Evidence map›Paper›PMID 18375755›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2008

Mechanism and kinetics of pore formation in membranes by water-soluble amphipathic peptides.

Ming-Tao Lee, Wei-Chin Hung, Fang-Yu Chen, Huey W Huang

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 112 papers.

0numbers the graph read from it
0cells of the map it votes in
112citing papers in PubMed
–field-weighted citation impact
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

112 citing papers in PubMed.

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  15. Interaction of βInternational journal of molecular sciences · 2023
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52 more citing papers are in PubMed but not listed here.

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.

Ming-Tao LeeNational Synchrotron Radiation Research Center, Hsinchu 30076, Taiwan.
Wei-Chin Hung
Fang-Yu Chen
Huey W Huang

Funding

Membrane-active Peptides and ProteinsR01GM055203 · NIGMS · RICE UNIVERSITY · PI HUANG, HUEY W. · 1997 to 2017
$5.0M
NIGMS NIH HHS GM55203NIGMS NIH HHS R01 GM055203
6 · The paper itself

Abstract

How antimicrobial peptides form pores in membranes is of interest as a fundamental membrane process. However, the underlying molecular mechanism, which has potential applications in therapeutics, nonviral gene transfer, and drug delivery, has been in dispute. We have resolved this mechanism by observing the time-dependent process of pore formation in individual giant unilamellar vesicles (GUVs) exposed to a melittin solution. An individual GUV first expanded its surface area at constant volume and then suddenly reversed to expanding its volume at constant area. The area expansion, the volume expansion, and the point of reversal all match the results of equilibrium measurements performed on peptide-lipid mixtures. The mechanism includes a negative feedback that makes peptide-induced pores stable with a well defined size, contrary to the suggestion that peptides disintegrate the membrane in a detergent-like manner.

Indexed as

Hydrophobic and Hydrophilic InteractionsKineticsMelittenPorositySolubilityUnilamellar LiposomesWaterX-Ray DiffractionMelittenUnilamellar LiposomesWater

Identifiers

PMID18375755
PMCPMC2278198

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.