Evidence map›Paper›PMID 36757021›Full record

ArticleBiomacromolecules2023

Lipidation Alters the Structure and Hydration of Myristoylated Intrinsically Disordered Proteins.

Jingjing Ji, Md Shahadat Hossain, Emily N Krueger, Zhe Zhang, Shivangi Nangia, Britnie Carpentier, Mae Martel, Shikha Nangia, Davoud Mozhdehi

Full text read
In one paragraph

Article in Biomacromolecules, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing 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

12 citing papers in PubMed.

  1. The Polymers of Life: Exploring Cellular Function Through Polymer Concepts.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Review
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  12. Spontaneous Self-Organized Order Emerging From Intrinsically Disordered Protein Polymers.Wiley interdisciplinary reviews. Nanomedicine and nanobiotechnology
    Review
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

9 authors.

Jingjing JiDepartment of Biomedical and Chemical Engineering, Syracuse University, Syracuse, New York 13244, United States.
Md Shahadat HossainDepartment of Chemistry, Syracuse University, Syracuse, New York 13244, United States.ORCID 0000-0002-6688-5310
Emily N KruegerDepartment of Chemistry, Syracuse University, Syracuse, New York 13244, United States.
Zhe ZhangDepartment of Chemistry, Syracuse University, Syracuse, New York 13244, United States.
Shivangi NangiaDepartment of Chemistry, University of Hartford, West Hartford, Connecticut 06117, United States.
Britnie CarpentierDepartment of Biomedical and Chemical Engineering, Syracuse University, Syracuse, New York 13244, United States.
Mae MartelDepartment of Biomedical and Chemical Engineering, Syracuse University, Syracuse, New York 13244, United States.
Shikha NangiaDepartment of Biomedical and Chemical Engineering, Syracuse University, Syracuse, New York 13244, United States.ORCID 0000-0003-1170-8461
Davoud MozhdehiDepartment of Biomedical and Chemical Engineering, Syracuse University, Syracuse, New York 13244, United States.ORCID 0000-0002-3440-8878

Funding

Breakthrough Molecular Dynamics Research via an Anton2 SupercomputerR01GM116961 · NIGMS · CARNEGIE-MELLON UNIVERSITY · PI BLOOD, PHILIP D. · 2016 to 2023
$3.0M
Genetically Encoded Lipidation to Manipulate Structure, Assembly, and Phase Behavior of ProteinsR35GM142899 · NIGMS · SYRACUSE UNIVERSITY · PI MOZHDEHI , DAVOUD · 2021 to 2025
$1.8M
NIGMS NIH HHS R01 GM116961NIGMS NIH HHS R35 GM142899
6 · The paper itself

Abstract

Lipidated proteins are an emerging class of hybrid biomaterials that can integrate the functional capabilities of proteins into precisely engineered nano-biomaterials with potential applications in biotechnology, nanoscience, and biomedical engineering. For instance, fatty-acid-modified elastin-like polypeptides (FAMEs) combine the hierarchical assembly of lipids with the thermoresponsive character of elastin-like polypeptides (ELPs) to form nanocarriers with emergent temperature-dependent structural (shape or size) characteristics. Here, we report the biophysical underpinnings of thermoresponsive behavior of FAMEs using computational nanoscopy, spectroscopy, scattering, and microscopy. This integrated approach revealed that temperature and molecular syntax alter the structure, contact, and hydration of lipid, lipidation site, and protein, aligning with the changes in the nanomorphology of FAMEs. These findings enable a better understanding of the biophysical consequence of lipidation in biology and the rational design of the biomaterials and therapeutics that rival the exquisite hierarchy and capabilities of biological systems.

Indexed as

ElastinIntrinsically Disordered ProteinsBiocompatible MaterialsBiotechnologyPeptidesTemperatureBiocompatible MaterialsElastinIntrinsically Disordered ProteinsPeptides

Identifiers

PMID36757021
PMCPMC10017028

What OpenQuestion holds

Textfull text, public
LicenceCC BY
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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.