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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_0380297 VERIFIED: NO
Provenance & Taxonomy
not reported [other]
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
None
Amidation
Bio-Activity Profile
Antimicrobial
PaperAPD2: the updated antimicrobial peptide database and its application in peptide design PMID18957441 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/18957441/
RECORD: Rec_0387279 VERIFIED: YES
Provenance & Taxonomy
Lithobates catesbeianus [Animal]; synthetic construct [Synthetic]
Temporins
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
None
Amidation
Bio-Activity Profile
Anticancer
SMMC-7721 (liver cancer)
50 μg/mL
MTT/MTS 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_0401645 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 Cytotoxic
A-549
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_0403856 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
HeLa (52.32 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/
RECORD: Rec_0410907 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
(57.62 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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