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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_0364690 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
Antimicrobial Antifungal
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_0370311 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
Hemolytic
Red blood cells
0.5 μM
Hemolysis
PMID8508915 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/8508915/
RECORD: Rec_0375004 VERIFIED: YES
Provenance & Taxonomy
Pelophylax ridibundus [Animal]
Brevinin
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antimicrobial Anti-Gram-negative Anti-Gram-positive Cytolytic Hemolytic
Gram-negative and Gram-positive bacteria
PMID18280749;18855342 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/18280749/
RECORD: Rec_0382235 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 Antifungal Insulin releasing
PaperL. Marenah et al. / Journal of Endocrinology 188 (2006) 1-9. Skin secretions of Rana saharica frogs reveal antimicrobial peptides esculentins-1 and -1B and brevinins-1E and -2EC with novel insulin releasing activity Evidence URLhttps://www.uniprot.org/uniprotkb/P32412/entry
RECORD: Rec_0395398 VERIFIED: YES
Provenance & Taxonomy
Pelophylax saharicus [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-negative
Escherichia coli
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/P84839/entry
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