in The journal of physical chemistry. B, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.6field-weighted citation impact, top 16% 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

11 citing papers in PubMed, 32 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

3 authors at 2 institutions in 2 countries.

Federica SimonelliPhysics Department , University of Genoa , Via Dodecaneso 33 , 16146 Genoa , Italy.
Giulia RossiPhysics Department , University of Genoa , Via Dodecaneso 33 , 16146 Genoa , Italy.ORCID 0000-0001-6916-2049
Luca MonticelliMMSB, UMR 5086 CNRS, Universitè de Lyon , 7, Passage du Vercors , 69007 Lyon , France.ORCID 0000-0002-6352-4595
University of Genoa · ITUniversité Claude Bernard Lyon 1 · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Engineered biomedical nanoparticles (NPs) administered via intravenous routes are prone to associate to serum proteins. The protein corona can mask the NP surface functionalization and hamper the delivery of the NP to its biological target. The design of corona-free NPs relies on our understanding of the chemical-physical features of the NP surface driving the interaction with serum proteins. Here, we address, by computational means, the interaction between human serum albumin (HSA) and a prototypical monolayer-protected Au nanoparticle. We show that both the chemical composition (charge, hydrophobicity) and the conformational preferences of the ligands decorating the NP surface affect the NP propensity to bind HSA.

Indexed as

GoldHumansLigandsMetal NanoparticlesModels, MolecularProtein ConformationSerum Albumin, HumanGoldLigandsSerum Albumin, Human

Identifiers

PMID30698447
PMCPMC6469838
OpenAlexW2912028193

What OpenQuestion holds

Textmetadata
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.