Keratin-derived antimicrobial peptides (KAMPs)

Keratinocyte-associated membrane components, specifically Keratin-derived antimicrobial peptides (KAMPs), are unique human antimicrobial peptides derived from the proteolytic processing of Keratin 6A (K6a) in epithelial cells. Unlike canonical antimicrobial peptides like defensins, KAMPs are salt-tolerant and utilize a non-alpha-beta structure characterized by flexible glycine-rich motifs to disrupt bacterial membranes. They are constitutively expressed in the human corneal epithelium and are significantly upregulated during infection or wound healing through a process involving K6a phosphorylation and ubiquitin-proteasomal processing. KAMPs exhibit potent bactericidal activity against major pathogens such as Pseudomonas aeruginosa and Staphylococcus aureus, making them a significant component of the innate immune defense of the ocular surface and other epithelia. Research suggests that manipulating the pathways that produce KAMPs, such as the activity of cullin-RING E3 ligases or the proteasome, could offer novel therapeutic strategies for treating recalcitrant infections and promoting epithelial repair.

Other names

Keratinocyte-associated membrane proteinKeratin 6A fragmentsKAMP-19KAMP-10KAMP-18CKAMP-36

KAMPs exert bactericidal effects by inducing pore formation and disrupting bacterial cell membranes through a distinct mechanism involving flexible glycine-rich sequences, which is salt-tolerant and independent of canonical amphipathic alpha-helical structures.