Evidence map›Paper›PMID 23713839›Full record

ArticleBiomacromolecules2013

Peptide fibrils with altered stability, activity, and cell selectivity.

Long Chen, Jun F Liang

Abstract read
In one paragraph

Article in Biomacromolecules, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing 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

12 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Peptide oligomers from ultra-short peptides using sortase.Biochemistry and biophysics reports · 2017
    Article
  10. Article
  11. Article
  12. Bacteria responsive antibacterial surfaces for indwelling device infections.Journal of controlled release : official journal of the Controlled Release Society · 2015
    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.

Long ChenDepartment of Chemistry, Chemical Biology, and Biomedical Engineering, Charles V. Schaefer School of Engineering and Sciences, Stevens Institute of Technology, Hoboken, New Jersey 07030, United States.
Jun F Liang

Funding

Polymer Grafted Implant Surfaces with Biofilm Sensitizing AbilityR15AI072748 · NIAID · THE TRUSTEES OF THE STEVENS INSTITUTE OF TECHNOLOGY · PI LIANG, JUN F · 2007 to 2007
$218k
Membrane-Acting Lytic PeptidesR15GM081874 · NIGMS · THE TRUSTEES OF THE STEVENS INSTITUTE OF TECHNOLOGY · PI LIANG, JUN F · 2007 to 2007
$218k
NIAID NIH HHS AI072748NIAID NIH HHS R15 AI072748NIGMS NIH HHS GM081874NIGMS NIH HHS R15 GM081874
6 · The paper itself

Abstract

Peptides have some unique and superior features compared to proteins. However, the use of peptides as therapeutics is hampered by their low stability and cell selectivity. In this study, a new lytic peptide (CL-1, FLGALFRALSRLL) was constructed. Under the physiological condition, peptide CL-1 self-assembled into dynamically stable aggregates with fibrils-like structures. Aggregated CL-1 demonstrated dramatically altered activity and stability in comparison with single molecule CL-1 and other lytic peptides: when incubated with cocultured bacteria and tissue cells, CL-1 aggregates killed bacteria selectively but spared cocultured human cells; CL-1 aggregates were kept intact in human serum for more than five hours. Peptide-cell interaction studies performed on lipid monolayers and live human tissue cells revealed that in comparison with monomeric CL-1, aggregated CL-1 had decreased cell affinity and membrane insertion capability on tissue cells. A dynamic process involving aggregate dissociation and rearrangement seemed to be an essential step for membrane bound CL-1 aggregates to realize its cytotoxicity to tissue cells. Our study suggests that peptide aggregation could be as important as the charge and secondary structure of a peptide in affecting peptide-cell interactions. Controlling peptide self-assembly represents a new way to increase the stability and cell selectivity of bioactive peptides for wide biomedical applications.

Indexed as

Anti-Bacterial AgentsAntimicrobial Cationic PeptidesCell Line, TumorHumansHydrogen-Ion ConcentrationPeptide FragmentsAnti-Bacterial AgentsAntimicrobial Cationic PeptidesCL-1 lytic peptidePeptide Fragments

Identifiers

PMID23713839
PMCPMC4203308

What OpenQuestion holds

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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.