MYP_107574
Basic Information
LL-37
Anticancer
Anticancer Cytotoxic anticancer activity Cytotoxic
Antimicrobial
Antimicrobial Antibacterial
Antimicrobial Antibacterial Anti-Gram-negative
Antimicrobial Antibacterial Anti-Gram-positive
Antimicrobial Antibacterial Anti-Mycobacterium
Antimicrobial Anti-biofilm Biofilm inhibition
Antimicrobial Antifungal
Antiparasitic Antiprotozoal Anti-Trypanosoma
Antiparasitic General antiparasitic Antiparasitic
Antiviral
Antiviral Anti-Coronavirus Anti-SARS-CoV-2
Antiviral Anti-Filovirus Anti-Ebola virus
Antiviral Anti-Herpesvirus Anti-HSV
Antiviral Antiviral mechanism Viral entry inhibition
Antiviral Antiviral mechanism Viral replication inhibition Replication inhibitor
Antiviral Virucidal activity
Immunology Immune cell migration Chemotactic peptide
Immunology Immune modulation Immunomodulatory activity
Immunology Inflammation modulation Anti-inflammatory
Immunology Innate immune defense Host defense peptide Host defense activity
Membrane / Ion-channel modulation Sodium channel modulation Sodium channel inhibitor
Reproductive biology Contraceptive activity Spermicidal
Toxicity / Safety Blood cell toxicity Hemolysis Hemolytic
Toxicity / Safety Cytotoxicity Cytotoxic
Venom / Toxin General toxin Cytotoxic
Venom / Toxin General toxin Toxic
Wound healing/Regeneration Wound healing
Standard
37 amino acids
C205H340N60O53
Standard
Sequence
LLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES
Physicochemical Analysis
4493.26 Da
10.61
5.76
5.55
0.1558
-0.72
0.97
-0.31
23.34
89.46
0.1081
0.00
0.00
The radar chart summarizes major physicochemical dimensions for quick comparison, while exact numerical values remain listed on the left.
Residue Composition
Amino Acid Composition
Chemical Descriptors
1901.12
-14.63
68.0
59.0
161.0
318.0
5.0
38.0
Structural Visualization
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0251039 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
Cathelicidin
32630
Structure & Mods
synthetic linear peptide [Linear]
all-D amino-acid peptide [D]
Bio-Activity Profile
Antibiofilm Antibacterial
Pseudomonas aeruginosa
142.521 μM
Total countable CFUs
RECORD: Rec_0256066 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
Cathelicidin
32630
Structure & Mods
synthetic linear peptide [Linear]
all-D amino-acid peptide [D]
Bio-Activity Profile
Antibiofilm Antibacterial
Staphylococcus aureus
12.5, 25, 50 μM
Total countable CFUs
RECORD: Rec_0256901 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
Cathelicidin
32630
Structure & Mods
synthetic linear peptide [Linear]
all-D amino-acid peptide [D]
Bio-Activity Profile
Antibiofilm Antibacterial
Burkholderia pseudomallei
20, 100 μM
Total countable CFUs
RECORD: Rec_0260139 VERIFIED: YES
Provenance & Taxonomy
Homo sapiens [Animal]
Cathelicidin
9606
Structure & Mods
linear peptide [Linear]
noncanonical stereochemical modification [Modified]
Acetylation
Deficiency in saliva LL-37 (leucine leucine 37) accords with occurrence of periodontal disease in patients with morbus Kostmann Pütsep K et al., 2002. Lower levels of LL-37 in serum are correlated with RSV and severity of bronchiolitis and viral etiology (Mansbach et al., 2017). The relationship of human LL-37 with cancer is complex (Reviewed by Wu et al. 2010). While LL-37 could promote cancer metastasis in certain cases, its fragment (FK-16) have been documented to have anti-cancer effects (Li et al., 2006). LL-37 appears to promote liver repair after acetaminophon-induced injury (Zhai et al., 2023). The N-terminal leucine pair of LL-37 is critical for autophage (Rekha et al., 2025). Therapeutic strategy: Sunlight and vitamin D, and light therapy: host expression:induced. The expression of LL-37 is transcriptionally regulated by vitamin D (Karlsson J et al. 2008), sunlight, and other factors. This might have provided the basis for Niels Finsen' light therapy to treat TB. Indeed, colocalization of LL-37 and mycobacteria element has been detected in macrophages(Deshpande et al., 2020). The administration of vitamin D (25D3) as supplement (leading to cathelicidin expression in epithelial cells) may prevent urinary tract infection (UTI) (Hertting, O et al. 2010). Other AMP inducing factors are listed here. Discovery: Discovered in 1995 by three labs (see the ref; Cowland JB et al. 1995; Larrick JW et al. 1995). The precursor protein is human cationic antimicrobial protein-18 kDa (hCAP-18). The mature peptide released by proteinase 3 is referred to as LL-37 (Gudmundsson GH et al., 1996), which is two residues shorter than the predicted form FALL-39 (AP03566). Sequence analysis: Molecular formula of LL-37: C205H341N59O53; Mol. Wt. 4493.312; molar extinction coefficient = 0. Post-translational chemical modification: Arginines of LL-37 can get citrullinated (Kilsgård et al., 2012), weakening its ability in preventing endotoxin-induced sepsis (Koziel J et al., 2014). It has been proved that citrullinated LL-37 can be detected when healthy people are exposed to LPS (Al-Adwani et al., 2020). Also, up to four out of the five arginines of LL-37 can be ADP-ribosylated, thereby regulating peptide properties in vivo (Picchianti et al., 2015). LL-37 may also be carbamylated (Koro et al., 2016). It appears that LL-37 in neutrophils (formylated,
Bio-Activity Profile
Antimicrobial Antifungal Antiviral Anticancer Antiparasitic Anti-inflammatory Spermicidal Wound healing
Mycobacterium smegmatis, M. bovis, L. casei, Listeria monocytogenes EGD
1.5 μg/mL
MIC
RECORD: Rec_0263789 VERIFIED: YES
Provenance & Taxonomy
Homo sapiens [Animal]
Cathelicidin
9606;0
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antibiofilm Antibacterial
Staphylococcus aureus
12.5, 25, 50 μM
Total countable CFUs
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