MYP_030838
Oncocin
Antimicrobial
Antimicrobial
▸
Antibacterial
Antimicrobial
▸
Antibacterial
▸
Anti-Gram-negative
Antimicrobial
▸
Antibacterial
▸
Anti-Gram-positive
Antimicrobial
▸
Antifungal
Standard
40 amino acids
C178H290N62O48S6
Standard
ATCDLLSPFKVGHAACALHCIALGRRGGWCDGRAVCNCRR
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.
Amino Acid Composition
1756.25
-20.25
70.0
60.0
136.0
294.0
6.0
40.0
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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RECORD: Rec_0237522
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
E. cloacae
0.125-4 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_0252908
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
Acinetobacter baumannii 5 strains
0.5-2 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_0255771
VERIFIED: NO
Provenance & Taxonomy
Hermetia illucens [Animal]
Defensin
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antimicrobial
RECORD: Rec_0265401
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
P. vulgaris
4 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_0268424
VERIFIED: YES
Provenance & Taxonomy
not reported [other]
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antimicrobial
P-aeruginos
>32-64 μM
MIC
Showing 5 records on this page · Page 3 of 4