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MYP_129173
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Basic Information
LL-37 (17-29)[F1A]
Antimicrobial
Antimicrobial ▸ Antibacterial
Antimicrobial ▸ Antibacterial ▸ Anti-Gram-negative
Antimicrobial ▸ Antibacterial ▸ Anti-Gram-positive
Toxicity / Safety ▸ Blood cell toxicity ▸ Hemolysis ▸ Hemolytic
Standard
13 amino acids
C74H131N25O17
Standard
Sequence
AKRIVQRIKDFLR
Physicochemical Analysis
1642.99 Da
11.72
3.79
3.60
0.2919
-0.52
0.97
-0.43
30.26
120.00
0.0769
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
730.65
-4.94
27.0
21.0
59.0
116.0
1.0
13.0
Structural Visualization
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0109511 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
Staphylococcus aureus ATCC 29213
40 μM
MIC
PMID23894079;32567085 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/23894079/
RECORD: Rec_0143434 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_0214360 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_0219331 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_0244102 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)
10 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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