Understand the source comparison
LL-37 vs Related Cathelicidin Fragments: When Nomenclature Actually Indicates Different Molecules
The table below clarifies when name changes reflect actual structural differences versus descriptive labeling. Critical for avoiding specification errors during procurement. LL-37 37 residues Reference sequence Full antimicrobial + immunomodulatory activity St
This page preserves a source comparison for education. It does not add a rating, recommendation or clinical judgment.
- The table below clarifies when name changes reflect actual structural differences versus descriptive labeling. Critical for avoiding specification errors during procurement.
- LL-37
- 37 residues
- Reference sequence
- Full antimicrobial + immunomodulatory activity
- Standard form. Baseline for comparison
- LL-37 peptide
- None. Identical sequence
- None. Functionally identical
- Same molecule. Naming is descriptive only
- LL-23
- 23 residues
- N-terminal truncation (lacks residues 1–14)
- 60–80% reduced antimicrobial potency, retained chemotactic function
- Different molecule. Not interchangeable with LL-37
- hCAP18
- 134 residues
- Full-length precursor containing LL-37 at C-terminus
- Minimal activity until proteolytic cleavage releases LL-37
- Inactive precursor. Requires proteinase-3 processing
- FK-13
- 13 residues
- Residues 17–29 fragment of LL-37
- Reduced spectrum, lacks immunomodulatory binding
- Truncated analog. Not equivalent to full LL-37
- LL-37 (human)
- None vs standard LL-37
- None. Species designation for clarity
- Descriptor for cross-species work. Sequence identical to LL-37