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MYP_116083
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Basic Information
Brevinin-2PRe
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
Standard
37 amino acids
C169H292N48O47S2
Standard
Sequence
GLLSVLKGVLKTAGKHIFKNVGGSLLDQAKCKISGQC
Physicochemical Analysis
3812.55 Da
9.79
4.82
4.53
0.1303
0.26
0.61
0.13
5.07
113.24
0.0270
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
1543.21
-15.90
55.0
55.0
136.0
266.0
2.0
39.0
Structural Visualization
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0169219 VERIFIED: YES
Provenance & Taxonomy
Rana pirica [Animal]
Brevinin
Structure & Mods
disulfide-constrained cyclic peptide [Cyclic]
canonical L-amino-acid peptide [L]
None
Cyclization
31-37
Bio-Activity Profile
Antimicrobial Antibacterial Anti-Gram-positive Anti-Gram-negative
Klebsiella pneumoniae
6 μM
MIC
PMID15003829 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/15003829/
RECORD: Rec_0220086 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
3.0 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_0224104 VERIFIED: YES
Provenance & Taxonomy
not reported [other]
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
None
None
Bio-Activity Profile
Antimicrobial
PaperDADP: the database of anuran defense peptides PMID22467909 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/22467909/
RECORD: Rec_0254635 VERIFIED: YES
Provenance & Taxonomy
Rana pirica [Animal]
Brevinin
Structure & Mods
disulfide-constrained cyclic peptide [Cyclic]
canonical L-amino-acid peptide [L]
None
Cyclization
31-37
Bio-Activity Profile
Antimicrobial Antibacterial Anti-Gram-positive Anti-Gram-negative
PMID15003829 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/15003829/
RECORD: Rec_0296907 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
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