Cathelicidin antimicrobial peptide

In humans, CAMP encodes the peptide precursor CAP-18 (18 kDa), which is processed by proteinase 3-mediated extracellular cleavage into the active form LL-37.

Cathelicidins thus serve a critical role in mammalian innate immune defense against invasive bacterial infection.

Whilst the defensins share common structural features, cathelicidin-related peptides are highly heterogeneous.

[4] Cathelicidins rapidly destroy the lipoprotein membranes of microbes enveloped in phagosomes after fusion with lysosomes in macrophages.

[12] LL-37 plays a role in the activation of cell proliferation and migration, contributing to the wound closure process.

Additionally cathelicidins may also be small-sized molecules (12-18 residues) with beta-hairpin structures, stabilized by one or two disulphide bonds.

[5] In 1995, Gudmundsson et al. assumed that the active antimicrobial peptide is formed of a 39-residue C-terminal domain (termed FALL-39).

[29] Lower plasma levels of human cathelicidin antimicrobial protein (hCAP18) appear to significantly increase the risk of death from infection in dialysis patients.

In psoriasis, damaged keratinocytes release LL-37 which forms complexes with self-genetic material (DNA or RNA) from other cells.

Chronic, oral Porphyromonas gingivalis, and herpesvirus (HSV-1) infections may contribute to the progression of Alzheimer's dementia.

Despite sustained interest, treatments derived or utilizing AMPs have not been widely adopted for clinical use for several reasons.