Evidence map›Paper›PMID 37801850›Full record

ArticleJournal of colloid and interface science2024

Characterization of nanodisc-forming peptides for membrane protein studies.

Bankala Krishnarjuna, Gaurav Sharma, Sang-Choul Im, Richard Auchus, G M Anantharamaiah, Ayyalusamy Ramamoorthy

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of colloid and interface science, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.8field-weighted citation impact, top 16% of its field
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

9 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
  2. Molecular Mechanisms Governing Peptide Nanodisc Assembly and Stability.bioRxiv : the preprint server for biology · 2026
    Article
  3. The Nanodisc System for Investigating Protein-Lipid Interactions.Methods in molecular biology (Clifton, N.J.) · 2026
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Nanodiscs for the study of membrane proteins.Current opinion in structural biology · 2024
    Review
  9. 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 at 2 institutions in 1 country.

Bankala KrishnarjunaBiophysics Program, Department of Chemistry, Biomedical Engineering, Macromolecular Science and Engineering, University of Michigan, Arbor, MI 48109, USA.
Gaurav SharmaBiophysics Program, Department of Chemistry, Biomedical Engineering, Macromolecular Science and Engineering, University of Michigan, Arbor, MI 48109, USA.
Sang-Choul ImDepartment of Pharmacology and Internal Medicine, Division of Metabolism, Endocrinology, & Diabetes, University of Michigan, Ann Arbor, MI 48109, USA.
Richard AuchusDepartment of Pharmacology and Internal Medicine, Division of Metabolism, Endocrinology, & Diabetes, University of Michigan, Ann Arbor, MI 48109, USA.
G M AnantharamaiahDepartment of Medicine, University of Alabama at Birmingham Medical Center, Birmingham, AL 35294, USA.
Ayyalusamy RamamoorthyBiophysics Program, Department of Chemistry, Biomedical Engineering, Macromolecular Science and Engineering, University of Michigan, Arbor, MI 48109, USA; National High Magnetic Field Laboratory, Department of Chemical and Biomedical Engineering, Tallahassee, FL 32310, USA. Electronic address: ramamoor@umich.edu.
University of Michigan · USUniversity of Alabama at Birmingham · US

Funding

Dynamics, Regulation and Function of p53 in Single CellsR35GM139572 · NIGMS · HARVARD MEDICAL SCHOOL · PI Galit Lahav · 2021 to 2026
$4.7M
Development of biophysical approaches to investigate high-resolution structure and dynamics of membrane proteinsR35GM139573 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Ayyalusamy Ramamoorthy · 2021 to 2026
$2.0M
NIGMS NIH HHS R35 GM139572NIGMS NIH HHS R35 GM139573
6 · The paper itself

Abstract

Lipid-bilayer nanodiscs provide a stable, native-like membrane environment for the functional and structural studies of membrane proteins and other membrane-binding molecules. Peptide-based nanodiscs having unique properties are developed for membrane protein studies and other biological applications. While the self-assembly process rendering the formation of peptide-nanodiscs is attractive, it is important to understand the stability and suitability of these nanodisc systems for membrane protein studies. In this study, we investigated the nanodiscs formation by the anti-inflammatory and tumor-suppressing peptide AEM28. AEM28 is a chimeric peptide containing a cationic-rich heparan sulfate proteoglycan- (HSPG)-binding domain from human apolipoprotein E (hapoE) (141-150) followed by the 18A peptide's amino acid sequence. AEM28-based nanodiscs made with different types of lipids were characterized using various biophysical techniques and compared with the nanodiscs formed using 2F or 4F peptides. Variable temperature dynamic light-scattering and

Indexed as

Membrane ProteinsNanostructuresEscherichia coliHumansLipid BilayersPeptidesLipid BilayersMembrane ProteinsPeptidesAEM28Cell membrane solubilizationNanodisc fusionNMRP450-CPR redox complexPeptide:lipid interactionPeptide nanodisc

Identifiers

PMID37801850
PMCPMC10864042
OpenAlexW4387122519

What Socratic 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 Socratic graph.