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MYP_065691
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Basic Information
Unnamed
Anticancer
Anticancer ▸ Cytotoxic anticancer activity ▸ Cytotoxic
Antimicrobial
Antimicrobial ▸ Antibacterial
Antimicrobial ▸ Antibacterial ▸ Anti-Gram-negative
Antimicrobial ▸ Antibacterial ▸ Anti-Gram-positive
Antimicrobial ▸ Antifungal
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
20 amino acids
C110H179N23O22S2
Standard
Sequence
FLSLALAALPKLFCLIFKKC
Physicochemical Analysis
2239.87 Da
9.39
2.74
2.50
0.1369
1.60
0.56
0.46
17.00
151.50
0.1500
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
705.72
0.47
26.0
27.0
73.0
157.0
4.0
19.0
Structural Visualization
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0394054 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]
14-20
Bio-Activity Profile
Antimicrobial Antibacterial Anti-Gram-negative
Escherichia coli
100.0 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_0400955 VERIFIED: YES
Provenance & Taxonomy
Rana amurensis [Animal]
Amurin
Structure & Mods
Linear peptide with a single intramolecular disulfide-stabilized loop [Linear]
Gene-encoded natural peptide composed of standard L-amino acids [L]
14-20
Bio-Activity Profile
Hemolytic Cytolytic
Erythrocytes
7.0 μM
HC50
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 Evidence URLhttps://www.uniprot.org/uniprotkb/A0AAS2/entry
RECORD: Rec_0406377 VERIFIED: YES
Provenance & Taxonomy
Rana dybowskii [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
14-20
Bio-Activity Profile
Antimicrobial Antibacterial Anti-Gram-negative
Escherichia coli
25.0 μM
MIC
PaperLi-Li Jin et al. / Comparative Biochemistry and Physiology, Part B 154 (2009) 174-178. Characterization of antimicrobial peptides isolated from the skin of the Chinese frog, Rana dybowskii PMID19539775 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/19539775/
RECORD: Rec_0409781 VERIFIED: YES
Provenance & Taxonomy
Rana dybowskii [Animal]
Brevinin
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
14-20
Bio-Activity Profile
Antimicrobial Antifungal Anticancer
Candida albicans
32 μM
MIC
PaperCytolytic peptides belonging to the brevinin-1 and brevinin-2 families isolated from the skin of the Japanese brown frog, Rana dybowskii
RECORD: Rec_0412939 VERIFIED: YES
Provenance & Taxonomy
Rana amurensis [Animal]
Brevinin
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antimicrobial Antibacterial Antifungal Anti-Gram-positive Anti-Gram-negative
Staphylococcus aureus
32 μM
MIC
PMID29366784 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/29366784/
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