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MYP_138608
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Basic Information
Brevinin-2PRa
Anticancer ▸ Cytotoxic anticancer activity ▸ Cytotoxic
Antimicrobial
Antimicrobial ▸ Antibacterial
Antimicrobial ▸ Antibacterial ▸ Anti-Gram-negative
Antimicrobial ▸ Antibacterial ▸ Anti-Gram-positive
Toxicity / Safety ▸ Blood cell toxicity ▸ Hemolysis ▸ Hemolytic
Toxicity / Safety ▸ Cytolysis / cell lysis ▸ Cytolytic activity
Toxicity / Safety ▸ Cytotoxicity ▸ Cytotoxic
Venom / Toxin ▸ General toxin ▸ Cytotoxic
Venom / Toxin ▸ General toxin ▸ Toxic
Standard
37 amino acids
C173H291N47O48S3
Standard
Sequence
GLMSLFKGVLKTAGKHIFKNVGGSLLDQAKCKITGEC
Physicochemical Analysis
3893.64 Da
9.51
3.83
3.53
0.1034
0.18
0.61
0.13
24.76
94.86
0.0541
0.00
125.00
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
1537.42
-14.62
55.0
56.0
138.0
271.0
3.0
38.0
Structural Visualization
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0228247 VERIFIED: YES
Provenance & Taxonomy
Rana pirica [Animal]
Brevinin
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
31-37
Bio-Activity Profile
Antimicrobial
Escherichia coli
6 μM
MIC
PaperA family of brevinin-2 peptides with potent activity against Pseudomonas aeruginosa from the skin of the Hokkaido frog, Rana pirica.
RECORD: Rec_0237846 VERIFIED: NO
Provenance & Taxonomy
Rana pirica [Animal]
Brevinin
Structure & Mods
disulfide-constrained cyclic peptide [Cyclic]
canonical L-amino-acid peptide [L]
31-37
Bio-Activity Profile
Antimicrobial Antibacterial Hemolytic
Escherichia coli, Pseudomonas aeruginosa, Enterobacter cloacae, Klebsiella pneumoniae, Staphylococcus aureus
RECORD: Rec_0283013 VERIFIED: YES
Provenance & Taxonomy
Rana pirica [Animal]
Brevinin
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antimicrobial Antibacterial Anti-Gram-positive Anti-Gram-negative
Candida albicans
100 μM
MIC
PMID15003829 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/15003829/
RECORD: Rec_0283148 VERIFIED: YES
Provenance & Taxonomy
Rana pirica [Animal]
Brevinin
Structure & Mods
Linear peptide with a single intramolecular disulfide-stabilized loop [Linear]
Gene-encoded natural peptide composed of standard L-amino acids [L]
31-37
Bio-Activity Profile
Antimicrobial Antibacterial Anti-Gram-positive
Staphylococcus aureus
25.0 μM
MIC
PaperJ.M. Conlon et al. / Regulatory Peptides 118 (2004) 135-141. A family of brevinin-2 peptides with potent activity against Pseudomonas aeruginosa from the skin of the Hokkaido frog, Rana pirica
RECORD: Rec_0292313 VERIFIED: YES
Provenance & Taxonomy
Rana pirica [Animal]
Brevinin
Structure & Mods
Linear peptide with a single intramolecular disulfide-stabilized loop [Linear]
Gene-encoded natural peptide composed of standard L-amino acids [L]
31-37
Bio-Activity Profile
Antimicrobial Antibacterial Anti-Gram-negative
Escherichia coli
6.0 μM
MIC
PaperJ.M. Conlon et al. / Regulatory Peptides 118 (2004) 135-141. A family of brevinin-2 peptides with potent activity against Pseudomonas aeruginosa from the skin of the Hokkaido frog, Rana pirica
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