Evidence map›Paper›PMID 39495202›Full record

ArticleBiomacromolecules2024

Genetically Engineered Liposwitch-Based Nanomaterials.

Md Shahadat Hossain, Alex Wang, Salma Anika, Zhe Zhang, Davoud Mozhdehi

Abstract read
In one paragraph

Article in Biomacromolecules, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
  2. Article
  3. 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

5 authors.

Md Shahadat HossainDepartment of Chemistry, Syracuse University, 111 College Place, Syracuse, New York 13244, United States.
Alex WangDepartment of Chemistry, Syracuse University, 111 College Place, Syracuse, New York 13244, United States.
Salma AnikaDepartment of Chemistry, Syracuse University, 111 College Place, Syracuse, New York 13244, United States.
Zhe ZhangDepartment of Chemistry, Syracuse University, 111 College Place, Syracuse, New York 13244, United States.
Davoud MozhdehiDepartment of Chemistry, Syracuse University, 111 College Place, Syracuse, New York 13244, United States.ORCID 0000-0002-3440-8878

Funding

Genetically Encoded Lipidation to Manipulate Structure, Assembly, and Phase Behavior of ProteinsR35GM142899 · NIGMS · SYRACUSE UNIVERSITY · PI MOZHDEHI , DAVOUD · 2021 to 2025
$1.8M
Zeiss LSM 980 with Airyscan2 microscope and Fast Mode for live cell and enhanced resolution imagingS10OD026946 · OD · SYRACUSE UNIVERSITY · PI PEPLING, MELISSA E · 2020 to 2020
$584k
NIGMS NIH HHS R35 GM142899NIH HHS S10 OD026946
6 · The paper itself

Abstract

Fusion of intrinsically disordered and globular proteins is a powerful strategy to create functional nanomaterials. However, the immutable nature of genetic encoding restricts the dynamic adaptability of nanostructures postexpression. To address this, we envisioned using a myristoyl switch, a protein that combines allostery and post-translational modifications─two strategies that modify protein properties without altering their sequence─to regulate intrinsically disordered protein (IDP)-driven nanoassembly. A typical myristoyl switch, allosterically activated by a stimulus, reveals a sequestered lipid for membrane association. We hypothesize that this conditional exposure of lipids can regulate the assembly of fusion proteins, a concept we term "liposwitching". We tested this by fusing recoverin, a calcium-dependent myristoyl switch, with elastin-like polypeptide, a thermoresponsive model IDP. Biophysical analyses confirmed recoverin's myristoyl-switch functionality, while dynamic light scattering and cryo-transmission electron microscopy showed distinct calcium- and lipidation-dependent phase separation and assembly. This study highlights liposwitching as a viable strategy for controlling DP-driven nanoassembly, enabling applications in synthetic biology and cellular engineering.

Indexed as

Intrinsically Disordered ProteinsNanostructuresCalciumElastinGenetic EngineeringPeptidesProtein Processing, Post-TranslationalRecombinant Fusion ProteinsCalciumElastinIntrinsically Disordered ProteinsPeptidesRecombinant Fusion Proteins

Identifiers

PMID39495202
PMCPMC11632658

What OpenQuestion holds

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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.