Evidence map›Paper›PMID 35738569›Full record

ArticleLangmuir : the ACS journal of surfaces and colloids2022

Lysozyme is Sterically Trapped Within the Silica Cage in Bioinspired Silica-Lysozyme Composites: A Multi-Technique Understanding of Elusive Protein-Material Interactions.

Francesco Bruno, Lucia Gigli, Giovanni Ferraro, Andrea Cavallo, Vladimir K Michaelis, Gil Goobes, Emiliano Fratini, Enrico Ravera

Open access · hybridAbstract read
In one paragraph

Article in Langmuir : the ACS journal of surfaces and colloids, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.6field-weighted citation impact, top 43% 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

4 citing papers in PubMed, 12 citations in OpenAlex.

  1. Review
  2. The structure of His15 acetamide-modified hen egg-white lysozyme: a nice surprise from an old friend.Acta crystallographica. Section F, Structural biology communications · 2025
    Article
  3. Article
  4. 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

8 authors at 4 institutions in 3 countries.

Francesco BrunoMagnetic Resonance Center (CERM), University of Florence, via L. Sacconi 6, Sesto Fiorentino 50019, Italy.ORCID 0000-0002-4590-4316
Lucia GigliMagnetic Resonance Center (CERM), University of Florence, via L. Sacconi 6, Sesto Fiorentino 50019, Italy.
Giovanni FerraroDepartment of Chemistry "Ugo Schiff", University of Florence, via della Lastruccia 3, Sesto Fiorentino 50019, Italy.ORCID 0000-0002-8376-2486
Andrea CavalloCERTEMA S.c.a.r.l., S.P. Del Cipressino Km 10, Cinigiano 58044, Italy.
Vladimir K MichaelisDepartment of Chemistry, University of Alberta, Edmonton Alberta T6G 2G2, Canada.ORCID 0000-0002-6708-7660
Gil GoobesDepartment of Chemistry, Bar-Ilan University, Ramat Gan 5290002, Israel.ORCID 0000-0001-5735-6700
Emiliano FratiniDepartment of Chemistry "Ugo Schiff", University of Florence, via della Lastruccia 3, Sesto Fiorentino 50019, Italy.ORCID 0000-0001-7104-6530
Enrico RaveraMagnetic Resonance Center (CERM), University of Florence, via L. Sacconi 6, Sesto Fiorentino 50019, Italy.ORCID 0000-0001-7708-9208
Interuniversity Consortium for Magnetic Resonance · ITConsorzio Interuniversitario per lo Sviluppo dei Sistemi a Grande Interfase · ITBar-Ilan University · ILUniversity of Alberta · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lysozyme is widely known to promote the formation of condensed silica networks from solutions containing silicic acid, in a reproducible and cost-effective way. However, little is known about the fate of the protein after the formation of the silica particles. Also, the relative arrangement of the different components in the resulting material is a matter of debate. In this study, we investigate the nature of the protein-silica interactions by means of solid-state nuclear magnetic resonance spectroscopy, small-angle X-ray scattering, and electron microscopy. We find that lysozyme and silica are in intimate contact and strongly interacting, but their interaction is neither covalent nor electrostatic: lysozyme is mostly trapped inside the silica by steric effects.

Indexed as

MuramidaseSilicon DioxideProteinsSilicic AcidMuramidaseProteinsSilicic AcidSilicon Dioxide

Identifiers

PMID35738569
PMCPMC9261187
OpenAlexW4283380133

What OpenQuestion holds

Textmetadata
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.