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MYP_120335
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Basic Information
Citropin-1.1 (Frogs, amphibians, animals)
Anticancer
Anticancer ▸ Cytotoxic anticancer activity ▸ Cytotoxic
Antimicrobial
Antimicrobial ▸ Antibacterial
Antimicrobial ▸ Antibacterial ▸ Anti-Gram-negative
Antimicrobial ▸ Antibacterial ▸ Anti-Gram-positive
Antimicrobial ▸ Anti-biofilm ▸ Biofilm inhibition
Antimicrobial ▸ Antifungal
Enzyme modulation ▸ Enzyme inhibition ▸ nNOS inhibitor
Immunology ▸ Inflammation modulation ▸ Anti-inflammatory
Membrane / Ion-channel modulation ▸ Calcium channel modulation ▸ Calcium channel inhibitor
Neurological / Signaling ▸ Neuropeptide activity ▸ Neuropeptide
Toxicity / Safety ▸ Blood cell toxicity ▸ Hemolysis ▸ Hemolytic
Toxicity / Safety ▸ Cytotoxicity ▸ Cytotoxic
Toxicity / Safety ▸ Negative safety assay result ▸ Non-hemolytic
Venom / Toxin ▸ General toxin ▸ Cytotoxic
Standard
16 amino acids
C76H130N18O20
Standard
Sequence
GLFDVIKKVASVIGGL
Physicochemical Analysis
1615.95 Da
8.59
0.76
0.55
0.0474
1.28
0.64
0.46
14.19
158.12
0.0625
0.00
0.00
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
609.39
-3.30
21.0
21.0
55.0
114.0
1.0
15.0
Structural Visualization
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0087322 VERIFIED: YES
Provenance & Taxonomy
Amphibian skin [Animal]
Citropin
Structure & Mods
linear peptide [Linear]
all-D amino-acid peptide [D]
None
Amidation
Bio-Activity Profile
Antimicrobial Anticancer
Leukemia group (NCI)
10 μM
IC50
PapernNOS inhibition, antimicrobial and anticancer activity of the amphibian skin peptide, citropin 1.1 and synthetic modifications. The solution structure of a modified citropin 1.1. Eur J Biochem. 2003 Mar;270(6):1141-1153. doi: 10.1046/j.1432-1033.2003.03462.x. PMID: 12631273. PMID12631273 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/12631273/
RECORD: Rec_0094959 VERIFIED: YES
Provenance & Taxonomy
Litoria citropa [Animal]
Aurein
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
Bacillus cereus
50 μg/mL
MIC
PMID10504394 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/10504394/
RECORD: Rec_0099353 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
Aurein
32630
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antimicrobial Antibacterial Antifungal Anti-Gram-positive Anti-Gram-negative
Cryptococcus neoformans var. grubii H99 ATCC 2088216microg/ml)
PMID31336137 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/31336137/
RECORD: Rec_0103420 VERIFIED: YES
Provenance & Taxonomy
Australian blue mountains [Animal]
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antimicrobial Antifungal Anticancer Anti-inflammatory
Micrococcus luteus
25 μg/mL
MIC
PaperHost defence peptides from the skin glands of the Australian blue mountains tree-frog Litoria citropa. Solution structure of the antibacterial peptide citropin 1.1.
RECORD: Rec_0106088 VERIFIED: YES
Provenance & Taxonomy
Ranoidea citropa [Animal]
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antimicrobial Anti-Gram-positive Non-hemolytic
Gram-positive bacteria
PMID10504394;11784303 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/10504394/
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