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.

The pleiotropic properties of LL-37 in relation to the different cells and tissues