Evidence map›Paper›PMID 30524669›Full record

ArticleComputational and structural biotechnology journal2018

Poly-sarcosine and Poly(Ethylene-Glycol) Interactions with Proteins Investigated Using Molecular Dynamics Simulations.

Giovanni Settanni, Timo Schäfer, Christian Muhl, Matthias Barz, Friederike Schmid

Open access · goldAbstract read
In one paragraph

Article in Computational and structural biotechnology journal, 2018. 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
–field-weighted citation impact, top 90% 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, 0 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Chemical Approaches to Synthetic Drug Delivery Systems for Systemic Applications.Angewandte Chemie (International ed. in English) · 2022
    Review
  5. Review
  6. Review
  7. Article
  8. Review
  9. Review
  10. A systematic strategy for the investigation of vaccines and drugs targeting bacteria.Computational and structural biotechnology journal · 2020
    Review
  11. 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

5 authors at 1 institution in 1 country.

Giovanni SettanniInstitut für Physik, Johannes Gutenberg University, Mainz, Germany.
Timo SchäferInstitut für Physik, Johannes Gutenberg University, Mainz, Germany.
Christian MuhlInstitut für Organische Chemie, Johannes Gutenberg University, Mainz, Germany.
Matthias BarzInstitut für Organische Chemie, Johannes Gutenberg University, Mainz, Germany.
Friederike SchmidInstitut für Physik, Johannes Gutenberg University, Mainz, Germany.
Johannes Gutenberg University Mainz · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nanoparticles coated with hydrophilic polymers often show a reduction in unspecific interactions with the biological environment, which improves their biocompatibility. The molecular determinants of this reduction are not very well understood yet, and their knowledge may help improving nanoparticle design. Here we address, using molecular dynamics simulations, the interactions of human serum albumin, the most abundant serum protein, with two promising hydrophilic polymers used for the coating of therapeutic nanoparticles, poly(ethylene-glycol) and poly-sarcosine. By simulating the protein immersed in a polymer-water mixture, we show that the two polymers have a very similar affinity for the protein surface, both in terms of the amount of polymer adsorbed and also in terms of the type of amino acids mainly involved in the interactions. We further analyze the kinetics of adsorption and how it affects the polymer conformations. Minor differences between the polymers are observed in the thickness of the adsorption layer, that are related to the different degree of flexibility of the two molecules. In comparison poly-alanine, an isomer of poly-sarcosine known to self-aggregate and induce protein aggregation, shows a significantly larger affinity for the protein surface than PEG and PSar, which we show to be related not to a different patterns of interactions with the protein surface, but to the different way the polymer interacts with water.

Indexed as

MD simulationNanoparticle protein coronaPEGPoly-peptoidPoly-sarcosine

Identifiers

PMID30524669
PMCPMC6259037
OpenAlexW2898448881

What OpenQuestion holds

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LicenceCC BY
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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.