Evidence map›Paper›PMID 28722016›Full record

ArticleNature communications2017

Silk micrococoons for protein stabilisation and molecular encapsulation.

Ulyana Shimanovich, Francesco S Ruggeri, Erwin De Genst, Jozef Adamcik, Teresa P Barros, David Porter, Thomas Müller, Raffaele Mezzenga, Christopher M Dobson, Fritz Vollrath and 2 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
5.2field-weighted citation impact, top 4% 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

45 citing papers in PubMed, 133 citations in OpenAlex.

  1. Article
  2. Article
  3. Silk protein plastics for sustained and controlled drug release.International journal of pharmaceutics · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Microcompartmentalization Controls Silk Feedstock Rheology.Langmuir : the ACS journal of surfaces and colloids · 2023
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Challenges in delivering therapeutic peptides and proteins: A silk-based solution.Journal of controlled release : official journal of the Controlled Release Society · 2022
    Review
  19. Article
  20. Article
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

12 authors at 4 institutions in 4 countries.

Ulyana ShimanovichDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.
Francesco S RuggeriDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.
Erwin De GenstDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.
Jozef AdamcikDepartment of Health Science and Technology, ETH Zurich 8092, Switzerland.
Teresa P BarrosDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.
David PorterDepartment of Zoology, University of Oxford, South Parks Road, Oxford OX1 3PS, UK.
Thomas MüllerDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.
Raffaele MezzengaDepartment of Health Science and Technology, ETH Zurich 8092, Switzerland.
Christopher M DobsonDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.
Fritz VollrathDepartment of Zoology, University of Oxford, South Parks Road, Oxford OX1 3PS, UK.
Chris HollandDepartment of Materials Science and Engineering, University of Sheffield, Sheffield S1 3JD, UK.ORCID 0000-0003-0913-2221
Tuomas P J KnowlesDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.
University of Cambridge · GBETH Zurich · CHUniversity of Oxford · GBUniversity of Sheffield · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Naturally spun silks generate fibres with unique properties, including strength, elasticity and biocompatibility. Here we describe a microfluidics-based strategy to spin liquid native silk, obtained directly from the silk gland of Bombyx mori silkworms, into micron-scale capsules with controllable geometry and variable levels of intermolecular β-sheet content in their protein shells. We demonstrate that such micrococoons can store internally the otherwise highly unstable liquid native silk for several months and without apparent effect on its functionality. We further demonstrate that these native silk micrococoons enable the effective encapsulation, storage and release of other aggregation-prone proteins, such as functional antibodies. These results show that native silk micrococoons are capable of preserving the full activity of sensitive cargo proteins that can aggregate and lose function under conditions of bulk storage, and thus represent an attractive class of materials for the storage and release of active biomolecules.

Indexed as

AnimalsBombyxElasticityProtein Conformation, beta-StrandProtein StabilitySilkSilk

Identifiers

PMID28722016
PMCPMC5524934
OpenAlexW2738603213

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.