‹ ›
MYP_056033
← PREVIOUS NEXT → BACK
Basic Information
Brevinin-2PRb
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
Venom / Toxin ▸ General toxin ▸ Toxic
Standard
37 amino acids
C173H291N49O48S3
Standard
Sequence
GLMSLFRGVLKTAGKHIFKNVGGSLLDQAKCKITGEC
Physicochemical Analysis
3921.66 Da
9.59
3.83
3.53
0.1034
0.16
0.67
0.10
28.82
94.86
0.0541
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
1573.30
-15.49
57.0
56.0
138.0
273.0
3.0
38.0
Structural Visualization
3D PDB MODEL
Drag to rotate. Click a residue or atom to inspect it; the selected residue is highlighted in amber in the current view mode. Use the buttons to zoom.
2D CHEMICAL STRUCTURE
Drag to move
Drag to move. Use the buttons to zoom.
Experimental Records
RECORD: Rec_0215997 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]
31-37
Bio-Activity Profile
Antimicrobial Antibacterial Anti-Gram-negative
Escherichia coli
3.0 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_0225584 VERIFIED: YES
Provenance & Taxonomy
not reported [other]
Brevinin
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
None
None
Bio-Activity Profile
Antimicrobial
Human erythrocytes
65 μM
HC50
Paperhttps://pubmed.ncbi.nlm.nih.gov/15003829/ PMID15003829 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/15003829/
RECORD: Rec_0236523 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]
31-37
Bio-Activity Profile
Hemolytic Cytolytic
Erythrocytes
65.0 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
RECORD: Rec_0269107 VERIFIED: YES
Provenance & Taxonomy
Rana pirica [Animal]
Brevinin
Structure & Mods
stapled cyclic peptide [Cyclic]
canonical L-amino-acid peptide [L]
None
Cyclization
31-37
Bio-Activity Profile
Antimicrobial Antibacterial Anti-Gram-positive Anti-Gram-negative
Yeast: Candida albicans
100 μM
MIC
PMID15003829 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/15003829/
RECORD: Rec_0282212 VERIFIED: YES
Provenance & Taxonomy
Rana pirica [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
Staphlococcus aureus NCTC 8325
25 μM
MIC
PMID15003829 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/15003829/
FIRST PREV 1 2 3 4 5 6 NEXT LAST
Showing 5 records on this page · Page 4 of 6