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MYP_074881
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Basic Information
CA(1-7)M(2-9)
Anticancer
Anticancer ▸ Cytotoxic anticancer activity ▸ Cytotoxic
Antimicrobial
Antimicrobial ▸ Antibacterial
Antimicrobial ▸ Antibacterial ▸ Anti-Gram-negative
Antimicrobial ▸ Antibacterial ▸ Anti-Gram-positive
Antimicrobial ▸ Antibacterial ▸ Anti-Mycobacterium
Antimicrobial ▸ Anti-biofilm ▸ Biofilm inhibition
Antimicrobial ▸ Antifungal
Antiparasitic ▸ Anti-Leishmania ▸ Antileishmanial
Antiparasitic ▸ Antimalarial
Antiparasitic ▸ Antiprotozoal ▸ Antimalarial ▸ Anti-Plasmodium
Antiparasitic ▸ General antiparasitic ▸ Antiparasitic
Toxicity / Safety ▸ Blood cell toxicity ▸ Hemolysis ▸ Hemolytic
Toxicity / Safety ▸ Cytotoxicity ▸ Cytotoxic
Venom / Toxin ▸ General toxin ▸ Cytotoxic
Venom / Toxin ▸ General toxin ▸ Toxic
Standard
15 amino acids
C89H151N21O16
Standard
Sequence
KWKLFKKIGAVLKVL
Physicochemical Analysis
1771.28 Da
10.60
4.76
4.54
0.3170
0.54
0.69
0.15
-28.99
149.33
0.1333
5500.00
5500.00
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
616.61
0.94
22.0
21.0
63.0
126.0
3.0
14.0
Structural Visualization
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0002652 VERIFIED: YES
Provenance & Taxonomy
not reported [other]
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
None
Amidation
Bio-Activity Profile
Antimicrobial
Sheep erythrocytes
40.2 μM
Paperhttps://pubmed.ncbi.nlm.nih.gov/20617807/ PMID20617807 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/20617807/
RECORD: Rec_0005603 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
Cecropin/Melittin hybrid
32630
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
None
Amidation
Lauryl at 1st lysine
Bio-Activity Profile
Antimicrobial Antibacterial Antifungal Antiparasitic Antileishmanial
Leishmania donovani MHOM/SD/00/1S-2D (amastigote)
1.3 μM
LD50; MTT assay
PaperN-terminal fatty acid substitution increases the leishmanicidal activity of CA(1-7)M(2-9), a cecropin-melittin hybrid peptide PMID11502512 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/11502512/
RECORD: Rec_0013219 VERIFIED: YES
Provenance & Taxonomy
Synthetic construct based on Other derivatives [Synthetic]
Cecropin
32630
Structure & Mods
linear peptide [Linear]
noncanonical stereochemical modification [Modified]
bacteria: The peptide forms pore on membranes. Structure: helical in 20% hexafluoroisopropanol (HFIP). You can rotate, zoom, and view the 3D structure bound to DPC micelles here in the PDB. In vitro toxicity: sheep RBC (LC >300 uM), not hemo.lytic. Surface immobilized peptide: It has been surface immobilized 2016 onto gold nanoparticles at a high density of 110 ug/cm2 with a braod activity spectrum (Rai A et al., 2016). Chemical modification: Succinylation of the amino acids at the N-terminus and lysine side chains inhibits the effect of this peptide on liposome permeability. This modification appears to block the formation of helical structure in liposome. Updated Jan2025
Bio-Activity Profile
Antimicrobial Antiparasitic
Escherichia coli ATCC 25922 or 23506
1-2 μg/mL
MIC
PaperShortened cecropin A-melittin hybrids. Significant size reduction retains potent antibiotic activity.
RECORD: Rec_0014288 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
Cecropin/Melittin hybrid
32630
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Trimethylation
Amidation
Lysine Nepsilon-Trimethylation
Bio-Activity Profile
Antimicrobial Antiparasitic Antimalarial Antileishmanial
Plasmodium falciparum
>50 μM
IC50; MTT assay
PaperLysine N(epsilon)-trimethylation, a tool for improving the selectivity of antimicrobial peptides PMID20617807 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/20617807/
RECORD: Rec_0016353 VERIFIED: YES
Provenance & Taxonomy
not reported [other]
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antimicrobial Antibacterial
PaperD.A.Devine, P.D.Marsh, R.S.Percival, M.Rangarajan, M.A.Curtis. ?Modulation of antibacterial peptide activity by products of Porphyromonas gingivalis and Prevotella ssp.?Microbiology, 145, 965-971.
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