Skip to content

Study · In vitro (cells) · 2010

4 results

Antibiotic-induced Porphyromonas gingivalis LPS release and inhibition of LPS-stimulated cytokines by antimicrobial peptides.

Walters SM, Dubey VS, Jeffrey NR, Dixon DR

Peptides10 Jun 2010Cited by 25 (Europe PMC)

Summary

The text of this summary is not shown here, because the article license does not allow reuse. Read it at the source (opens in a new tab)

Text rights: Publisher copyright. Results still quote short attributed sentences.

Results from this study4

4 results from studies that gave the peptide. No result from this study comes from people.

  1. 01LabIn vitro (cells)Activity measurement

    In whole blood stimulated with P. gingivalis LPS, LL‑37 inhibited TNF-alpha production and was the most potent of three antimicrobial peptides tested.

    In plain wordsIn lab tests with blood, LL‑37 lowered TNF-alpha caused by gum-bacteria toxin more than two other peptides did.

    Peptide
    LL-37
    Outcome
    DecreaseTNF-alpha production after P. gingivalis LPS
    Study

    humann: not reported in source

    Whole blood stimulated with purified P. gingivalis LPS
    Comparator
    Two other antimicrobial peptides
    Outcome group
    Inflammation markers · Immune and inflammation
    Studied dose
    Dose not stated

    Source sentences

    Summary
    Among the three AMPs tested, LL-37 was found to be the most potent inhibitor of cytokine (tumor necrosis factor-alpha, interleukin-1beta, interleukin-6) production and completely neutralized purified P. ginigivalis LPS activity in the chromogenic limulus amebocyte lysate (LAL) and whole blood cytoki…
    1 context sentence
    Summary · context
    Therefore, we examined the ability of various classes of antibiotics to induce LPS release from Porphyromonas gingivalis as well as the ability of antimicrobial peptides (AMPs) to inhibit purified LPS.
  2. 02LabIn vitro (cells)Activity measurement

    In whole blood stimulated with P. gingivalis LPS, LL‑37 inhibited interleukin-1beta production and was the most potent of three antimicrobial peptides tested.

    In plain wordsIn lab tests with blood, LL‑37 lowered IL-1beta caused by gum-bacteria toxin more than two other peptides did.

    Peptide
    LL-37
    Outcome
    DecreaseIL-1beta production after P. gingivalis LPS
    Study

    humann: not reported in source

    Whole blood stimulated with purified P. gingivalis LPS
    Comparator
    Two other antimicrobial peptides
    Outcome group
    Inflammation markers · Immune and inflammation
    Studied dose
    Dose not stated

    Source sentences

    Summary
    Among the three AMPs tested, LL-37 was found to be the most potent inhibitor of cytokine (tumor necrosis factor-alpha, interleukin-1beta, interleukin-6) production and completely neutralized purified P. ginigivalis LPS activity in the chromogenic limulus amebocyte lysate (LAL) and whole blood cytoki…
    1 context sentence
    Summary · context
    Therefore, we examined the ability of various classes of antibiotics to induce LPS release from Porphyromonas gingivalis as well as the ability of antimicrobial peptides (AMPs) to inhibit purified LPS.
  3. 03LabIn vitro (cells)Activity measurement

    In whole blood stimulated with P. gingivalis LPS, LL‑37 inhibited interleukin-6 production and was the most potent of three antimicrobial peptides tested.

    In plain wordsIn lab tests with blood, LL‑37 lowered IL-6 caused by gum-bacteria toxin more than two other peptides did.

    Peptide
    LL-37
    Outcome
    DecreaseIL-6 production after P. gingivalis LPS
    Study

    humann: not reported in source

    Whole blood stimulated with purified P. gingivalis LPS
    Comparator
    Two other antimicrobial peptides
    Outcome group
    Inflammation markers · Immune and inflammation
    Studied dose
    Dose not stated

    Source sentences

    Summary
    Among the three AMPs tested, LL-37 was found to be the most potent inhibitor of cytokine (tumor necrosis factor-alpha, interleukin-1beta, interleukin-6) production and completely neutralized purified P. ginigivalis LPS activity in the chromogenic limulus amebocyte lysate (LAL) and whole blood cytoki…
    1 context sentence
    Summary · context
    Therefore, we examined the ability of various classes of antibiotics to induce LPS release from Porphyromonas gingivalis as well as the ability of antimicrobial peptides (AMPs) to inhibit purified LPS.
  4. 04LabIn vitro (cell-free)Activity measurement

    In the limulus amebocyte lysate assay, LL‑37 completely neutralized purified P. gingivalis LPS activity.

    In plain wordsIn lab tests, LL‑37 completely neutralized the activity of toxin from a gum-disease bacterium.

    Peptide
    LL-37
    Outcome
    DecreaseNeutralisation of purified P. gingivalis LPS activity (LAL assay)
    Study

    n: not reported in source

    Chromogenic limulus amebocyte lysate assay
    Comparator
    Two other antimicrobial peptides
    Outcome group
    Inflammation markers · Immune and inflammation
    Studied dose
    Dose not stated

    Source sentences

    Summary
    completely neutralized purified P. ginigivalis LPS activity in the chromogenic limulus amebocyte lysate (LAL) and whole blood cytokine stimulation assays
    1 context sentence
    Summary · context
    Therefore, we examined the ability of various classes of antibiotics to induce LPS release from Porphyromonas gingivalis as well as the ability of antimicrobial peptides (AMPs) to inhibit purified LPS.

AI wrote and checked these results. AI can make mistakes, so check important results against the source.

Version history

PepBank keeps every version of the data on this study. Status changes from Retraction Watch, Europe PMC and Crossref are listed with their source.

  1. Version 3Current

    11 Oct 2026, 00:50 UTC

    Study results updated

  2. Version 2

    9 Oct 2026, 03:03 UTC

    Study data updated · source update from Europe PMC

  3. Version 1

    9 Oct 2026, 02:59 UTC

    First added · source update from Europe PMC

Subjects

Terms as the source lists them.

PepBank is a research reference. Talk to a doctor before you use any peptide.