Miscellaneous/General | Antimicrobial peptides (AMPs) are peptides that form part of the host's important innate immunity mechanism against pathogenic microorganisms such as Gram-positive and negative bacteria, fungi, and viruses. AMPs are short peptides, exhibit a broad-spectrum antimicrobial activity at physiological conditions, and are predominantly cationic. LL-37 is a 37 amino acid host defense peptide derived from the C-terminus of the only human calethicidin, hCAP18. This peptide has been found in many different cell types and body fluids and is linked with antimicrobial, antitumor, antiviral and immunomodulatory properties. Cytotoxic to both bacterial and normal eukaryotic cells, LL-37 is significantly resistant to proteolytic degradation in solution. In addition, LL-37 has been shown to play a role in chemoattraction, dendritic cell differentiation, mast cell degranulation, cytokine secretion, and angiogenesis stimulation. LL-37 has also been investigated as a wound-healing agent. In other species, the C-terminal antimicrobial region varies in sizes, sequences, and structures. LifeTein's LL-37 is an all-D-amino acid peptide. Please read more details about the D amino acid peptides: https://www. lifetein. com/Peptide-Synthesis-D-Amino-Acid. html |
Scientific Background | LL-37 (All D amino acid), Antimicrobial Peptide, human is a synthetic research peptide in the LL-37/cathelicidin antimicrobial peptide family. LL-37 is the 37-residue C-terminal antimicrobial peptide released from human hCAP18. It is amphipathic and cationic, interacts with microbial membranes, and has been widely studied for antimicrobial, antibiofilm, membrane, inflammatory, chemotactic, and wound-response activities. All-D LL-37 retains the same nominal sequence composition but has reversed stereochemistry and should be treated as a distinct research analog. |
Experimental Notes | The exact sequence, residue range, species, stereochemistry, terminal state, labels, and other modifications can materially affect activity. Match the supplied construct to the intended assay and published reference context. |
