Peptide name : Human A-defensin-1 (HNP1)

Source/Organism : Not found

Linear/Cyclic : Linear

Chirality : L

Peptide length: 30

C-terminal modification: Linear

N-terminal modification : Not found

Non-natural peptide information: None

Assay type : MTT assay

Assay time : 48h

Activity : Not found

Cell line : A549

Cancer type : Lung cancer

Other activity : Not found

Amino acid composition bar chart :

Molecular mass : 3448.077 Dalton

Aliphatic index : 0.653

Instability index : 55.71

Hydrophobicity (GRAVY) : 0.3

Isoelectric point : 8.6783

Charge (pH 7) : 2.7362

Aromaticity : 0.166

Molar extinction coefficient (cysteine, cystine): (9970, 10345)

Hydrophobic/hydrophilic ratio : 2

hydrophobic moment : -0.040

Missing amino acid : H,M,K,S,D,N,V

Most occurring amino acid : C

Most occurring amino acid frequency : 6

Least occurring amino acid : P

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (0.2, 0.1, 0.3)

SMILES Notation: CC[C@H](C)[C@H](NC(=O)[C@H](CS)NC(=O)[C@H](C)NC(=O)[C@@H]1CCCN1C(=O)[C@@H](NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](CS)NC(=O)[C@H](Cc1ccc(O)cc1)NC(=O)[C@H](CS)NC(=O)[C@H](C)N)[C@@H](C)CC)C(=O)N[C@@H](C)C(=O)NCC(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](Cc1ccc(O)cc1)C(=O)NCC(=O)N[C@H](C(=O)N[C@@H](CS)C(=O)N[C@H](C(=O)N[C@@H](Cc1ccc(O)cc1)C(=O)N[C@@H](CCC(N)=O)C(=O)NCC(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](Cc1c[nH]c2ccccc12)C(=O)N[C@@H](C)C(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@@H](CS)C(=O)N[C@@H](CS)C(=O)O)[C@@H](C)CC)[C@@H](C)O

1 : Xu N, et al. Human alpha-defensin-1 inhibits growth of human lung adenocarcinoma xenograft in nude mice. Mol Cancer Ther. 2008; 7:1588-97. doi: 10.1158/1535-7163.MCT-08-0010

Paper title : Human alpha-defensin-1 inhibits growth of human lung adenocarcinoma xenograft in nude mice.

Doi : https://doi.org/10.1158/1535-7163.MCT-08-0010

Abstract : Human alpha-defensin-1 (HNP1), a small antimicrobial peptide, shows cytotoxicity to tumor cells in vitro and inhibitory activity for pathologic neovascularization in vivo. Here, we did a gene therapy with a plasmid that expresses a secretable form of HNP1 for assaying its antitumor activity. The expression and secretion of HNP1 were determined by reverse transcription-PCR and ELISA in vitro. We found that expression of HNP1 in A549 tumor cells caused significant growth inhibition. This effect is most likely cell autonomous, as a significant amount of recombinant HNP1 protein was found to be accumulated in the cytoplasm by immunohistochemical staining using an anti-HNP1 antibody and the supernatant containing secreted HNP1 failed to produce any noticeable antitumor activity. Flow cytometry and Hoechst 33258 staining showed that the number of apoptotic cells among the A549 cells expressing recombinant HNP1 proteins was significantly greater than that of the nontransfected control cultures, suggesting that this growth-inhibitory activity was due to an apoptotic mechanism triggered by the intracellular HNP1. The antitumor activity of intracellularly expressed HNP1 was also shown in vivo. Decreased microvessel density and increased lymphocyte infiltration were observed in tumor tissue from HNP1-treated mice through histologic analysis. These results indicate that intracellularly expressed HNP1 induces tumor cell apoptosis, which inhibits tumor growth. The antiangiogenesis effect of HNP1 may contribute to its inhibitory activity in vivo, and HNP1 might involve the host immune response to tumor. These findings provide a rationale for developing HNP1-based gene therapy for cancer.