Evidence map›Paper›PMID 23022591›Full record

ArticlePeptides2012

Insights into buforin II membrane translocation from molecular dynamics simulations.

Donald E Elmore

Abstract read
In one paragraph

Article in Peptides, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.1field-weighted citation impact, top 25% 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

13 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. Article
  8. Antimicrobial Peptide Mechanisms Studied by Whole-Cell Deuterium NMR.International journal of molecular sciences · 2022
    Review
  9. Review
  10. Review
  11. Article
  12. Article
  13. 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

1 author at 1 institution in 1 country.

Donald E ElmoreDepartment of Chemistry, Wellesley College, 106 Central St, Wellesley, MA 02481, United States. delmore@wellesley.edu
Wellesley College · US

Funding

Characterization and Design of Histone-Derived Antimicrobial PeptidesR15AI079685 · NIAID · WELLESLEY COLLEGE · PI ELMORE, DONALD E. · 2010 to 2015
$630k
NIAID NIH HHS R15 AI079685NIAID NIH HHS R15AI079685
6 · The paper itself

Abstract

Buforin II is a histone-derived antimicrobial peptide that readily translocates across lipid membranes without causing significant membrane permeabilization. Previous studies showed that mutating the sole proline of buforin II dramatically decreases its translocation. As well, researchers have proposed that the peptide crosses membranes in a cooperative manner by forming transient toroidal pores. This paper reports molecular dynamics simulations designed to investigate the structure of buforin II upon membrane entry and evaluate whether the peptide is able to form toroidal pore structures. These simulations showed a relationship between protein-lipid interactions and increased structural deformations of the buforin N-terminal region promoted by proline. Moreover, simulations with multiple peptides show how buforin II can embed deeply into membranes and potentially form toroidal pores. Together, these simulations provide structural insight into the translocation process for buforin II in addition to providing more general insight into the role proline can play in antimicrobial peptides.

Indexed as

Molecular Dynamics SimulationPhosphatidylcholinesProteins1-palmitoyl-2-oleoylphosphatidylcholinebuforin IIPhosphatidylcholinesProteins

Identifiers

PMID23022591
PMCPMC3513657
OpenAlexW1999924514

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.