Evidence map›Paper›PMID 40326759›Full record

ArticleJournal of materials chemistry. B2025

Architectural control of rod-coil block polypeptide thermoresponsive self-assembly

Bin Wang, Weiran Xie, Tianren Zhang, Darrin J Pochan, Jeffery G Saven, Kristi L Kiick

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of materials chemistry. B, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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

6 authors.

Bin WangDepartment of Materials Science and Engineering, University of Delaware, Newark, DE, USA. kiick@udel.edu.ORCID http://orcid.org/0000-0002-7835-7160
Weiran XieDepartment of Materials Science and Engineering, University of Delaware, Newark, DE, USA. kiick@udel.edu.ORCID http://orcid.org/0000-0003-0316-2411
Tianren ZhangDepartment of Materials Science and Engineering, University of Delaware, Newark, DE, USA. kiick@udel.edu.ORCID http://orcid.org/0000-0003-2899-5727
Darrin J PochanDepartment of Materials Science and Engineering, University of Delaware, Newark, DE, USA. kiick@udel.edu.
Jeffery G SavenDepartment of Chemistry, University of Pennsylvania, Philadelphia, PA, USA.
Kristi L KiickDepartment of Materials Science and Engineering, University of Delaware, Newark, DE, USA. kiick@udel.edu.

Funding

Predictive Modeling & Optimal Control Framework for Model-Based Epidemic Response in DelawareP20GM103446 · NIGMS · UNIVERSITY OF DELAWARE · PI Shawn W Polson · 2012 to 2026
$67.2M
Understanding synovial macrophage inflamm-aging within osteoarthritisP20GM139760 · NIGMS · UNIVERSITY OF DELAWARE · PI DAWN M ELLIOTT · 2021 to 2026
$19.1M
Data Management and Storage System for Shared Resource FacilitiesS10OD028725 · OD · UNIVERSITY OF DELAWARE · PI POLSON, SHAWN W · 2021 to 2021
$600k
Acquisition of a Zeiss LSM710 Confocal MicroscopeS10RR027273 · NCRR · UNIVERSITY OF DELAWARE · PI DUNCAN, MELINDA K · 2010 to 2010
$494k
Zeiss LSM710 Inverted Confocal MicroscopeS10OD016361 · OD · UNIVERSITY OF DELAWARE · PI CAPLAN, JEFFREY L · 2015 to 2015
$444k
NCRR NIH HHS S10 RR027273NIGMS NIH HHS P20 GM103446NIGMS NIH HHS P20 GM139760NIH HHS S10 OD016361NIH HHS S10 OD028725
6 · The paper itself

Abstract

The architectural control of the self-assembly of a series of block polypeptides comprising a concatenation of an elastin-like peptide and a coiled-coil, bundle-forming peptide (ELP-BFPs), has been demonstrated. Assembly of the polypeptides is controlled by coacervation of the hydrophobic ELP domain, while the type of coiled-coil assembly of the BFP and the specific placement of short histidine tags significantly tunes assembly behavior. Spectrophotometric analysis of self-assembly demonstrated that the transition temperature of assembly can be controlled by the design of the BFP domain and positioning of the His-tags in the constructs. Cryogenic transmission electron microscopy of assembled polypeptides confirmed distinct morphologies including core-shell particles and multilayer vesicles, depending on the parallel or antiparallel bundle architecture of the block polypeptide. The results have applications in materials design and highlight the potential for controlling multi-stimuli responsiveness and morphologies through fine control of the architectural features of the component polypeptide domains.

Indexed as

PeptidesTemperatureElastinParticle SizeElastinPeptides

Identifiers

PMID40326759
PMCPMC12054350

What OpenQuestion holds

Textmetadata
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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.