Peptide name : (LLKK)4 linear peptide

Source/Organism : Synthetic

Linear/Cyclic : Linear

Chirality : L

Peptide length: 16

C-terminal modification: Linear

N-terminal modification : Amidation

Non-natural peptide information:

Assay type : MTT assay

Assay time : 48-h

Activity : Cell Viability (%) ~ 15.07 ± 0.5 at 30 µg/mL

Cell line : Bcap-37

Cancer type : Breast Cancer

Other activity : Antimicrobial

Amino acid composition bar chart :

Molecular mass : 1948.6545 Dalton

Aliphatic index : 1.95

Instability index : -27.768

Hydrophobicity (GRAVY) : -0.05

Isoelectric point : 10.845

Charge (pH 7) : 7.7521

Aromaticity : 0

Molar extinction coefficient (cysteine, cystine): (0, 0)

Hydrophobic/hydrophilic ratio : 1

hydrophobic moment : -0.880

Missing amino acid : A,C,D,E,F,G,H,I,M,N,P,Q,R,S,T,V,W,Y

Most occurring amino acid : L

Most occurring amino acid frequency : 8

Least occurring amino acid : L

Least occurring amino acid frequency : 8

Secondary structure fraction (Helix, Turn, Sheet): (100, 0, 50)

SMILES Notation: CC(C)C[C@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](N)CC(C)C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCCN)C(=O)O

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.