Peptide name : Cr-ACP1

Source/Organism : Not found

Linear/Cyclic : Linear

Chirality : L

Peptide length: 9

C-terminal modification: Linear

N-terminal modification : Not found

Non-natural peptide information: None

Assay type : MTT assay

Assay time : 3h

Activity : IC50 : 1.5 mM

Cell line : Hep2

Cancer type : Human epidermoid cancer

Other activity : Anti-bacterial activity

Amino acid composition bar chart :

Molecular mass : 1050.1639 Dalton

Aliphatic index : 0.866

Instability index : 13.1667

Hydrophobicity (GRAVY) : 0.0444

Isoelectric point : 4.2079

Charge (pH 7) : -1.2029

Aromaticity : 0.222

Molar extinction coefficient (cysteine, cystine): (5500, 5500)

Hydrophobic/hydrophilic ratio : 2

hydrophobic moment : 1.6056

Missing amino acid : C,R,H,Q,T,P,M,I,E,S,Y,N

Most occurring amino acid : D

Most occurring amino acid frequency : 2

Least occurring amino acid : A

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (0.3, 0.3, 0.4)

SMILES Notation: CC(C)C[C@H](NC(=O)[C@H](CCCCN)NC(=O)[C@H](Cc1c[nH]c2ccccc12)NC(=O)[C@H](C)N)C(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CC(=O)O)C(=O)NCC(=O)N[C@H](C(=O)O)C(C)C

1 : Mandal SM, et al. Identification and characterization of a bactericidal and proapoptotic peptide from Cycas revoluta seeds with DNA binding properties. J Cell Biochem. 2012; 113:184-93. doi: 10.1002/jcb.23343

Paper title : Identification and characterization of a bactericidal and proapoptotic peptide from Cycas revoluta seeds with DNA binding properties.

Doi : https://doi.org/10.1002/jcb.23343

Abstract : Nowadays, novel pharmacies have been screened from plants. Among them are the peptides, which show multiple biotechnological activities. In this report, a small peptide (Ala-Trp-Lys-Leu-Phe-Asp-Asp-Gly-Val) with a molecular mass of 1,050 Da was purified from Cycas revoluta seeds by using reversed-phase liquid chromatography. This peptide shows clear deleterious effects against human epidermoid cancer (Hep2) and colon carcinoma cells (HCT15). It caused inhibition of cancer cell proliferation and further disruption of nucleosome structures, inducing apoptosis by direct DNA binding. A remarkable antibacterial activity was also observed in this same peptide. Nevertheless, no significant lysis of normal RBC cells was observed in the presence of peptide. Additionally, an acetylation at the N-termini portion is able to reduce both activities. Bioinformatics tools were also utilized for construction of a three-dimensional model showing a single amphipathic helix. Since in vitro binding studies show that the target of this peptide seems to be DNA, theoretical docking studies were also performed to better understand the interaction between peptide and nucleic acids and also to shed some light on the acetyl group role. Firstly, binding studies showed that affinity contacts basically occur due to electrostatic attraction. The complex peptide-ssDNA was clearly oriented by residues Ala(1), Lys(3), and Asp(6), which form several hydrogen bonds that are able to stabilize the complex. When acetyl was added, hydrogen bonds are broken, reducing the peptide affinity. In summary, it seems that information here provided could be used to design a novel derivative of this peptide which a clear therapeutic potential.