LL-37
LL-37 is a peptide, indexed here under Tissue repair peptides.
Identity
| Field | Value |
|---|---|
| Classification | Peptide |
| Primary class | Tissue repair peptides |
| CAS registry number | 154947-66-7[1] |
| PubChem CID | 16198951[1] |
| UniProt accession | Unknown No UniProt query was run in v1. |
| Molecular formula | C205H340N60O53[1] |
| Molecular weight | 4493 g/mol[1] |
| Amino-acid sequence | Unknown Not reported by the PubChem property set retrieved for this record; no sequence database query was run in v1. |
| Reported half-life | Unknown No pharmacokinetics source was retrieved in v1. PubChem does not carry half-life as a property, so this is recorded as not yet sourced rather than estimated. |
What the cited literature examines
LL-37 is described in a 2006 Biochimica et Biophysica Acta review as the only human member of the cathelicidin family of antimicrobial peptides. A 2001 Blood paper reports that its precursor hCAP-18 is processed to LL-37 by extracellular cleavage with proteinase 3, a 1998 Antimicrobial Agents and Chemotherapy paper reports its activities as a cathelin-associated antimicrobial peptide of human neutrophils, and a 2008 Infection and Immunity paper reports an effect on bacterial biofilm formation.
The rest of the retrieved set concerns expression and immune signalling. A 1997 Journal of Biological Chemistry paper reports induction of the gene in human keratinocytes during inflammation, a 1998 Proceedings of the National Academy of Sciences paper reports expression in epithelia of the human lung, a 2000 Blood paper reports expression by lymphocyte and monocyte populations, a 2000 Journal of Experimental Medicine paper reports that it uses formyl peptide receptor-like 1, a 2002 Journal of Immunology paper describes it as a multifunctional modulator of innate immune responses, a 2003 Journal of Clinical Investigation paper reports an angiogenic role, and a 2010 Stem Cells paper reports its secretion by mesenchymal stem cells.
[3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13]Reported mechanism
A human cathelicidin antimicrobial peptide; the retrieved records report direct antimicrobial activity and signalling through formyl peptide receptor-like 1.
[5, 10]Stated in the titles of the cited 1998 Antimicrobial Agents and Chemotherapy and 2000 Journal of Experimental Medicine papers.
Targets named in the cited records: bacterial membranes, formyl peptide receptor-like 1.
FDA application register
A query of the FDA Drugs@FDA application register on 2026-10-09 returned no application records for this compound name. This compound is not approved by the FDA for human use.[2]
Scope statement: this records the result of a single automated query against the openFDA drugsfda endpoint on the stated date. It is not legal advice and is not a jurisdiction-by-jurisdiction legality assessment.
Retrieved 2026-10-09.
Amounts reported in the cited literature
Unknown. No retrieved record in this dataset states an amount, so none is shown. Where an amount is recorded it is what a named study reported administering in its own stated model, in the past tense, and is not a protocol.
No study-reported dose was taken from a source read in v1. Literature-reported values are only recorded where the retrieved citation metadata states the figure.
Adverse effects reported in the cited literature
Unknown. No retrieved record in this dataset reports an adverse effect for this compound, so no row is shown. Absence of a row records the absence of a retrieved report, nothing more.
No adverse-effect row was taken from a source read in v1. Rows are only recorded with the study model named and the reporting citation attached.
Other names
LL-37 appears under these other names in the cited records or in common usage. Each one resolves to this page rather than to a separate page of its own.
- cathelicidin LL-37
- hCAP-18 derived peptide
- human cathelicidin
Where this page sits
Research records
Cited research records for LL-37, each with its identifier, the publication type it is indexed as, and the study model stated by its assigned subject headings.
Compounds indexed next to it
- KPV — Tissue repair peptides
- Thymosin beta 4 — Tissue repair peptides
Class page: Tissue repair peptides. Full index: all indexed compounds.
Questions this page answers
What does the cited literature examine for LL-37?
LL-37 is described in a 2006 Biochimica et Biophysica Acta review as the only human member of the cathelicidin family of antimicrobial peptides. A 2001 Blood paper reports that its precursor hCAP-18 is processed to LL-37 by extracellular cleavage with proteinase 3, a 1998 Antimicrobial Agents and Chemotherapy paper reports its activities as a cathelin-associated antimicrobial peptide of human neutrophils, and a 2008 Infection and Immunity paper reports an effect on bacterial biofilm formation.
Which class is LL-37 indexed under?
LL-37 is indexed under Tissue repair peptides. This grouping covers peptides whose retrieved research literature is predominantly concerned with tissue repair endpoints in laboratory and animal models, rather than a single shared receptor.
What does the FDA application register show for LL-37?
A query of the FDA Drugs@FDA application register on 2026-10-09 returned no application records for this compound name. This compound is not approved by the FDA for human use.
Sources
- PubChem Compound Summary for CID 16198951, LL-37. PubChem, National Library of Medicine (2026). pubchem:16198951
- Drugs@FDA application register query for this compound, no application records returned. U.S. Food and Drug Administration, openFDA drugsfda endpoint (2026). fda:ll-37
- LL-37, the only human member of the cathelicidin family of antimicrobial peptides. Biochimica et biophysica acta (2006). pmid:16716248
- Human cathelicidin, hCAP-18, is processed to the antimicrobial peptide LL-37 by extracellular cleavage with proteinase 3. Blood (2001). pmid:11389039
- Activities of LL-37, a cathelin-associated antimicrobial peptide of human neutrophils. Antimicrobial agents and chemotherapy (1998). pmid:9736536
- Human host defense peptide LL-37 prevents bacterial biofilm formation. Infection and immunity (2008). pmid:18591225
- The expression of the gene coding for the antibacterial peptide LL-37 is induced in human keratinocytes during inflammatory disorders. The Journal of biological chemistry (1997). pmid:9182550
- The peptide antibiotic LL-37/hCAP-18 is expressed in epithelia of the human lung where it has broad antimicrobial activity at the airway surface. Proceedings of the National Academy of Sciences of the United States of America (1998). pmid:9689116
- The human antimicrobial and chemotactic peptides LL-37 and alpha-defensins are expressed by specific lymphocyte and monocyte populations. Blood (2000). pmid:11049988
- LL-37, the neutrophil granule- and epithelial cell-derived cathelicidin, utilizes formyl peptide receptor-like 1 (FPRL1) as a receptor to chemoattract human peripheral blood neutrophils, monocytes, and T cells. The Journal of experimental medicine (2000). pmid:11015447
- The human antimicrobial peptide LL-37 is a multifunctional modulator of innate immune responses. Journal of immunology (Baltimore, Md. : 1950) (2002). pmid:12244186
- An angiogenic role for the human peptide antibiotic LL-37/hCAP-18. The Journal of clinical investigation (2003). pmid:12782669
- Antibacterial effect of human mesenchymal stem cells is mediated in part from secretion of the antimicrobial peptide LL-37. Stem cells (Dayton, Ohio) (2010). pmid:20945332
On each stated value was matched to the record cited for it. That is record matching, not an appraisal of the research. Compiled and checked by: Peptide Monographs editorial desk. No qualified clinical reviewer.