Peptide name : 4-arm branched peptide

Source/Organism : Synthetic

Linear/Cyclic : Linear

Chirality : L

Peptide length: Not available

C-terminal modification: Linear

N-terminal modification : Free

Non-natural peptide information: thermal oxidation between the thiol group of cysteine residue in the two 2-arm branched

Assay type : MTT assay

Assay time : 48-h

Activity : Cell Viability (%) ~ 51.4 ± 4.2 at 30 µg/mL

Cell line : Bcap-37

Cancer type : Breast Cancer

Other activity : Antimicrobial

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

3D-structure: Not available

Secondary structure fraction (Helix, Turn, Sheet): Not available

SMILES Notation: Not available

Molecular descriptors: Not available

ADMET properties: Not available

1 : Wang X, et al. Branched α-helical peptides enhanced antitumor efficacy and selectivity. Biomater Sci. 2020; 8:6387-6394. doi: 10.1039/d0bm00629g

Paper title : Branched α-helical peptides enhanced antitumor efficacy and selectivity.

Doi : https://doi.org/10.1039/d0bm00629g

Abstract : Drug resistance to traditional chemotherapeutics is one of the main challenges in cancer treatment. Herein, cationic antimicrobial peptides (CAPs) were repurposed as anticancer agents to counter chemotherapy drug resistance. After a systematic study of de novo designed synthetic α-helical CAPs in various cell lines, the 4-arm branched peptide {[(LLKK)2]2κC}2 was found to exhibit better selectivity compared to its linear counterpart (LLKK)4, and was more effective than the 2-arm branched peptide [(LLKK)2]2κC. In particular, the 4-arm branched peptide could counter drug resistance and kill multiple drug resistant cells. Mechanism studies reveal that these α-helical peptides killed both the parent and resistant cancer cells based on the apoptotic pathway. The in vivo study in mice bearing breast tumors showed that branched peptides could be retained at the tumour sites after intratumoral injection and significantly reduced tumor growth while exhibiting minimal toxicity on main organs. These results indicate that the 4-arm branched peptide is a promising candidate for anticancer therapy.