Evidence map›Paper›PMID 40108179›Full record

ArticleNature communications2025

Multiphasic condensates formed with mono-component of tetrapeptides via phase separation.

Laicheng Zhou, Longchen Zhu, Cong Wang, Tengyan Xu, Jing Wang, Bin Zhang, Xin Zhang, Huaimin Wang

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 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing 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

15 citing papers in PubMed.

  1. Review
  2. Article
  3. Design of Fuel-Dependent, Complex-Coacervate-Based Synthetic Cells.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Sequence-Modulated Active Tripeptide Condensates for Tandem Catalysis.Angewandte Chemie (International ed. in English) · 2026
    Article
  11. A molecular grammar for programmable multiphase protein-RNA vesicles.bioRxiv : the preprint server for biology · 2026
    Article
  12. Review
  13. Review
  14. Article
  15. Sequence-encoded interactions program internal condensate architecture.bioRxiv : the preprint server for biology · 2025
    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

8 authors.

Laicheng Zhou *Department of Chemistry, Zhejiang University, Hangzhou, 310058, Zhejiang Province, China.
Longchen Zhu *Department of Chemistry, School of Science, Westlake University, No. 600 Yungu Road, Hangzhou, 310030, Zhejiang Province, China.
Cong Wang *Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA, 02139, USA.ORCID http://orcid.org/0000-0001-5998-3740
Tengyan XuDepartment of Chemistry, School of Science, Westlake University, No. 600 Yungu Road, Hangzhou, 310030, Zhejiang Province, China.
Jing WangDepartment of Chemistry, School of Science, Westlake University, No. 600 Yungu Road, Hangzhou, 310030, Zhejiang Province, China.
Bin ZhangDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, MA, 02139, USA. binz@mit.edu.ORCID http://orcid.org/0000-0002-3685-7503
Xin ZhangDepartment of Chemistry, School of Science, Westlake University, No. 600 Yungu Road, Hangzhou, 310030, Zhejiang Province, China. zhangxin@westlake.edu.cn.ORCID http://orcid.org/0000-0001-6686-1645
Huaimin WangDepartment of Chemistry, School of Science, Westlake University, No. 600 Yungu Road, Hangzhou, 310030, Zhejiang Province, China. wanghuaimin@westlake.edu.cn.ORCID http://orcid.org/0000-0002-8796-0367

Funding

National Natural Science Foundation of China (National Science Foundation of China) 82272145
6 · The paper itself

Abstract

Biomolecular condensates, formed by liquid-liquid phase separation of biomacromolecules, play crucial roles in regulating physiological events in biological systems. While multiphasic condensates have been extensively studied, those derived from a single component of short peptides have not yet been reported. Here, we report the symmetrical core-shell structural biomolecular condensates formed with a programmable tetrapeptide library via phase separation. Our findings reveal that tryptophan is essential for core-shell structure formation due to its strongest homotypical π-π interaction, enabling us to modulate the structure of condensates from core-shell to homogeneous by altering the amino acid composition. Molecular dynamics simulation combined with cryogenic focused ion beam scanning electron microscopy and cryogenic electron microscopy show that the inner core of multiphasic tetrapeptide condensates is solid-like, consisting of ordered structures. The core is enveloped by a liquid-like shell, stabilizing the core structure. Furthermore, we demonstrate control over multiphasic condensate formation through intrinsic redox reactions or post-translational modifications, facilitating the rational design of synthetic multiphasic condensates for various applications on demand.

Indexed as

Biomolecular CondensatesOligopeptidesCryoelectron MicroscopyMicroscopy, Electron, ScanningMolecular Dynamics SimulationPhase SeparationTryptophanOligopeptidesTryptophan

Identifiers

PMID40108179
PMCPMC11923152

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.