Peptide Database

Peptide NameOncocin

Function Ontology

Antimicrobial

Antimicrobial ▸ Antibacterial

Antimicrobial ▸ Antibacterial ▸ Anti-Gram-negative

Antimicrobial ▸ Antibacterial ▸ Anti-Gram-positive

Antimicrobial ▸ Antifungal

Standard StatusStandard

Sequence Length40 amino acids

Chemical FormulaC178H290N62O48S6

DescriptionStandard

        ATCDLLSPFKVGHAACALHCIALGRRGGWCDGRAVCNCRR
    

Molecular Weight4258.98 Da

Isoelectric Point (pI)8.98

Net Charge (pH 7.0)3.91

Net Charge (pH 7.4) 3.53

Charge Density (pH 7.0) 0.0978

GRAVY Index0.18

Hydrophobic Moment 0.51

Boman Index0.00

Instability Index70.13

Aliphatic Index 78.25

Aromaticity 0.0500

Extinction Coeff. Reduced 5500.00

Extinction Coeff. Oxidized 5875.00

The radar chart summarizes major physicochemical dimensions for quick comparison, while exact numerical values remain listed on the left.

Amino Acid Composition

TPSA 1756.25

LogP -20.25

H-bond Donors 70.0

H-bond Acceptors 60.0

Rotatable Bonds 136.0

Heavy Atoms 294.0

Ring Count 6.0

Amide Bonds 40.0

3D PDB MODEL

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2D CHEMICAL STRUCTURE

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RECORD: Rec_0046379 VERIFIED: YES

Provenance & Taxonomy

OrganismSynthetic construct [Synthetic]

FamilyPrAMP

Tax ID32630

Structure & Mods

Configlinear peptide [Linear]

Chiralitymixed L/D amino-acid peptide [Mixed]

C-TermAmidation

Other ModsInterestingly, 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

Function

Antimicrobial

TargetStenotrophomonas

Activity8-32 μg/mL

MethodMIC

Half-LifeInterestingly, 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_0072633 VERIFIED: YES

Provenance & Taxonomy

OrganismHermetia illucens [Animal]

FamilyDefensin

Tax ID343691

Structure & Mods

Configlinear peptide [Linear]

Chiralitycanonical L-amino-acid peptide [L]

Bio-Activity Profile

Function

Antimicrobial Antibacterial Antifungal Anti-Gram-positive Anti-Gram-negative

TargetMRC-5 SV2

Activity32 μM

MethodIC50

RECORD: Rec_0094723 VERIFIED: YES

Provenance & Taxonomy

OrganismHermetia illucens [Animal]

FamilyDefensin

Tax ID343691

Structure & Mods

Configlinear peptide [Linear]

Chiralitycanonical L-amino-acid peptide [L]

Bio-Activity Profile

Function

Antimicrobial Antibacterial Antifungal Anti-Gram-positive Anti-Gram-negative

TargetPseudomonas aeruginosa ATCC 9027

Activity32 μM

MethodIC50

RECORD: Rec_0103601 VERIFIED: YES

Provenance & Taxonomy

OrganismSynthetic construct [Synthetic]

FamilyPrAMP

Tax ID32630

Structure & Mods

Configlinear peptide [Linear]

Chiralitymixed L/D amino-acid peptide [Mixed]

C-TermAmidation

Other ModsInterestingly, 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

Function

Antimicrobial

TargetPseudomonas aeruginosa 8 strains

Activity2-8 μg/mL

MethodMIC

Half-LifeInterestingly, 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_0108189 VERIFIED: YES

Provenance & Taxonomy

OrganismHermetia illucens [Animal]

FamilyDefensin

Tax ID343691

Structure & Mods

Configlinear peptide [Linear]

Chiralitycanonical L-amino-acid peptide [L]

Bio-Activity Profile

Function

Antimicrobial Antibacterial Antifungal Anti-Gram-positive Anti-Gram-negative

TargetA. fumigatus B42928

Activity32 μM

MethodIC50

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