Research Comparison
LL-37 (Human Cathelicidin) vs MOTS-c
A side-by-side research comparison of LL-37 (Human Cathelicidin) and MOTS-c drawn from Cobalt Peptides' peptide database records.
LL-37 (Human Cathelicidin)
LL-37 is the only known human cathelicidin antimicrobial peptide, consisting of 37 amino acids and derived from the precursor protein hCAP18. It plays a critical role in innate immunity, exhibiting broad-spectrum antimicrobial activity against bacteria, viruses, and fungi while also modulating inflammatory responses and promoting tissue repair. It is most commonly studied in topical applications for wound healing, where it provides both antimicrobial protection and regenerative support. Clinical and experimental data show significant improvements in chronic wound healing, though systemic use remains less well characterized.
MOTS-c
MOTS-c (Mitochondrial Open Reading Frame of the 12S rRNA-c) is a 16-amino acid mitochondrial-derived peptide encoded by mitochondrial DNA. It functions as a mitohormone, regulating metabolic homeostasis, insulin sensitivity, and cellular stress responses. Unlike nuclear-encoded peptides, MOTS-c is produced within mitochondria and can translocate to the nucleus under metabolic stress, where it influences gene expression. Its primary activity involves activation of the AMPK pathway via the folate-AICAR axis, making it a key regulator of energy metabolism and mitochondrial function.