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MYP_132161
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Basic Information
I14M
Antimicrobial
Antimicrobial ▸ Antibacterial
Antimicrobial ▸ Antibacterial ▸ Anti-Gram-negative
Antimicrobial ▸ Antibacterial ▸ Anti-Gram-positive
Antimicrobial ▸ Antifungal
Standard
14 amino acids
C71H124N26O19S3
Standard
Sequence
IIYCNRRTGKCQRM
Physicochemical Analysis
1742.10 Da
10.10
3.74
3.50
0.2670
-0.78
0.49
-0.43
32.69
55.71
0.0714
1490.00
1615.00
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
779.98
-8.57
31.0
26.0
60.0
119.0
1.0
15.0
Structural Visualization
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0309440 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
Thanatin
32630
Structure & Mods
synthetic linear peptide [Linear]
canonical L-amino-acid peptide [L]
4-11
APD analysis reveals that this sequence is similar (66.67%) to Thanatin R: 21%, I=C: 14%. Chemical modification: C-C disulfide bond
Bio-Activity Profile
Antimicrobial Antifungal
F-oxysporum
>40 μM
MIC
PaperStructure-activity analysis of thanatin, a 21-residue inducible insect defense peptide with sequence homology to frog skin antimicrobial peptides.
RECORD: Rec_0310828 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
32630
Structure & Mods
topology not specified [Not included yet]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antimicrobial Antibacterial Anti-Gram-positive Anti-Gram-negative Antifungal
Alternaria brassicicola
5-10 μM
MIC
PaperStructure-activity analysis of thanatin, a 21-residue inducible insect defense peptide with sequence homology to frog skin antimicrobial peptides. Proc Natl Acad Sci U S A. 1996 Feb 6;93(3):1221-1225. doi: 10.1073/pnas.93.3.1221. PMID: 8577744. PMID8577744 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/8577744/
RECORD: Rec_0313887 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
Thanatin
32630
Structure & Mods
synthetic linear peptide [Linear]
canonical L-amino-acid peptide [L]
4-11
APD analysis reveals that this sequence is similar (66.67%) to Thanatin R: 21%, I=C: 14%. Chemical modification: C-C disulfide bond
Bio-Activity Profile
Antimicrobial Antifungal
A. brassicola
5-10 μM
MIC
PaperStructure-activity analysis of thanatin, a 21-residue inducible insect defense peptide with sequence homology to frog skin antimicrobial peptides.
RECORD: Rec_0315118 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
32630
Structure & Mods
topology not specified [Not included yet]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antimicrobial Antibacterial Anti-Gram-positive Anti-Gram-negative Antifungal
Escherichia coli D22
20-40 μM
MIC
PaperStructure-activity analysis of thanatin, a 21-residue inducible insect defense peptide with sequence homology to frog skin antimicrobial peptides. Proc Natl Acad Sci U S A. 1996 Feb 6;93(3):1221-1225. doi: 10.1073/pnas.93.3.1221. PMID: 8577744. PMID8577744 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/8577744/
RECORD: Rec_0317340 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
Thanatin
32630
Structure & Mods
synthetic linear peptide [Linear]
canonical L-amino-acid peptide [L]
4-11
APD analysis reveals that this sequence is similar (66.67%) to Thanatin R: 21%, I=C: 14%. Chemical modification: C-C disulfide bond
Bio-Activity Profile
Antimicrobial Antifungal
N. crassa
20-40 μM
MIC
PaperStructure-activity analysis of thanatin, a 21-residue inducible insect defense peptide with sequence homology to frog skin antimicrobial peptides.
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