MYP_030838
Basic Information
Oncocin
Antimicrobial
Antimicrobial Antibacterial
Antimicrobial Antibacterial Anti-Gram-negative
Antimicrobial Antibacterial Anti-Gram-positive
Antimicrobial Antifungal
Standard
40 amino acids
C178H290N62O48S6
Standard
Sequence
ATCDLLSPFKVGHAACALHCIALGRRGGWCDGRAVCNCRR
Physicochemical Analysis
4258.98 Da
8.98
3.91
3.53
0.0978
0.18
0.51
0.00
70.13
78.25
0.0500
5500.00
5875.00
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
1756.25
-20.25
70.0
60.0
136.0
294.0
6.0
40.0
Structural Visualization
3D PDB MODEL
Drag to rotate. Click a residue or atom to inspect it; the selected residue is highlighted in amber in the current view mode. Use the buttons to zoom.
2D CHEMICAL STRUCTURE
Drag to move
Drag to move. Use the buttons to zoom.
Experimental Records
RECORD: Rec_0125440 VERIFIED: YES
Provenance & Taxonomy
Hermetia illucens [Animal]
Defensin
343691
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antimicrobial Antibacterial Antifungal Anti-Gram-positive Anti-Gram-negative
Candida albicans B59630
32 μM
IC50
RECORD: Rec_0140797 VERIFIED: YES
Provenance & Taxonomy
Synthetic construct [Synthetic]
PrAMP
32630
Structure & Mods
linear peptide [Linear]
mixed L/D amino-acid peptide [Mixed]
Amidation
Interestingly, D-amino acids can be partially incorporated to confer other desired properties (e.g., serum stability) to the peptide without sacrificing peptide activity (Gan et al., 2024). Up to 9 C-terminal residues can be replaced with D-amino acids. In contrast, full sequence stereo-randomization to sr-Onc abolished ribosome binding, similar to the case for the enantiomer D-Onc and further diastereomers containing D-residues in the ribosome binding stretch, such as DL7-Onc. For other derivatives, please refer to the ref above. D-amino acid incorporated peptides are resistant to serum degradation
Bio-Activity Profile
Antimicrobial
Klebsiella pneumoniae 6 strains
0.25-8 μg/mL
MIC
Interestingly, D-amino acids can be partially incorporated to confer other desired properties (e.g., serum stability) to the peptide without sacrificing peptide activity (Gan et al., 2024). Up to 9 C-terminal residues can be replaced with D-amino acids. In contrast, full sequence stereo-randomization to sr-Onc abolished ribosome binding, similar to the case for the enantiomer D-Onc and further diastereomers containing D-residues in the ribosome binding stretch, such as DL7-Onc. For other derivatives, please refer to the ref above. D-amino acid incorporated peptides are resistant to serum degradation.
RECORD: Rec_0164369 VERIFIED: YES
Provenance & Taxonomy
Hermetia illucens [Animal]
Defensin
343691
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antimicrobial Antibacterial Antifungal Anti-Gram-positive Anti-Gram-negative
Escherichia coli ATCC 8739
32 μM
IC50
RECORD: Rec_0197117 VERIFIED: YES
Provenance & Taxonomy
Synthetic construct [Synthetic]
PrAMP
32630
Structure & Mods
linear peptide [Linear]
mixed L/D amino-acid peptide [Mixed]
Amidation
Interestingly, D-amino acids can be partially incorporated to confer other desired properties (e.g., serum stability) to the peptide without sacrificing peptide activity (Gan et al., 2024). Up to 9 C-terminal residues can be replaced with D-amino acids. In contrast, full sequence stereo-randomization to sr-Onc abolished ribosome binding, similar to the case for the enantiomer D-Onc and further diastereomers containing D-residues in the ribosome binding stretch, such as DL7-Onc. For other derivatives, please refer to the ref above. D-amino acid incorporated peptides are resistant to serum degradation
Bio-Activity Profile
Antimicrobial
Escherichia coli 8 strains
0.5-8 μg/mL
MIC
Interestingly, D-amino acids can be partially incorporated to confer other desired properties (e.g., serum stability) to the peptide without sacrificing peptide activity (Gan et al., 2024). Up to 9 C-terminal residues can be replaced with D-amino acids. In contrast, full sequence stereo-randomization to sr-Onc abolished ribosome binding, similar to the case for the enantiomer D-Onc and further diastereomers containing D-residues in the ribosome binding stretch, such as DL7-Onc. For other derivatives, please refer to the ref above. D-amino acid incorporated peptides are resistant to serum degradation.
RECORD: Rec_0206451 VERIFIED: YES
Provenance & Taxonomy
not reported [other]
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antimicrobial
E-coli
>32-64 μM
MIC
Showing 5 records on this page · Page 2 of 4