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Study · Not a test of the peptide alone · 2021

5 results

Antimicrobial Activities of LL-37 Fragment Mutant-Poly (Lactic-Co-Glycolic) Acid Conjugate against Staphylococcus aureus, Escherichia coli, and Candida albicans.

Mori T, Yoshida M, Hazekawa M, Ishibashi D, Hatanaka Y, Nagao T, Kakehashi R, Kojima H, Uno R, Ozeki M, Kawasaki I, Yamashita T, Nishikawa J, Uchida T

International journal of molecular sciences12 May 2021Cited by 10 (Europe PMC)

PMID34065861 (opens in a new tab)PMCIDPMC8151943 (opens in a new tab)DOI10.3390/ijms22105097 (opens in a new tab)PepBankPUB-34065861
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Summary

Various peptides and their derivatives have been reported to exhibit antimicrobial activities. Although these activities have been examined against microorganisms, novel methods have recently emerged for conjugation of the biomaterials to improve their activities. Here, we prepared CKR12-PLGA, in which CKR12 (a mutated fragment of human cathelicidin peptide, LL-37) was conjugated with poly (lactic-co-glycolic) acid (PLGA), and compared the antimicrobial and antifungal activities of the conjugated peptide with those of FK13 (a small fragment of LL-37) and CKR12 alone. The prepared CKR12-PLGA was characterized by dynamic light scattering and measurement of the zeta potential, critical micellar concentration, and antimicrobial activities of the fragments and conjugate. Although CKR12 showed higher antibacterial activities than FK13 against Staphylococcus aureus and Escherichia coli, the antifungal activity of CKR12 was lower than that of FK13. CKR12-PLGA showed higher antibacterial activities against S. aureus and E. coli and higher antifungal activity against Candida albicans compared to those of FK13. Additionally, CKR12-PLGA showed no hemolytic activity in erythrocytes, and scanning and transmission electron microscopy suggested that CKR12-PLGA killed and disrupted the surface structure of microbial cells. Conjugation of antimicrobial peptide fragment analogues was a successful approach for obtaining increased microbial activity with minimized cytotoxicity.
CC BYText from Europe PMC. Highlighted sentences are the source of results.

Results from this study5

No result from this study comes from a test of the peptide.

Studies that did not test the peptide alone5

In this study, LL-37 was a lab tool or a carrier, part of a mix, or the subject of a lab method. These results are not evidence about taking LL-37.

  1. 01LabNot a test of LL-37 aloneIn vitro (cells)Activity measurement

    In lab tests, the LL‑37 fragment mutant CKR12 had higher antibacterial activity than the fragment FK13 against S. aureus and E. coli.

    In plain wordsIn lab tests, an LL‑37 fragment variant killed S. aureus and E. coli bacteria better than another LL‑37 fragment, FK13.

    Peptide
    LL-37
    Outcome
    IncreaseAntibacterial activity of CKR12 versus FK13
    Study

    n: not reported in source

    S. aureus, E. coli and C. albicans in vitro
    Comparator
    FK13
    Outcome group
    Infection and antimicrobial activity · Infection

    Source sentences

    Summary
    Although CKR12 showed higher antibacterial activities than FK13 against Staphylococcus aureus and Escherichia coli
    1 context sentence
    Summary · context
    Here, we prepared CKR12-PLGA, in which CKR12 (a mutated fragment of human cathelicidin peptide, LL-37) was conjugated with poly (lactic-co-glycolic) acid (PLGA), and compared the antimicrobial and antifungal activities of the conjugated peptide with those of FK13 (a small fragment of LL-37) and CKR12 alone.

    In this study, LL-37 was a lab tool or a carrier, part of a mix, or the subject of a lab method. This result is not evidence about taking LL-37.

  2. 02LabNot a test of LL-37 aloneIn vitro (cells)Activity measurement

    In lab tests, the antifungal activity of CKR12 was lower than that of FK13.

    In plain wordsIn lab tests, the LL‑37 fragment variant CKR12 worked less well against fungus than the fragment FK13.

