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MYP_137230
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Basic Information
Unnamed
Anticancer
Antimicrobial
Antimicrobial ▸ Antibacterial
Antimicrobial ▸ Antifungal
Toxicity / Safety ▸ Cytotoxicity ▸ Cytotoxic
Standard
13 amino acids
C78H134N20O17
Standard
Sequence
LLRHVVKILEKYL
Physicochemical Analysis
1624.02 Da
9.70
1.85
1.59
0.1421
0.60
0.82
0.11
44.93
194.62
0.0769
1490.00
1490.00
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
612.67
0.06
22.0
20.0
56.0
115.0
2.0
12.0
Structural Visualization
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0088056 VERIFIED: NO
Provenance & Taxonomy
Lithobates catesbeianus [Animal]
Temporin
Structure & Mods
Single-chain peptide backbone represented as a linear sequence entry [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antimicrobial
PaperZhao R-L, Han J-Y, Han W-Y, He H-X, Ma J-F (2011) Effects of Two Novel Peptides from Skin of Lithobates Catesbeianus on Tumor Cell Morphology and Proliferation. Molecular Cloning - Selected Applications in Medicine and Biology. Evidence URLhttps://camp.bicnirrh.res.in/seqDisp.php?id=CAMPSQ3791
RECORD: Rec_0089184 VERIFIED: YES
Provenance & Taxonomy
Lithobates catesbeianus [Animal]
Temporin
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antimicrobial Antifungal Anticancer
Also, B-subtitlis
>64 μM
MIC
PaperEffects of Two Novel Peptides from Skin of Lithobates Catesbeianus on Tumor Cell Morphology and Proliferation
RECORD: Rec_0121651 VERIFIED: YES
Provenance & Taxonomy
Lithobates catesbeianus [Animal]; synthetic construct [Synthetic]
Temporin
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
None
Amidation
Bio-Activity Profile
Anticancer
HL7702
50 μg/mL
inhibition assay
PaperWang C et al. Designed synthetic analogs of the alpha-helical peptide temporin-La with improved antitumor efficacies via charge modification and incorporation of the integrin alpha-v beta-3 homing domain. J Pept Sci. 2012. PMID22641352 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/22641352/
RECORD: Rec_0138997 VERIFIED: YES
Provenance & Taxonomy
Lithobates catesbeianus [Animal]
Temporin
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antimicrobial Antifungal Anticancer Antibacterial
Staphylococcus aureus ATCC 25923
2.5 μg/mL
MIC
PaperEffects of Two Novel Peptides from Skin of Lithobates Catesbeianus on Tumor Cell Morphology and Proliferation
RECORD: Rec_0157328 VERIFIED: YES
Provenance & Taxonomy
Lithobates catesbeianus [Animal]; synthetic construct [Synthetic]
Temporin
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
None
Amidation
Bio-Activity Profile
Antimicrobial Anticancer
SMMC-7721 (52.77 Inhibition ratio at 50 μg/ml)
MTT/MTS cell-proliferation and cytotoxicity assay
PaperWang C et al. Designed synthetic analogs of the alpha-helical peptide temporin-La with improved antitumor efficacies via charge modification and incorporation of the integrin alpha-v beta-3 homing domain. J Pept Sci. 2012. PMID22641352 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/22641352/
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