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MYP_005689
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Basic Information
Brevinin-1BYb (Frogs, amphibians, animals)
Anticancer ▸ Cytotoxic anticancer activity ▸ Cytotoxic
Antimicrobial
Antimicrobial ▸ Antibacterial
Antimicrobial ▸ Antibacterial ▸ Anti-Gram-negative
Antimicrobial ▸ Antibacterial ▸ Anti-Gram-positive
Antimicrobial ▸ Antifungal
Antimicrobial ▸ Antifungal ▸ Anti-Candida
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
24 amino acids
C123H208N28O27S2
Standard
Sequence
FLPILASLAAKLGPKLFCLVTKKC
Physicochemical Analysis
2575.27 Da
9.70
3.74
3.50
0.1557
1.12
0.49
0.34
23.05
138.33
0.0833
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
859.58
-2.54
31.0
33.0
84.0
180.0
4.0
23.0
Structural Visualization
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0328770 VERIFIED: YES
Provenance & Taxonomy
Rana boylii [Animal]
Brevinin
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
18-24
Bio-Activity Profile
Antimicrobial Antifungal
Candida albicans
16 μM
MIC
PaperIsolation of peptides of the brevinin-1 family with potent candidacidal activity from the skin secretions of the frog Rana boylii
RECORD: Rec_0350298 VERIFIED: YES
Provenance & Taxonomy
Rana boylii [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]
18-24
Bio-Activity Profile
Antimicrobial Antibacterial Anti-Gram-positive
Staphylococcus aureus
4.0 μM
MIC
PaperJ.M. Conlon et al. / J. Peptide Res. 62 (2003) 207-213. Isolation of peptides of the brevinin-1 family with potent candidacidal activity from the skin secretions of the frog Rana boylii Evidence URLhttps://www.uniprot.org/uniprotkb/P84112/entry
RECORD: Rec_0363356 VERIFIED: YES
Provenance & Taxonomy
Rana boylii [Animal]
Brevinin
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
18-24
Bio-Activity Profile
Antimicrobial Antifungal
ed B. dendrobatidis
6.25 μM
MIC
PaperIsolation of peptides of the brevinin-1 family with potent candidacidal activity from the skin secretions of the frog Rana boylii
RECORD: Rec_0379513 VERIFIED: YES
Provenance & Taxonomy
Rana boylii [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 Antifungal Hemolytic
PaperPubMed PMID: 14531844 PMID14531844 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/14531844/
RECORD: Rec_0399006 VERIFIED: YES
Provenance & Taxonomy
Rana boylii [Animal]
Brevinin
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
-
Escherichia coli TOP10
Mex pooled growth assay (OD_ID at 4.5 h; Wald adjusted p-value)
PaperKoch P, Schmitt S, Cardner M, Beerenwinkel N, Panke S, Held M. Discovery of antimicrobials by massively parallelized growth assays (Mex). Scientific Reports. 2022;12:4097. doi:10.1038/s41598-022-07755-7 PMID35260685 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/35260685/
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