dbacp00304
General Description
Peptide name : Temporin-SHf
Source/Organism : Sahara frog
Linear/Cyclic : linear
Chirality : Not found
Sequence Information
Sequence : FFFLSRIF*
Peptide length: Not available
C-terminal modification: linear
N-terminal modification : Amidation
Non-natural peptide information: None
Activity Information
Assay type : MTT assay
Assay time : 24h
Activity : IC50 : 32.76 ± 1.528 µM
Cell line : MCF-7
Cancer type : Not specified
Other activity : Not found
Physicochemical Properties
Amino Acid Composition Bar Chart : Not available
Molecular mass : Not available
Aliphatic index : Not available
Instability index : Not available
Hydrophobicity (GRAVY) : Not available
Isoelectric point : Not available
Charge (pH 7) : Not available
Aromaticity : Not available
Molar extinction coefficient (cysteine, cystine): Not available
Hydrophobic/hydrophilic ratio : Not available
hydrophobic moment : Not available
Missing amino acid : Not available
Most occurring amino acid : Not available
Most occurring amino acid frequency : Not available
Least occurring amino acid : Not available
Least occurring amino acid frequency : Not available
Structural Information
3D-structure: Not available
Secondary structure fraction (Helix, Turn, Sheet): Not available
SMILES Notation: Not available
Secondary Structure :
| Method | Prediction |
|---|---|
| GOR | Not available |
| Chou-Fasman (CF) | Not available |
| Neural Network (NN) | Not available |
| Joint/Consensus | Not available |
Molecular Descriptors and ADMET Properties
Molecular descriptors: Not available
ADMET properties: Not available
Cross Referencing Databases databases
Pubmed Id : 38319435, .
Uniprot : Not available
CancerPPD : Not available
ApIAPDB : Not available
Reference
1 : Antony A, et al. Antimicrobial and antitumor properties of anuran peptide temporin-SHf induce apoptosis in A549 lung cancer cells. Amino Acids. 2024; 56:12. doi: 10.1007/s00726-023-03373-3
Literature
Paper title : Antimicrobial and antitumor properties of anuran peptide temporin-SHf induce apoptosis in A549 lung cancer cells.
Doi : https://doi.org/10.1007/s00726-023-03373-3
Abstract : Temporin-SHf is a linear, ultra-short, hydrophobic, α-helix, and phe-rich cationic antimicrobial peptide. The antitumor activities and mechanism of temporin-SHf-induced cancer cell death are unknown. The temporin-SHf was synthesized by solid-phase Fmoc chemistry and antimicrobial and antitumor activities were investigated. Temporin-SHf was microbiocidal, non-hemolytic, and cytotoxic to human cancer cells but not to non-tumorigenic cells. It affected the cancer cells' lysosomal integrity and caused cell membrane damage. The temporin-SHf inhibited A549 cancer cell proliferation and migration. It is anti-angiogenic and causes cancer cell death through apoptosis. The molecular mechanism of action of temporin-SHf confirmed that it kills cancer cells by triggering caspase-dependent apoptosis through an intrinsic mitochondrial pathway. Owing to its short length and broad spectrum of antitumor activity, temporin-SHf is a promising candidate for developing a new class of anticancer drugs.