Peptide name : LB-DR5-1

Source/Organism : Not found

Linear/Cyclic : Linear

Chirality : L

Peptide length: 20

C-terminal modification: Linear

N-terminal modification : Not found

Non-natural peptide information: None

Assay type : Not specified

Assay time : Not found

Activity : IC50 : 6 nM

Cell line : SK-MES-1

Cancer type : Not specified

Other activity : Not found

Amino acid composition bar chart :

Molecular mass : 2323.8413 Dalton

Aliphatic index : 0.44

Instability index : 64.255

Hydrophobicity (GRAVY) : 0.125

Isoelectric point : 6.0483

Charge (pH 7) : -0.2677

Aromaticity : 0.05

Molar extinction coefficient (cysteine, cystine): (5500, 5625)

Hydrophobic/hydrophilic ratio : 1.5

hydrophobic moment : 0.0583

Missing amino acid : R,H,P,I,F,Y,G

Most occurring amino acid : M

Most occurring amino acid frequency : 4

Least occurring amino acid : Q

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (0.5, 0.1, 0.2)

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

1 : Li B, et al. Activation of the proapoptotic death receptor DR5 by oligomeric peptide and antibody agonists. J Mol Biol. 2006; 361:522-36. doi: 10.1016/j.jmb.2006.06.042

Paper title : Activation of the proapoptotic death receptor DR5 by oligomeric peptide and antibody agonists.

Doi : https://doi.org/10.1016/j.jmb.2006.06.042

Abstract : The cell-extrinsic apoptotic pathway triggers programmed cell death in response to certain ligands that bind to cell-surface death receptors. Apoptosis is essential for normal development and homeostasis in metazoans, and furthermore, selective activation of the cell-extrinsic pathway in tumor cells holds considerable promise for cancer therapy. We used phage display to identify peptides and synthetic antibodies that specifically bind to the human proapoptotic death receptor DR5. Despite great differences in overall size and structure, the DR5-binding peptides and antibodies shared a tripeptide motif, which was conserved within a disulfide-constrained loop of the peptides and the third complementarity determining region of the antibody heavy chains. The X-ray crystal structure of an antibody in complex with DR5 revealed that the tripeptide motif is buried at the core of the interface, confirming its central role in antigen recognition. We found that certain peptides and antibodies exhibited potent proapoptotic activity against DR5-expressing SK-MES-1 lung carcinoma cells. These phage-derived ligands may be useful for elucidating DR5 activation at the molecular level and for creating synthetic agonists of proapoptotic death receptors.