Peptide name : DRS S1

Source/Organism : Dermaseptins B

Linear/Cyclic : Linear

Chirality : L

Peptide length: 34

C-terminal modification: Linear

N-terminal modification : Free

Non-natural peptide information: None

Assay type : Thymidine incorporation assay

Assay time : 6h

Activity : Not found

Cell line : MCF-7

Cancer type : Breast cancer

Other activity : Anti-microbial activity

Amino acid composition bar chart :

Molecular mass : 3455.0584 Dalton

Aliphatic index : 0.923

Instability index : 1.8471

Hydrophobicity (GRAVY) : 0.1853

Isoelectric point : 10.001

Charge (pH 7) : 2.8802

Aromaticity : 0.029

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

Hydrophobic/hydrophilic ratio : 1.61538461

hydrophobic moment : -0.599

Missing amino acid : C,R,P,E,F,Y,N,V

Most occurring amino acid : A

Most occurring amino acid frequency : 8

Least occurring amino acid : W

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (0.5, 0.1, 0.3)

SMILES Notation: CC[C@H](C)[C@H](NC(=O)[C@@H](NC(=O)[C@H](CC(=O)O)NC(=O)[C@H](C)NC(=O)[C@H](C)NC(=O)[C@H](C)NC(=O)CNC(=O)[C@H](CC(C)C)NC(=O)[C@H](C)NC(=O)[C@H](C)NC(=O)[C@H](CCCCN)NC(=O)CNC(=O)[C@H](C)NC(=O)[C@H](Cc1c[nH]cn1)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](C)NC(=O)[C@H](CCSC)NC(=O)[C@@H](NC(=O)CNC(=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](CCSC)NC(=O)[C@@H](NC(=O)[C@H](CCCCN)NC(=O)[C@H](Cc1c[nH]c2ccccc12)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](C)N)[C@@H](C)O)[C@@H](C)O)[C@@H](C)O)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCC(N)=O)C(=O)NCC(=O)N[C@H](C(=O)N[C@@H](CCC(N)=O)C(=O)O)[C@@H](C)O

1 : Charpentier S, et al. Structure, synthesis, and molecular cloning of dermaseptins B, a family of skin peptide antibiotics. J Biol Chem. 1998; 273:14690-7. doi: 10.1074/jbc.273.24.14690

Paper title : Structure, synthesis, and molecular cloning of dermaseptins B, a family of skin peptide antibiotics.

Doi : https://doi.org/10.1074/jbc.273.24.14690

Abstract : Analysis of antimicrobial activities that are present in the skin secretions of the South American frog Phyllomedusa bicolor revealed six polycationic (lysine-rich) and amphipathic alpha-helical peptides, 24-33 residues long, termed dermaseptins B1 to B6, respectively. Prepro-dermaseptins B all contain an almost identical signal peptide, which is followed by a conserved acidic propiece, a processing signal Lys-Arg, and a dermaseptin progenitor sequence. The 22-residue signal peptide plus the first 3 residues of the acidic propiece are encoded by conserved nucleotides encompassed by the first coding exon of the dermaseptin genes. The 25-residue amino-terminal region of prepro-dermaseptins B shares 50% identity with the corresponding region of precursors for D-amino acid containing opioid peptides or for antimicrobial peptides originating from the skin of distantly related frog species. The remarkable similarity found between prepro-proteins that encode end products with strikingly different sequences, conformations, biological activities and modes of action suggests that the corresponding genes have evolved through dissemination of a conserved "secretory cassette" exon.