Evidence map›Paper›PMID 40886156›Full record

ArticleBiomacromolecules2025

Role of Charge Patterning and Hydrophobicity in Peptide-Based Complex Coacervates.

Arvind Sathyavageeswaran, Pankaj Kumar Pandey, Nickolas Holmlund, Priyanka Kaushik, Shannon McIntosh, Raneem Mokdad, Sarah L Perry

Abstract read
In one paragraph

Article in Biomacromolecules, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed.

  1. Article
  2. Article
  3. Reversible Nucleolar Complex Coacervation by Short Cationic Peptides.Journal of the American Chemical Society · 2026
    Article
  4. Article
  5. 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

7 authors.

Arvind SathyavageeswaranDepartment of Chemical Engineering, University of Massachusetts Amherst, Amherst, Massachusetts 01003, United States.
Pankaj Kumar PandeyDepartment of Chemical Engineering, University of Massachusetts Amherst, Amherst, Massachusetts 01003, United States.ORCID 0009-0001-2304-5135
Nickolas HolmlundDepartment of Chemical Engineering, University of Massachusetts Amherst, Amherst, Massachusetts 01003, United States.
Priyanka KaushikDepartment of Chemical Engineering, University of Massachusetts Amherst, Amherst, Massachusetts 01003, United States.
Shannon McIntoshDepartment of Chemical Engineering, University of Massachusetts Amherst, Amherst, Massachusetts 01003, United States.
Raneem MokdadDepartment of Chemical Engineering, University of Massachusetts Amherst, Amherst, Massachusetts 01003, United States.
Sarah L PerryDepartment of Chemical Engineering, University of Massachusetts Amherst, Amherst, Massachusetts 01003, United States.ORCID 0000-0003-2301-6710

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Complex coacervation has emerged as a powerful model for studying the self-assembly of intrinsically disordered proteins (IDPs) in biological condensates in cells. We characterized the phase behavior and rheology of coacervates formed from peptides with regular repeating sequences to examine the effects of charge patterning and hydrophobicity on coacervate stability and material properties. Our results show that increasing the size of charged blocks enhances salt resistance via electrostatic cooperativity, while incorporating small hydrophobic segments further stabilizes coacervates and increases viscosity through hydrophobic clustering. Interestingly, our results involving alanine as the neutral residue suggest that structural conformations present for peptides with shorter block sizes may contribute to increased viscosity within the coacervate phase. Overall, these findings underscore the potential of sequence-controlled materials as versatile platforms for engineering self-assembling materials with tunable mechanical and phase properties.

Indexed as

Intrinsically Disordered ProteinsPeptidesHydrophobic and Hydrophilic InteractionsRheologyStatic ElectricityViscosityIntrinsically Disordered ProteinsPeptides

Identifiers

PMID40886156
PMCPMC12525026

What OpenQuestion holds

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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.