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MYP_036540
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Basic Information
Lt-F11Q (Derived from Lt)
Antimicrobial
Antimicrobial ▸ Antibacterial
Antimicrobial ▸ Antibacterial ▸ Anti-Gram-negative
Antimicrobial ▸ Antibacterial ▸ Anti-Gram-positive
Toxicity / Safety ▸ Blood cell toxicity ▸ Hemolysis ▸ Hemolytic
Standard
13 amino acids
C76H134N26O18
Standard
Sequence
FKRIVQRIKDQLR
Physicochemical Analysis
1700.04 Da
11.72
3.76
3.55
0.2892
-0.92
0.90
-0.55
24.50
112.31
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
773.74
-5.69
28.0
22.0
62.0
120.0
1.0
14.0
Structural Visualization
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0104667 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_0143692 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
10 μM
MIC
PMID23894079 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/23894079/
RECORD: Rec_0171359 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_0306062 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/
RECORD: Rec_0317010 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/
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