dbACP: A Comprehensive Database of Anti-Cancer Peptides

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.