Peptide name : peptide containing the BH3 regions from Bad

Source/Organism : BH3-only, Sensizers (BAD, HRK, Noxa)

Linear/Cyclic : Linear

Chirality : L

Peptide length: 26

C-terminal modification: Linear

N-terminal modification : Not found

Non-natural peptide information: None

Assay type : Cell viability assay

Assay time : Not found

Activity : Not found

Cell line : FL5.12

Cancer type : Not specified

Other activity : Not found

Amino acid composition bar chart :

Molecular mass : 3117.4554 Dalton

Aliphatic index : 0.526

Instability index : 44.0692

Hydrophobicity (GRAVY) : -0.976

Isoelectric point : 8.5869

Charge (pH 7) : 0.7676

Aromaticity : 0.153

Molar extinction coefficient (cysteine, cystine): (6990, 6990)

Hydrophobic/hydrophilic ratio : 0.85714285

hydrophobic moment : 1.2694

Missing amino acid : C,H,T,P,I,V

Most occurring amino acid : R

Most occurring amino acid frequency : 4

Least occurring amino acid : N

Least occurring amino acid frequency : 1

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

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

1 : Kelekar A, et al. Bad is a BH3 domain-containing protein that forms an inactivating dimer with Bcl-XL. Mol Cell Biol. 1997; 17:7040-6. doi: 10.1128/MCB.17.12.7040

Paper title : Bad is a BH3 domain-containing protein that forms an inactivating dimer with Bcl-XL.

Doi : https://doi.org/10.1128/MCB.17.12.7040

Abstract : The Bcl-2 related protein Bad is a promoter of apoptosis and has been shown to dimerize with the anti-apoptotic proteins Bcl-2 and Bcl-XL. Overexpression of Bad in murine FL5.12 cells demonstrated that the protein not only could abrogate the protective capacity of coexpressed Bcl-XL but could accelerate the apoptotic response to a death signal when it was expressed in the absence of exogenous Bcl-XL. Using deletion analysis, we have identified the minimal domain in the murine Bad protein that can dimerize with Bcl-xL. A 26-amino-acid peptide within this domain, which showed significant homology to the alpha-helical BH3 domains of related apoptotic proteins like Bak and Bax, was found to be necessary and sufficient to bind Bcl-xL. To determine the role of dimerization in regulating the death-promoting activity of Bad and the death-inhibiting activity of Bcl-xL, mutations within the hydrophobic BH3-binding pocket in Bcl-xL that eliminated the ability of Bcl-xL to form a heterodimer with Bad were tested for the ability to promote cell survival in the presence of Bad. Several of these mutants retained the ability to impart protection against cell death regardless of the level of coexpressed Bad protein. These results suggest that BH3-containing proteins like Bad promote cell death by binding to antiapoptotic members of the Bcl-2 family and thus inhibiting their survival promoting functions.