Evidence map›Paper›PMID 20163089›Full record

ArticleThe journal of physical chemistry. B2010

Interactions of alamethicin with model cell membranes investigated using sum frequency generation vibrational spectroscopy in real time in situ.

Shuji Ye, Khoi Tan Nguyen, Zhan Chen

Open access · greenAbstract read
In one paragraph

Article in The journal of physical chemistry. B, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
6.3field-weighted citation impact, top 3% 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

25 citing papers in PubMed, 78 citations in OpenAlex.

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  9. Theoretical Sum Frequency Generation Spectroscopy of Peptides.The journal of physical chemistry. B · 2015
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  15. Dependence of Alamethicin Membrane Orientation on the Solution Concentration.The journal of physical chemistry. C, Nanomaterials and interfaces · 2013
    Article
  16. Article
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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

3 authors at 2 institutions in 2 countries.

Shuji YeDepartment of Chemistry, University of Michigan, Ann Arbor, Michigan 48109, USA.
Khoi Tan Nguyen
Zhan Chen
University of Science and Technology of China · CNUniversity of Michigan–Ann Arbor · US

Funding

SFG Investigation of Peptide and Protein Orientations in MembranesR01GM081655 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI CHEN, ZHAN · 2008 to 2012
$1.5M
NIGMS NIH HHS 1R01GM081655-01A2NIGMS NIH HHS R01 GM081655
6 · The paper itself

Abstract

Structures of membrane-associated peptides and molecular interactions between peptides and cell membrane bilayers govern biological functions of these peptides. Sum frequency generation (SFG) vibrational spectroscopy has been demonstrated to be a powerful technique to study such structures and interactions at the molecular level. In this research, SFG has been applied, supplemented by attenuated total reflectance Fourier transform infrared spectroscopy (ATR-FTIR), to characterize the interactions between alamethicin (a model for larger channel proteins) and different lipid bilayers in the absence of membrane potential. The orientation of alamethicin in lipid bilayers has been determined using SFG amide I spectra detected with different polarization combinations. It was found that alamethicin adopts a mixed alpha-helical and 3(10)-helical structure in fluid-phase lipid bilayers. The helix (mainly alpha-helix) at the N-terminus tilts at about 63 degrees versus the surface normal in a fluid-phase 1,2-dimyristoyl-d54-sn-glycero-3-phosphocholine-1,1,2,2-d4-N,N,N-trimethyl-d9 (d-DMPC)/1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) bilayer. The 3(10)-helix at the C-terminus (beyond the Pro14 residue) tilts at about 43 degrees versus the surface normal. This is the first time to apply SFG to study a 3(10)-helix experimentally. When interacting with a gel-phase lipid bilayer, alamethicin lies down on the gel-phase bilayer surface or aggregates or both, which does not have significant insertion into the lipid bilayer.

Indexed as

Models, MolecularAlamethicinDimyristoylphosphatidylcholineLipid BilayersPhosphatidylcholinesProtein Structure, SecondarySpectroscopy, Fourier Transform InfraredVibration1-palmitoyl-2-oleoylphosphatidylcholineAlamethicinDimyristoylphosphatidylcholineLipid BilayersPhosphatidylcholines

Identifiers

PMID20163089
PMCPMC2844632
OpenAlexW2048741757

What OpenQuestion holds

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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.