Evidence map›Paper›PMID 37989570›Full record

ArticleJournal of the American Chemical Society2023

How Cell-Penetrating Peptides Behave Differently from Pore-Forming Peptides: Structure and Stability of Induced Transmembrane Pores.

Haleh Alimohamadi, Jaime de Anda, Michelle W Lee, Nathan W Schmidt, Taraknath Mandal, Gerard C L Wong

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

11 citing papers in PubMed, 16 citations in OpenAlex.

  1. Review
  2. Review
  3. SARS-CoV-2 peptide fragments selectively dysregulate specific immune cell populations via Gaussian curvature targeting.Proceedings of the National Academy of Sciences of the United States of America · 2026
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 3 institutions in 2 countries.

Haleh AlimohamadiDepartment of Bioengineering, University of California, Los Angeles, Los Angeles, California 90025, United States.ORCID 0000-0001-6576-2426
Jaime de AndaDepartment of Bioengineering, University of California, Los Angeles, Los Angeles, California 90025, United States.ORCID 0000-0003-2129-0775
Michelle W LeeDepartment of Bioengineering, University of California, Los Angeles, Los Angeles, California 90025, United States.ORCID 0000-0003-1613-9501
Nathan W SchmidtDepartment of Bioengineering, University of California, Los Angeles, Los Angeles, California 90025, United States.
Taraknath MandalDepartment of Physics, Indian Institute of Technology Kanpur, Kanpur 208016, India.
Gerard C L WongDepartment of Bioengineering, University of California, Los Angeles, Los Angeles, California 90025, United States.ORCID 0000-0003-0893-6383
California NanoSystems Institute · USUniversity of California, Los Angeles · USIndian Institute of Technology Kanpur · IN

Funding

A Synchrotron Radiation Structural Biology ResourcesP30GM133894 · NIGMS · STANFORD UNIVERSITY · PI Aina E. Cohen, KEITH O HODGSON · 2020 to 2026
$43.3M
Vascular Biology Training GrantT32HL069766 · NHLBI · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI LUSIS, ALDONS JAKE · 2002 to 2022
$7.4M
American Heart Association-American Stroke Association 966662NHLBI NIH HHS T32 HL069766NIGMS NIH HHS P30 GM133894
6 · The paper itself

Abstract

Peptide-induced transmembrane pore formation is commonplace in biology. Examples of transmembrane pores include pores formed by antimicrobial peptides (AMPs) and cell-penetrating peptides (CPPs) in bacterial membranes and eukaryotic membranes, respectively. In general, however, transmembrane pore formation depends on peptide sequences, lipid compositions, and intensive thermodynamic variables and is difficult to observe directly under realistic solution conditions, with structures that are challenging to measure directly. In contrast, the structure and phase behavior of peptide-lipid systems are relatively straightforward to map out experimentally for a broad range of conditions. Cubic phases are often observed in systems involving pore-forming peptides; however, it is not clear how the structural tendency to induce negative Gaussian curvature (NGC) in such phases is quantitatively related to the geometry of biological pores. Here, we leverage the theory of anisotropic inclusions and devise a facile method to estimate transmembrane pore sizes from geometric parameters of cubic phases measured from small-angle X-ray scattering (SAXS) and show that such estimates compare well with known pore sizes. Moreover, our model suggests that although AMPs can induce stable transmembrane pores for membranes with a broad range of conditions, pores formed by CPPs are highly labile, consistent with atomistic simulations.

Indexed as

Cell-Penetrating PeptidesAmino Acid SequenceLipid BilayersScattering, Small AngleX-Ray DiffractionCell-Penetrating PeptidesLipid Bilayers

Identifiers

PMID37989570
PMCPMC11870675
OpenAlexW4388880320

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.