Evidence map›Paper›PMID 40069227›Full record

ArticleNature communications2025

Binary peptide coacervates as an active model for biomolecular condensates.

Shoupeng Cao, Peng Zhou, Guizhi Shen, Tsvetomir Ivanov, Xuehai Yan, Katharina Landfester, Lucas Caire da Silva

Abstract read
In one paragraph

Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
–field-weighted citation impact
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

26 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
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  5. Article
  6. Article
  7. Article
  8. Article
  9. MgChem & bio engineering · 2026
    Article
  10. Review
  11. Article
  12. Enantiopurity-Dependent Peptide Coacervates and Asymmetric Organocatalysis.Small (Weinheim an der Bergstrasse, Germany) · 2026
    Article
  13. Sequence-Modulated Active Tripeptide Condensates for Tandem Catalysis.Angewandte Chemie (International ed. in English) · 2026
    Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Emergent properties of supramolecular peptide assemblies.Chemical communications (Cambridge, England) · 2026
    Review
  19. Article
  20. 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

7 authors.

Shoupeng Cao *College of Polymer Science and Engineering, State Key Laboratory of Polymer Materials Engineering, Sichuan University, Chengdu, 610065, PR China.ORCID http://orcid.org/0000-0002-5856-2407
Peng Zhou *State Key Laboratory of Biochemical Engineering, Key Laboratory of Biopharmaceutical Preparation and Delivery, Institute of Process Engineering, Chinese Academy of Science, Beijing, 100190, PR China.ORCID http://orcid.org/0000-0002-6849-3855
Guizhi ShenState Key Laboratory of Biochemical Engineering, Key Laboratory of Biopharmaceutical Preparation and Delivery, Institute of Process Engineering, Chinese Academy of Science, Beijing, 100190, PR China.
Tsvetomir IvanovMax Planck Institute for Polymer Research, 55128, Mainz, Germany.
Xuehai YanState Key Laboratory of Biochemical Engineering, Key Laboratory of Biopharmaceutical Preparation and Delivery, Institute of Process Engineering, Chinese Academy of Science, Beijing, 100190, PR China. yanxh@ipe.ac.cn.ORCID http://orcid.org/0000-0002-0890-0340
Katharina LandfesterMax Planck Institute for Polymer Research, 55128, Mainz, Germany. landfester@mpip-mainz.mpg.de.ORCID http://orcid.org/0000-0001-9591-4638
Lucas Caire da SilvaMax Planck Institute for Polymer Research, 55128, Mainz, Germany. lucas.cairedasilva@mcgill.ca.ORCID http://orcid.org/0000-0003-4663-3471

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Biomolecular condensates formed by proteins and nucleic acids are critical for cellular processes. Macromolecule-based coacervate droplets formed by liquid-liquid phase separation serve as synthetic analogues, but are limited by complex compositions and high molecular weights. Recently, short peptides have emerged as an alternative component of coacervates, but tend to form metastable microdroplets that evolve into rigid nanostructures. Here we present programmable coacervates using binary mixtures of diphenylalanine-based short peptides. We show that the presence of different short peptides stabilizes the coacervate phase and prevents the formation of rigid structures, allowing peptide coacervates to be used as stable adaptive compartments. This approach allows fine control of droplet formation and dynamic morphological changes in response to physiological triggers. As compartments, short peptide coacervates sequester hydrophobic molecules and enhance bio-orthogonal catalysis. In addition, the incorporation of coacervates into model synthetic cells enables the design of Boolean logic gates. Our findings highlight the potential of short peptide coacervates for creating adaptive biomimetic systems and provide insight into the principles of phase separation in biomolecular condensates.

Indexed as

Biomolecular CondensatesPeptidesArtificial CellsDipeptidesHydrophobic and Hydrophilic InteractionsNanostructuresPhenylalanineDipeptidesPeptidesPhenylalaninephenylalanylphenylalanine

Identifiers

PMID40069227
PMCPMC11897134

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Registered trials

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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.