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MYP_109022
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Basic Information
Hadrurin
Anticancer ▸ Cytotoxic anticancer activity ▸ Cytotoxic
Antimicrobial
Antimicrobial ▸ Antibacterial
Antimicrobial ▸ Antibacterial ▸ Anti-Gram-negative
Antimicrobial ▸ Antibacterial ▸ Anti-Gram-positive
Antimicrobial ▸ Antibiotic activity
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
Venom / Toxin ▸ General toxin ▸ Toxicity
Standard
41 amino acids
C199H333N57O57
Standard
Sequence
GILDTIKSIASKVWNSKTVQDLKRKGINWVANKLGVSPQAA
Physicochemical Analysis
4436.12 Da
10.30
4.76
4.54
0.1160
-0.20
0.63
0.01
28.54
104.63
0.0488
11000.00
11000.00
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
1879.56
-19.46
65.0
62.0
152.0
313.0
5.0
45.0
Structural Visualization
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0292272 VERIFIED: NO
Provenance & Taxonomy
not reported [other]
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
None
None
Bio-Activity Profile
Antimicrobial Antibacterial Toxic Anti-Gram-positive Cytotoxic Anti-Gram-negative
PaperCAMP: Collection of sequences and structures of antimicrobial peptides PMID24265220 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/24265220/
RECORD: Rec_0300966 VERIFIED: YES
Provenance & Taxonomy
Hadrurus aztecus [Animal]
Structure & Mods
linear peptide [Linear]
mixed L/D amino-acid peptide [Mixed]
Amidation
Reported to be the first antimicrobial peptide ever purified from scorpion venom. Host expression:constitutive: The scorpion makes hadrurin as a cytolytic poison for an attack of its prey and as an antimicrobial defense molecule to stop putative invasive microorganisms
Bio-Activity Profile
Antimicrobial
S. marscencens ATCC 13880
10 μM
MIC
PaperHadrurin, a new antimicrobial peptide from the venom of the scorpion Hadrurus aztecus.
RECORD: Rec_0319674 VERIFIED: NO
Provenance & Taxonomy
Hadrurus aztecus [Animal]
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antimicrobial
PaperPatent US 7862826 B2 Evidence URLhttps://patents.google.com/patent/US7862826B2/en PatentUS 7862826 B2
RECORD: Rec_0334984 VERIFIED: YES
Provenance & Taxonomy
Hadrurus aztecus [Animal]
Structure & Mods
linear peptide [Linear]
mixed L/D amino-acid peptide [Mixed]
Amidation
Reported to be the first antimicrobial peptide ever purified from scorpion venom. Host expression:constitutive: The scorpion makes hadrurin as a cytolytic poison for an attack of its prey and as an antimicrobial defense molecule to stop putative invasive microorganisms
Bio-Activity Profile
Antimicrobial Toxicity
human RBC: highly hemolytic, 80% hemolysis at 20 uM
<10 μM
HC50
PaperHadrurin, a new antimicrobial peptide from the venom of the scorpion Hadrurus aztecus.
RECORD: Rec_0337644 VERIFIED: YES
Provenance & Taxonomy
not reported [other]
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antimicrobial Antibacterial
PaperTorres-Larios A., Gurrola G.B., Zamudio F.Z., Possani L.D.;. "Hadrurin, a new antimicrobial peptide from the venom of the scorpion Hadrurus aztecus."; Eur. J. Biochem. 267:5023-5031(2000). Evidence URLhttps://www.uniprot.org/uniprotkb/HADR_HADAZ/entry
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