Evidence map›Paper›PMID 16500957›Full record

ArticleBiophysical journal2006

Orientation of a beta-hairpin antimicrobial peptide in lipid bilayers from two-dimensional dipolar chemical-shift correlation NMR.

Ming Tang, Alan J Waring, Robert I Lehrer, Mei Hong

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
2.5field-weighted citation impact, top 13% 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

10 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. The chemistry and biology of theta defensins.Angewandte Chemie (International ed. in English) · 2014
    Review
  3. Article
  4. Review
  5. θ-Defensins: cyclic peptides with endless potential.The Journal of biological chemistry · 2012
    Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. 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

4 authors at 2 institutions in 1 country.

Ming TangDepartment of Chemistry, Iowa State University, Ames, Iowa 50011, USA.
Alan J Waring
Robert I Lehrer
Mei Hong
Iowa State University · USUniversity of California, Los Angeles · 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
TOPICAL PROTEGRINS TO PREVENT STDS &HIV INFECTIONP01AI037945 · NIAID · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI LEHRER, ROBERT IRVING · 1995 to 2003
$3.1M
DEFENSINS--ANTIMICROBIAL PEPTIDES OF HUMAN NEUTROPHILSR37AI022839 · NIAID · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI LEHRER, ROBERT IRVING · 1993 to 2002
$1.1M
DEFENSINS: ANTIMICROBIAL PEPTIDES OF HUMAN NEUTROPHILSR01AI022839 · NIAID · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI LEHRER, ROBERT IRVING · 1986 to 1994
–
NIAID NIH HHS AI-22839NIAID NIH HHS AI-37945NIAID NIH HHS P01 AI037945NIGMS NIH HHS GM-066976NIGMS NIH HHS R01 GM066976
6 · The paper itself

Abstract

The orientation of a beta-sheet membrane peptide in lipid bilayers is determined, for the first time, using two-dimensional (2D) (15)N solid-state NMR. Retrocyclin-2 is a disulfide-stabilized cyclic beta-hairpin peptide with antibacterial and antiviral activities. We used 2D separated local field spectroscopy correlating (15)N-(1)H dipolar coupling with (15)N chemical shift to determine the orientation of multiply (15)N-labeled retrocyclin-2 in uniaxially aligned phosphocholine bilayers. Calculated 2D spectra exhibit characteristic resonance patterns that are sensitive to both the tilt of the beta-strand axis and the rotation of the beta-sheet plane from the bilayer normal and that yield resonance assignment without the need for singly labeled samples. Retrocyclin-2 adopts a transmembrane orientation in dilauroylphosphatidylcholine bilayers, with the strand axis tilted at 20 degrees +/- 10 degrees from the bilayer normal, but changes to a more in-plane orientation in thicker 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphatidyl-choline (POPC) bilayers with a tilt angle of 65 degrees +/- 15 degrees . These indicate that hydrophobic mismatch regulates the peptide orientation. The 2D spectra are sensitive not only to the peptide orientation but also to its backbone (phi, psi) angles. Neither a bent hairpin conformation, which is populated in solution, nor an ideal beta-hairpin with uniform (phi, psi) angles and coplanar strands, agrees with the experimental spectrum. Thus, membrane binding orders the retrocyclin conformation by reducing the beta-sheet curvature but does not make it ideal. (31)P NMR spectra of lipid bilayers with different compositions indicate that retrocyclin-2 selectively disrupts the orientational order of anionic membranes while leaving zwitteronic membranes intact. These structural results provide insights into the mechanism of action of this beta-hairpin antimicrobial peptide.

Indexed as

Membrane FluidityModels, ChemicalModels, MolecularAntimicrobial Cationic PeptidesComputer SimulationDefensinsLipid BilayersMagnetic Resonance SpectroscopyMembrane ProteinsPeptides, CyclicProtein ConformationAntimicrobial Cationic PeptidesDefensinsLipid BilayersMembrane ProteinsPeptides, Cyclicretrocyclin-2, human

Identifiers

PMID16500957
PMCPMC1440742
OpenAlexW2060408614

What OpenQuestion holds

Textmetadata
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.