Peptide reference
LL-37
Cathelicidin LL-37 ·Human cathelicidin antimicrobial peptide ·hCAP-18 (C-terminal fragment) ·CAMP gene product (mature peptide)
What cited sources report about LL-37
LL-37, also called cathelicidin LL-37 or human cathelicidin antimicrobial peptide, is the 37-amino-acid α-helical cationic peptide released from the C-terminus of hCAP-18 (the gene product of CAMP) by proteolytic processing. It is the only cathelicidin encoded in the human genome. The peptide is currently slated for FDA Pharmacy Compounding Advisory Committee (PCAC) review at a meeting in February 2027 (exact date pending). As of the cited literature, LL-37 has no FDA-approved indication and no marketing authorization in any major jurisdiction. The summaries below report what individual cited sources state; this page does not assert claims beyond what those sources report.
Ahmad et al. (2026) — Current Protein and Peptide Science
A review from the Faculty of Pharmacy at Integral University surveyed antimicrobial peptides, including cathelicidins such as LL-37, as candidate adjunctive therapies for multidrug- and extensively-drug-resistant tuberculosis. The authors observed that AMPs disrupt bacterial membranes and may modulate host immune responses including phagosome–lysosome fusion and autophagy, while noting that peptide stability and delivery remain barriers to clinical translation.
Many AMPs have shown strong antimycobacterial activity in vitro and in vivo, including defensins, cathelicidins (like LL-37), and synthetic analogues. Even with these encouraging outcomes, issues such as peptide stability and efficient delivery still stand in the way of clinical use.
Tanabe et al. (2026) — Journal of Oral Biosciences
A review from the Department of Oral Microbiology at Asahi University School of Dentistry catalogued LL-37 interactions with bacterial DNA in dental plaque. The authors described LL-37–bacterial-DNA complexes as nuclease-resistant aggregates that abrogate the peptide’s intrinsic antimicrobial activity while activating TLR9 and the NLRP3 inflammasome — framing LL-37 as a context-dependent dual-function peptide rather than a one-directional antimicrobial.
This dual nature of LL-37, whereby it acts as an antimicrobial peptide when alone, yet promotes biofilm formation and inflammation when complexed with bacterial DNA, sheds new light on the mechanisms underlying biofilm persistence and chronic inflammation.
Zhang et al. (2026) — Sheng Wu Gong Cheng Xue Bao (Chinese Journal of Biotechnology)
A 2026 review from the College of Veterinary Medicine at Southwest University surveyed porcine antimicrobial peptides — a family that includes cathelicidins structurally related to LL-37 — and characterized their immunomodulatory and antimicrobial mechanisms. The authors framed AMPs as candidates for anti-infective drug development given the growing limitations of conventional antibiotics.
Porcine antimicrobial peptides (AMPs) possess excellent antimicrobial activities and multiple biological functions, playing an essential role in the host’s innate immune defense against pathogen infections.
PubChem — LL-37
The PubChem compound entry/search results for LL-37 catalogue the 37-amino-acid cathelicidin antimicrobial peptide (mature C-terminal fragment of hCAP-18) and aggregate synonym sets and links to underlying chemical and biological literature.
Coverage notes
LL-37 has been the subject of a large preclinical literature and a small set of clinical trials registered on ClinicalTrials.gov (e.g., wound-healing and infection-related protocols), but no large registrational efficacy trial has yielded an FDA approval as of the last_updated date. The cited 2026 reviews observe that peptide stability and delivery remain practical barriers and that LL-37’s biology is dual — antimicrobial in some contexts and pro-inflammatory in others. This page will be updated when the February 2027 PCAC briefing materials are released.