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MYP_164419
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Basic Information
V16M
Antimicrobial
Antimicrobial ▸ Antibacterial
Antimicrobial ▸ Antibacterial ▸ Anti-Gram-negative
Antimicrobial ▸ Antibacterial ▸ Anti-Gram-positive
Antimicrobial ▸ Antifungal
Standard
16 amino acids
C81H140N28O21S3
Standard
Sequence
VPIIYCNRRTGKCQRM
Physicochemical Analysis
1938.35 Da
10.10
3.71
3.47
0.2320
-0.52
0.49
-0.30
41.89
66.88
0.0625
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
829.39
-8.44
32.0
28.0
64.0
133.0
2.0
17.0
Structural Visualization
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0407593 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
carotovora
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_0409151 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
32630
Structure & Mods
synthetic linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antimicrobial Antibacterial Antifungal Anti-Gram-positive Anti-Gram-negative
Fusarium culmorum
10-20 μM
MIC
PMID8577744 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/8577744/
RECORD: Rec_0410752 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
Thanatin
32630
Structure & Mods
synthetic linear peptide [Linear]
canonical L-amino-acid peptide [L]
6-13
APD analysis reveals that this sequence is similar (76.19%) to Thanatin R: 19%, I=C: 13%. Chemical modification: disulfide bond C6-C13 based on the truncated sequence
Bio-Activity Profile
Antimicrobial Antifungal
T. viride
20-40 μM
MIC
PaperStructure-activity analysis of thanatin, a 21-residue inducible insect defense peptide with sequence homology to frog skin antimicrobial peptides.
RECORD: Rec_0414477 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 D31
0.6-1.2 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_0416252 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
Thanatin
32630
Structure & Mods
synthetic linear peptide [Linear]
canonical L-amino-acid peptide [L]
6-13
APD analysis reveals that this sequence is similar (76.19%) to Thanatin R: 19%, I=C: 13%. Chemical modification: disulfide bond C6-C13 based on the truncated sequence
Bio-Activity Profile
Antimicrobial Antifungal
Klebsiella pneumoniae
2.5-5 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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