Peptide name : AEM-28

Source/Organism : Synthetic

Linear/Cyclic : Linear

Chirality : L

Peptide length: 28

C-terminal modification: Linear

N-terminal modification : Free

Non-natural peptide information:

Assay type : MTS assay

Assay time : 24-h

Activity : ~50% cell viability at 10 μg/mL

Cell line : SK-OV-3

Cancer type : Ovarian Cancer

Other activity : Anti-inflammatory and Anticancer

Amino acid composition bar chart :

Molecular mass : 3535.2357 Dalton

Aliphatic index : 1.046

Instability index : 48.2361

Hydrophobicity (GRAVY) : -0.7

Isoelectric point : 10.370

Charge (pH 7) : 5.7609

Aromaticity : 14.28

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

Hydrophobic/hydrophilic ratio : 0.8667

hydrophobic moment : 0.2541

Missing amino acid : C,G,H,I,M,N,P,Q,S,T

Most occurring amino acid : L

Most occurring amino acid frequency : 6

Least occurring amino acid : W

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (60., 7.1, 39.)

SMILES Notation: CC(C)C[C@H](NC(=O)[C@H](Cc1c[nH]c2ccccc12)NC(=O)[C@H](CC(=O)O)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@@H](N)CC(C)C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@@H](Cc1ccc(O)cc1)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CCCCN)C(=O)N[C@H](C(=O)N[C@@H](C)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](C)C(=O)N[C@@H](Cc1ccccc1)C(=O)O)C(C)C

1 : Su F, et al. Bovine HDL and Dual Domain HDL-Mimetic Peptides Inhibit Tumor Development in Mice. J Cancer Res Ther Oncol. 2020; 8:(unknown pages). doi: 10.17303/jcrto.2020.8.101

Paper title : Bovine HDL and Dual Domain HDL-Mimetic Peptides Inhibit Tumor Development in Mice.

Doi : https://doi.org/10.17303/jcrto.2020.8.101

Abstract : A growing body of literature supports the role of apolipoproteins present in HDL in the treatment of pro-inflammatory diseases including cancer. We examined whether bovine HDL (bHDL) and three dual-domain peptides, namely AEM-28 and its analog AEM-28-2, and HM-10/10, affect tumor growth and development in mouse models of ovarian and colon cancer. We demonstrate that bHDL inhibits mouse colorectal cancer cell line CT26-mediated lung tumor development, and mouse ovarian cancer cell line ID8-mediated tumor burden. We also demonstrate that, although to different degrees, dual-domain peptides inhibit cell viability of mouse and human ovarian and colon cancer cell lines, but not that of normal human colonic epithelial cells or NIH3T3 mouse fibroblasts. Dual-domain peptides administered subcutaneously or in a chow diet decrease CT26 cell-mediated tumor burden, tumor growth, and tumor dissemination in BALB/c mice. Plasma levels of lysophosphatidic acid (LPA) are significantly reduced in mice that received bHDL and the dual-domain peptides, suggesting that reduction by effecting accumulation and/or synthesis of pro-inflammatory lipids may be one of the mechanisms for the inhibition of tumor development by bHDL and the dual-domain peptides. Our studies suggest that therapeutics based on apolipoproteins present in HDL may be novel agents for the treatment of epithelial adenocarcinomas of the ovary and colon.