Evidence map›Paper›PMID 40386766›Full record

ReviewMolecular systems design & engineering2025

Toward understanding biomolecular materials comprising intrinsically disordered proteins

Bin Wang, Tianren Zhang, Sirui Shen, Darrin J Pochan, Jeffery G Saven, Kristi L Kiick

Abstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in Molecular systems design & engineering, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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 https://orcid.org/0000-0002-7835-7160
Tianren ZhangDepartment of Materials Science and Engineering, University of Delaware Newark DE USA kiick@udel.edu.ORCID https://orcid.org/0000-0003-2899-5727
Sirui ShenDepartment of Materials Science and Engineering, University of Delaware Newark DE USA kiick@udel.edu.ORCID https://orcid.org/0009-0003-7886-8221
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 saven@sas.upenn.edu.
Kristi L KiickDepartment of Materials Science and Engineering, University of Delaware Newark DE USA kiick@udel.edu.ORCID https://orcid.org/0000-0001-8587-0301

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
This renovation project will create over 1455 sq. ft. of state- of-the-art reseaP20GM104316 · NIGMS · UNIVERSITY OF DELAWARE · PI FOX, JOSEPH M · 2014 to 2024
$26.8M
Understanding synovial macrophage inflamm-aging within osteoarthritisP20GM139760 · NIGMS · UNIVERSITY OF DELAWARE · PI DAWN M ELLIOTT · 2021 to 2026
$19.1M
UDE COBRE: STRAINED MOLECULES FOR SYNTHESIS OF UNNATURAL AMINO ACIDSP20RR017716 · NCRR · UNIVERSITY OF DELAWARE · PI BEEBE, THOMAS PAUL · 2002 to 2011
$16.9M
Collagen-mediated approaches to improve the local delivery and hypothermic release of osteoarthritis therapeuticsR01AR080707 · NIAMS · UNIVERSITY OF DELAWARE · PI Christopher Price · 2023 to 2026
$2.4M
Highly resilient, hydrophilic bioelastomers for engineering vocal fold tissueR01DC011377 · NIDCD · UNIVERSITY OF DELAWARE · PI KIICK, KRISTI L · 2012 to 2016
$2.3M
NCRR NIH HHS P20 RR017716NIAMS NIH HHS R01 AR080707NIDCD NIH HHS R01 DC011377NIGMS NIH HHS P20 GM103446NIGMS NIH HHS P20 GM104316NIGMS NIH HHS P20 GM139760
6 · The paper itself

Abstract

Intrinsically disordered proteins (IDPs) yield solutions with tunable phase transition behavior and have been widely applied in designing stimuli-responsive materials. Understanding interactions between amino acid residues of the IDP sequence is critical to designing new IDP-based materials with selective phase behavior, assembly, and mechanical properties. The lack of defined structure for this class of proteins complicates accurate prediction of their molecular-scale behavior. In this review, recent progress is presented in the development and application of simulation methods to describe the behavior of IDPs. Results for elastin-like polypeptides (ELPs) and resilin-like polypeptides (RLPs) are highlighted, focusing on studies that compare simulation results with experimental findings.

Identifiers

PMID40386766
PMCPMC12082076

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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.