Peptide name : A4K14 - Citropin 1.1 - Sp 1

Source/Organism : Synthetic

Linear/Cyclic : Cyclic

Chirality : L

Peptide length: Not available

C-terminal modification: Cyclic

N-terminal modification : Amidation

Non-natural peptide information: S5= (S)-2-(4-pentenyl)alanine

Assay type : CCK-8 assay

Assay time : 24-h

Activity : IC50 = 8.94 µM

Cell line : C4-2B

Cancer type : Prostate Cancer

Other activity : Antimicrobial and Anticancer

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 N, et al. Design, Synthesis, and Antitumor Activities Study of Stapled A4K14-Citropin 1.1 Peptides. Front Chem. 2020; 8:616147. doi: 10.3389/fchem.2020.616147

Paper title : Design, Synthesis, and Antitumor Activities Study of Stapled A4K14-Citropin 1.1 Peptides.

Doi : https://doi.org/10.3389/fchem.2020.616147

Abstract : A4K14-citropin 1.1 is a structurally optimized derivative derived from amphibians' skin secreta peptide Citropin, which exhibits broad biological activities. However, the application of A4K14-citropin 1.1 as a cancer therapeutic is restricted by its structural flexibility. In this study, a series of all-hydrocarbon stapled peptides derivatives of A4K14-citropin 1.1 were designed and synthesized, and their chemical and biological characteristics were also investigated. Among them, A4K14-citropin 1.1-Sp1 and A4K14-citropin 1.1-Sp4 displayed improved helicity levels, greater protease stability, and increased antitumor activity compared with the original peptide, which establishes them as promising lead compounds for novel cancer therapeutics development. These results revealed the important influence of all-hydrocarbon stapling side chain on the secondary structure, hydrolase stability, and biological activity of A4K14-citropin 1.1.