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MYP_150200
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Basic Information
LL-37 (17-29)[V5Q]
Antimicrobial
Antimicrobial ▸ Antibacterial
Antimicrobial ▸ Antibacterial ▸ Anti-Gram-negative
Antimicrobial ▸ Antibacterial ▸ Anti-Gram-positive
Toxicity / Safety ▸ Blood cell toxicity ▸ Hemolysis ▸ Hemolytic
Standard
13 amino acids
C80H134N26O18
Standard
Sequence
FKRIQQRIKDFLR
Physicochemical Analysis
1748.08 Da
11.72
3.76
3.55
0.2892
-1.03
0.88
-0.54
40.05
90.00
0.1538
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
773.74
-5.11
28.0
22.0
63.0
124.0
2.0
14.0
Structural Visualization
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0038378 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
Cathelicidin
32630
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antimicrobial Antibacterial
Escherichia coli ATCC 25922
5 μM
MIC
PMID23894079 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/23894079/
RECORD: Rec_0054169 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
32630
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
None
None
Bio-Activity Profile
Antimicrobial Antibacterial Anti-Gram-positive Anti-Gram-negative Hemolytic
human red blood cells
PaperDisruption of interactions between hydrophobic residues on nonpolar faces is a key determinant in decreasing hemolysis and increasing antimicrobial activities of α-helical amphipathic peptides PMID23894079 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/23894079/
RECORD: Rec_0198209 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
32630
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
None
None
Bio-Activity Profile
Antimicrobial Antibacterial Anti-Gram-positive Anti-Gram-negative
Gram-positive bacteria: Staphylococcus aureus (ATCC 29213)
40 μM
MIC
PaperDisruption of interactions between hydrophobic residues on nonpolar faces is a key determinant in decreasing hemolysis and increasing antimicrobial activities of α-helical amphipathic peptides PMID23894079 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/23894079/
RECORD: Rec_0198955 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
32630
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
None
None
Bio-Activity Profile
Antimicrobial Antibacterial Anti-Gram-positive Anti-Gram-negative Hemolytic
PaperDisruption of interactions between hydrophobic residues on nonpolar faces is a key determinant in decreasing hemolysis and increasing antimicrobial activities of α-helical amphipathic peptides PMID23894079 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/23894079/
RECORD: Rec_0230752 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
32630
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
None
None
Bio-Activity Profile
Antimicrobial Antibacterial Anti-Gram-positive Anti-Gram-negative
Gram-negative bacteria: Escherichia coli (ATCC 25922)
5 μM
MIC
PaperDisruption of interactions between hydrophobic residues on nonpolar faces is a key determinant in decreasing hemolysis and increasing antimicrobial activities of α-helical amphipathic peptides PMID23894079 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/23894079/
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