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MYP_133298
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Basic Information
Brevinin-2EC
Antimicrobial
Antimicrobial ▸ Antibacterial
Antimicrobial ▸ Antibacterial ▸ Anti-Gram-negative
Antimicrobial ▸ Antibacterial ▸ Anti-Gram-positive
Antimicrobial ▸ Antibiotic activity
Immunology ▸ Innate immune defense ▸ Host defense peptide ▸ Defense peptide
Toxicity / Safety ▸ Blood cell toxicity ▸ Hemolysis ▸ Hemolytic
Toxicity / Safety ▸ Cytolysis / cell lysis ▸ Cytolytic activity
Toxicity / Safety ▸ Negative safety assay result ▸ Non-hemolytic
Standard
34 amino acids
C154H267N43O46S2
Standard
Sequence
GILLDKLKNFAKTAGKGVLQSLLNTASCKLSGQC
Physicochemical Analysis
3521.16 Da
9.60
3.74
3.50
0.1099
0.18
0.65
0.09
20.86
109.12
0.0294
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
1464.53
-16.75
52.0
52.0
125.0
245.0
1.0
37.0
Structural Visualization
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0138921 VERIFIED: YES
Provenance & Taxonomy
Rana esculenta [Animal]
Brevinin
Structure & Mods
topology not specified [Not included yet]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antimicrobial Antibacterial Anti-Gram-positive Anti-Gram-negative Hemolytic
human erythrocytes
100 μM
LC50
PaperPubMed PMID: 8163497 | PubMed PMID: 16394170 PMID8163497;16394170 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/8163497/
RECORD: Rec_0140796 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
PMID8163497 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/8163497/
RECORD: Rec_0190605 VERIFIED: YES
Provenance & Taxonomy
Pelophylax esculentus [Animal]
Brevinin
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
28-34
Bio-Activity Profile
Antimicrobial
PaperAntimicrobial peptides from skin secretions of Rana esculenta. Molecular cloning of cDNAs encoding esculentin and brevinins and isolation of new active peptides.
RECORD: Rec_0195402 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]
28-34
Bio-Activity Profile
Antimicrobial Antibacterial
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/P84842/entry
RECORD: Rec_0200786 VERIFIED: YES
Provenance & Taxonomy
Rana esculenta [Animal]
Brevinin
Structure & Mods
topology not specified [Not included yet]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antimicrobial Antibacterial Anti-Gram-positive Anti-Gram-negative Hemolytic
PaperPubMed PMID: 8163497 | PubMed PMID: 16394170 PMID8163497;16394170 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/8163497/
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