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MYP_031050
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Basic Information
Brevinin-1E (Frogs, amphibians, animals)
Anticancer ▸ Cytotoxic anticancer activity ▸ Cytotoxic
Antimicrobial
Antimicrobial ▸ Antibacterial
Antimicrobial ▸ Antibacterial ▸ Anti-Gram-negative
Antimicrobial ▸ Antibacterial ▸ Anti-Gram-positive
Antimicrobial ▸ Antifungal
Hormonal / Endocrine ▸ Hormone peptide
Toxicity / Safety ▸ Blood cell toxicity ▸ Hemolysis ▸ Hemolytic
Toxicity / Safety ▸ Cytolysis / cell lysis ▸ Cytolytic activity
Toxicity / Safety ▸ Cytotoxicity ▸ Cytotoxic
Toxicity / Safety ▸ Negative safety assay result ▸ Non-hemolytic
Venom / Toxin ▸ General toxin ▸ Cytotoxic
Venom / Toxin ▸ General toxin ▸ Toxic
Standard
24 amino acids
C128H209N31O27S2
Standard
Sequence
FLPLLAGLAANFLPKIFCKITRKC
Physicochemical Analysis
2678.35 Da
9.85
3.74
3.50
0.1557
0.95
0.78
0.29
12.30
126.25
0.1250
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
918.32
-2.93
33.0
33.0
86.0
188.0
5.0
24.0
Structural Visualization
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0168013 VERIFIED: YES
Provenance & Taxonomy
Rana esculenta [Animal]
Brevinin
Structure & Mods
disulfide-constrained cyclic peptide [Cyclic]
canonical L-amino-acid peptide [L]
None
Cyclization
18-24
Bio-Activity Profile
Antimicrobial Antibacterial Anti-Gram-positive Anti-Gram-negative Antifungal Cytotoxic
PMID8508915;8163497 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/8508915/
RECORD: Rec_0177436 VERIFIED: YES
Provenance & Taxonomy
not reported [other]
Brevinin
Structure & Mods
cyclic peptide [Cyclic]
canonical L-amino-acid peptide [L]
None
None
Bio-Activity Profile
Antimicrobial Antibacterial
Rat erythrocytes
0.7 μM
Hemolysis
Paperhttps://pubmed.ncbi.nlm.nih.gov/11892852/ PMID11892852 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/11892852/
RECORD: Rec_0186055 VERIFIED: YES
Provenance & Taxonomy
Pelophylax ridibundus [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]
Amidation
18-24
Bio-Activity Profile
Hemolytic Cytolytic
Erythrocytes
0.41 μM
HC50
PaperMi-Yun Kwon et al. / Biochimica et Biophysica Acta 1387 (1998) 239-248. Structure-activity analysis of brevinin 1E amide, an antimicrobial peptide from Rana esculenta Evidence URLhttps://www.uniprot.org/uniprotkb/P86149/entry
RECORD: Rec_0188428 VERIFIED: YES
Provenance & Taxonomy
Rana esculenta [Animal]
Brevinin
Structure & Mods
Single-chain peptide backbone represented as a linear sequence entry [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antimicrobial Antibacterial Anti-Gram-positive Anti-Gram-negative
E.coliD21
1.8 μM
MIC
PMID8508915 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/8508915/
RECORD: Rec_0198629 VERIFIED: YES
Provenance & Taxonomy
Pelophylax esculentus [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]
Amidation
18-24
Bio-Activity Profile
Antimicrobial Antibacterial Anti-Gram-positive
Staphylococcus aureus
2.33 μM
MIC
PaperMi-Yun Kwon et al. / Biochimica et Biophysica Acta 1387 (1998) 239-248. Structure-activity analysis of brevinin 1E amide, an antimicrobial peptide from Rana esculenta Evidence URLhttps://www.uniprot.org/uniprotkb/P32412/entry
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