Evidence map›Paper›PMID 19396367›Full record

ReviewMolecular bioSystems2009

Structure and mechanism of beta-hairpin antimicrobial peptides in lipid bilayers from solid-state NMR spectroscopy.

Ming Tang, Mei Hong

Open access · greenAbstract readReview
In one paragraph

Review in Molecular bioSystems, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
–field-weighted citation impact, top 93% 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

40 citing papers in PubMed, 83 citations in OpenAlex.

  1. Review
  2. Review
  3. Combating Bacterial Infections with Vitamin D-Induced Antimicrobial Peptides.Advances in experimental medicine and biology · 2026
    Review
  4. Solid-State NMR of Virus Membrane Proteins.Accounts of chemical research · 2025
    Article
  5. Article
  6. Article
  7. Synthesis and Biological Evaluation of NewMolecules (Basel, Switzerland) · 2021
    Article
  8. Review
  9. Rediscovery of antimicrobial peptides as therapeutic agents.Journal of microbiology (Seoul, Korea) · 2021
    Review
  10. Antimicrobial Mechanism of pBD2 againstMolecules (Basel, Switzerland) · 2020
    Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Review
  16. Review
  17. Article
  18. Article
  19. Computational prediction of the optimal oligomeric state for membrane-inserted β-barrels of protegrin-1 and related mutants.Journal of peptide science : an official publication of the European Peptide Society · 2017
    Article
  20. Mechanism of Four de Novo Designed Antimicrobial Peptides.The Journal of biological chemistry · 2016
    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

2 authors at 1 institution in 1 country.

Ming TangDepartment of Chemistry, Iowa State University, Ames, IA 50011, USA.
Mei Hong
Iowa State University · US

Funding

Structures and lipid interactions of curvature-inducing membrane peptides by NMRR01GM066976 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI HONG, MEI · 2003 to 2021
$4.8M
NIGMS NIH HHS GM066976NIGMS NIH HHS R01 GM066976
6 · The paper itself

Abstract

The membrane-bound structure, lipid interaction, and dynamics of the arginine-rich beta-hairpin antimicrobial peptide PG-1 as studied by solid-state NMR are highlighted here. A variety of solid-state NMR techniques, including paramagnetic relaxation enhancement, (1)H and (19)F spin diffusion, dipolar recoupling distance experiments, and 2D anisotropic-isotropic correlation experiments, are used to elucidate the structural basis for the membrane disruptive activity of this representative beta-hairpin antimicrobial peptide. We found that PG-1 structure is membrane dependent: in bacteria-mimetic anionic lipid membranes the peptide forms oligomeric transmembrane beta-barrels, whereas in cholesterol-rich membranes mimicking eukaryotic cells the peptide forms beta-sheet aggregates on the surface of the bilayer. PG-1 causes toroidal pore defects in the anionic membrane, suggesting that the cationic arginine residues drag the lipid phosphate groups along as the peptide inserts. Mutation of PG-1 to reduce the number of cationic residues or to change the arginine guanidinium structure significantly changes the degree of insertion and orientation of the peptide in the lipid membrane, resulting in much weaker antimicrobial activities.

Indexed as

Amino Acid SequenceAnimalsAntimicrobial Cationic PeptidesHumansLipid BilayersModels, BiologicalModels, MolecularMolecular Sequence DataNuclear Magnetic Resonance, BiomolecularProtein ConformationStructure-Activity RelationshipAntimicrobial Cationic PeptidesLipid Bilayers

Identifiers

PMID19396367
PMCPMC2866158
OpenAlexW2005568374

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.