Evidence map›Paper›PMID 19520860›Full record

ArticleThe Journal of biological chemistry2009

Designed beta-boomerang antiendotoxic and antimicrobial peptides: structures and activities in lipopolysaccharide.

Anirban Bhunia, Harini Mohanram, Prerna N Domadia, Jaume Torres, Surajit Bhattacharjya

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
3.0field-weighted citation impact, top 10% 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

42 citing papers in PubMed, 102 citations in OpenAlex.

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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

5 authors at 1 institution in 1 country.

Anirban BhuniaSchool of Biological Sciences, Division of Structural and Computational Biology, Nanyang Technological University, Singapore 637551.
Harini MohanramSchool of Biological Sciences, Division of Structural and Computational Biology, Nanyang Technological University, Singapore 637551.
Prerna N DomadiaSchool of Biological Sciences, Division of Structural and Computational Biology, Nanyang Technological University, Singapore 637551.
Jaume TorresSchool of Biological Sciences, Division of Structural and Computational Biology, Nanyang Technological University, Singapore 637551.
Surajit BhattacharjyaSchool of Biological Sciences, Division of Structural and Computational Biology, Nanyang Technological University, Singapore 637551.
Nanyang Technological University · SG

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lipopolysaccharide (LPS), an integral part of the outer membrane of Gram-negative bacteria, is involved in a variety of biological processes including inflammation, septic shock, and resistance to host-defense molecules. LPS also provides an environment for folding of outer membrane proteins. In this work, we describe the structure-activity correlation of a series of 12-residue peptides in LPS. NMR structures of the peptides derived in complex with LPS reveal boomerang-like beta-strand conformations that are stabilized by intimate packing between the two aromatic residues located at the 4 and 9 positions. This structural feature renders these peptides with a high ability to neutralize endotoxicity, >80% at 10 nM concentration, of LPS. Replacements of these aromatic residues either with Ala or with Leu destabilizes the boomerang structure with the concomitant loss of antiendotoxic and antimicrobial activities. Furthermore, the aromatic packing stabilizing the beta-boomerang structure in LPS is found to be maintained even in a truncated octapeptide, defining a structured LPS binding motif. The mode of action of the active designed peptides correlates well with their ability to perturb LPS micelle structures. Fourier transform infrared spectroscopy studies of the peptides delineate beta-type conformations and immobilization of phosphate head groups of LPS. Trp fluorescence studies demonstrated selective interactions with LPS and the depth of insertion into the LPS bilayer. Our results demonstrate the requirement of LPS-specific structures of peptides for endotoxin neutralizations. In addition, we propose that structures of these peptides may be employed to design proteins for the outer membrane.

Indexed as

Amino Acid MotifsAnti-Infective AgentsAntimicrobial Cationic PeptidesCell MembraneEndotoxinsHemagglutininsLipid BilayersLipopolysaccharidesMicellesMicrobial Sensitivity TestsPeptidesProtein ConformationProtein Structure, SecondarySpectrometry, FluorescenceSpectrophotometry, InfraredAnti-Infective AgentsAntimicrobial Cationic PeptidesEndotoxinsHemagglutininsLipid BilayersLipopolysaccharidesMicellesPeptides

Identifiers

PMID19520860
PMCPMC2755923
OpenAlexW1964927873

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.