Evidence map›Paper›PMID 41649084›Full record

ArticleSmall (Weinheim an der Bergstrasse, Germany)2026

Genetically Encoded Sterol-Modification of a Synthetic Intrinsically Disordered Protein Drives Its Self-Assembly Into Diverse Morphologies.

Sarah Yeon-Kyoung Kim, Taranpreet Kaur, Yulia Shmidov, Matthew Yiren Wang, Lixin Fan, Abigail Leo, Nicolas Angustia, Yan Xiang, Daniel Reker, Ashutosh Chilkoti

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Small (Weinheim an der Bergstrasse, Germany), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. The Polymers of Life: Exploring Cellular Function Through Polymer Concepts.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Review
  2. 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

10 authors.

Sarah Yeon-Kyoung KimDepartment of Chemistry and Biochemistry, Washington and Lee University, Lexington, Virginia, USA.ORCID https://orcid.org/0000-0003-1500-4955
Taranpreet KaurDepartment of Biomedical Engineering, Duke University, Durham, North Carolina, USA.
Yulia ShmidovDepartment of Biomedical Engineering, Duke University, Durham, North Carolina, USA.
Matthew Yiren WangWallace H. Coulter Department of Biomedical Engineering, Georgia Institute of Technology, Atlanta, Georgia, USA.
Lixin FanBasic Science Program, Frederick National Laboratory For Cancer Research, SAXS Facility of the National Cancer Institute, Frederick, Maryland, USA.
Abigail LeoDepartment of Chemistry and Biochemistry, Washington and Lee University, Lexington, Virginia, USA.
Nicolas AngustiaDepartment of Chemistry and Biochemistry, Washington and Lee University, Lexington, Virginia, USA.
Yan XiangDepartment of Biomedical Engineering, Duke University, Durham, North Carolina, USA.
Daniel RekerDepartment of Biomedical Engineering, Duke University, Durham, North Carolina, USA.
Ashutosh ChilkotiDepartment of Biomedical Engineering, Duke University, Durham, North Carolina, USA.ORCID https://orcid.org/0000-0002-1569-2228

Funding

Genetically Encoded Smart Biohybrid MaterialsR35GM127042 · NIGMS · DUKE UNIVERSITY · PI CHILKOTI, ASHUTOSH · 2018 to 2022
$2.2M
Designing Personalized Formulations with Machine LearningR35GM151255 · NIGMS · DUKE UNIVERSITY · PI Daniel Reker · 2023 to 2026
$1.4M
NIGMS NIH HHS R35 GM127042NIGMS NIH HHS R35 GM151255NIH HHS R35-GM127042NIH HHS R35GM151255North Carolina Biotechnology Center 2017-IDG-1018
6 · The paper itself

Abstract

Post-translational modifications (PTMs) of proteins are used by natural systems to expand beyond the 20 canonical amino acids. The variation introduced at the sequence level by PTMs after expression leads to changes in both the structure and function of proteins. PTMs expand the chemical repertoire from which new biomaterials can be constructed. Inspired by the post-translational conjugation of cholesterol to proteins, we have synthesized five new hybrid lipid-protein biomaterials called Sterol-modified polypeptides (STaMPs). These STaMPs consist of an elastin-like polypeptide (ELP) conjugated to a sterol, namely coprostanol, epicoprostanol, androstanol, galeterone, or dehydroepiandrosterone. We show that STaMPs exhibit sterol-dependent self-assembly behavior, ranging from predominantly monomeric random coils for the most hydrophilic sterols to spherical micelles for the most hydrophobic sterols. Furthermore, the sterols modify the typical LCST behavior of ELPs in a predictable fashion depending on the hydrophobicity of the sterol appended.

Indexed as

SterolsElastinHydrophobic and Hydrophilic InteractionsPeptidesProtein Processing, Post-TranslationalElastinPeptidesSterolselastin‐like polypeptideslipidationpost‐translational modificationsprotein engineeringself‐assembly

Identifiers

PMID41649084
PMCPMC13255090

What OpenQuestion holds

Textmetadata
LicenceTDM
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.