    Peptide
    LL-37
    Outcome
    DecreaseAntifungal activity of CKR12 versus FK13
    Study

    n: not reported in source

    S. aureus, E. coli and C. albicans in vitro
    Comparator
    FK13
    Outcome group
    Infection and antimicrobial activity · Infection

    Source sentences

    Summary
    the antifungal activity of CKR12 was lower than that of FK13.
    1 context sentence
    Summary · context
    Here, we prepared CKR12-PLGA, in which CKR12 (a mutated fragment of human cathelicidin peptide, LL-37) was conjugated with poly (lactic-co-glycolic) acid (PLGA), and compared the antimicrobial and antifungal activities of the conjugated peptide with those of FK13 (a small fragment of LL-37) and CKR12 alone.

    In this study, LL-37 was a lab tool or a carrier, part of a mix, or the subject of a lab method. This result is not evidence about taking LL-37.

  3. 03LabNot a test of LL-37 aloneIn vitro (cells)Activity measurement

    In lab tests, the CKR12-PLGA conjugate showed higher antibacterial activity against S. aureus and E. coli and higher antifungal activity against C. albicans than FK13.

    In plain wordsIn lab tests, an LL‑37 fragment joined to PLGA killed bacteria and fungus better than the fragment FK13.

    Peptide
    LL-37
    Outcome
    IncreaseAntibacterial and antifungal activity of CKR12-PLGA versus FK13
    Study

    n: not reported in source

    S. aureus, E. coli and C. albicans in vitro
    Comparator
    FK13
    Outcome group
    Infection and antimicrobial activity · Infection

    Source sentences

    Summary
    CKR12-PLGA showed higher antibacterial activities against S. aureus and E. coli and higher antifungal activity against Candida albicans compared to those of FK13.
    1 context sentence
    Summary · context
    Here, we prepared CKR12-PLGA, in which CKR12 (a mutated fragment of human cathelicidin peptide, LL-37) was conjugated with poly (lactic-co-glycolic) acid (PLGA), and compared the antimicrobial and antifungal activities of the conjugated peptide with those of FK13 (a small fragment of LL-37) and CKR12 alone.

    In this study, LL-37 was a lab tool or a carrier, part of a mix, or the subject of a lab method. This result is not evidence about taking LL-37.

  4. 04LabNot a test of LL-37 aloneIn vitro (cells)Safety outcome

    In lab tests, the CKR12-PLGA conjugate showed no hemolytic activity in erythrocytes.

    In plain wordsIn lab tests, the LL‑37 fragment conjugate did not damage red blood cells.

    Peptide
    LL-37
    Outcome
    No significant changeHemolytic activity of CKR12-PLGA
    Study

    n: not reported in source

    S. aureus, E. coli and C. albicans in vitro
    Outcome group
    Adverse events · Pharmacology

    Source sentences

    Summary
    CKR12-PLGA showed no hemolytic activity in erythrocytes
    1 context sentence
    Summary · context
    Here, we prepared CKR12-PLGA, in which CKR12 (a mutated fragment of human cathelicidin peptide, LL-37) was conjugated with poly (lactic-co-glycolic) acid (PLGA), and compared the antimicrobial and antifungal activities of the conjugated peptide with those of FK13 (a small fragment of LL-37) and CKR12 alone.

    In this study, LL-37 was a lab tool or a carrier, part of a mix, or the subject of a lab method. This result is not evidence about taking LL-37.

  5. 05LabNot a test of LL-37 aloneIn vitro (cells)Mechanism

    Scanning and transmission electron microscopy suggested that the CKR12-PLGA conjugate killed microbial cells and disrupted their surface structure.

    In plain wordsIn lab tests, electron microscopy suggested the LL‑37 fragment conjugate killed microbes and damaged their surface.

    Peptide
    LL-37
    Outcome
    Not applicableMicrobial cell disruption by CKR12-PLGA
    Study

    n: not reported in source

    S. aureus, E. coli and C. albicans in vitro
    Outcome group
    Infection and antimicrobial activity · Infection

    Source sentences

    Summary
    scanning and transmission electron microscopy suggested that CKR12-PLGA killed and disrupted the surface structure of microbial cells.
    1 context sentence
    Summary · context
    Here, we prepared CKR12-PLGA, in which CKR12 (a mutated fragment of human cathelicidin peptide, LL-37) was conjugated with poly (lactic-co-glycolic) acid (PLGA), and compared the antimicrobial and antifungal activities of the conjugated peptide with those of FK13 (a small fragment of LL-37) and CKR12 alone.

    In this study, LL-37 was a lab tool or a carrier, part of a mix, or the subject of a lab method. This result is not evidence about taking LL-37.

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, 02:56 UTC

    First added · source update from Europe PMC

Subjects

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