Peptide name : Pseudosubstrate Peptides Inhibit Akt )

Source/Organism : Human FOXO3, AKTide-2T

Linear/Cyclic : Linear

Chirality : L

Peptide length: 20

C-terminal modification: Linear

N-terminal modification : Not found

Non-natural peptide information: None

Assay type : Akt kinase

Assay time : Not found

Activity : Not found

Cell line : HeLa

Cancer type : Not specified

Other activity : Not found

Amino acid composition bar chart :

Molecular mass : 2463.6154 Dalton

Aliphatic index : 0.39

Instability index : 32.12

Hydrophobicity (GRAVY) : -1.395

Isoelectric point : 4.6426

Charge (pH 7) : -3.1664

Aromaticity : 0.15

Molar extinction coefficient (cysteine, cystine): (1490, 1490)

Hydrophobic/hydrophilic ratio : 0.66666666

hydrophobic moment : 0.1764

Missing amino acid : C,W,Q,M,I,K,S,N

Most occurring amino acid : E

Most occurring amino acid frequency : 4

Least occurring amino acid : V

Least occurring amino acid frequency : 1

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

SMILES Notation: CC(C)C[C@H](NC(=O)[C@H](CCC(=O)O)NC(=O)[C@@H](N)C(C)C)C(=O)N[C@@H](CC(=O)O)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@@H](CCC(=O)O)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@H](C(=O)N[C@@H](Cc1ccc(O)cc1)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](Cc1ccccc1)C(=O)NCC(=O)N[C@@H](Cc1c[nH]cn1)C(=O)O)[C@@H](C)O

1 : Luo Y, et al. Pseudosubstrate peptides inhibit Akt and induce cell growth inhibition. Biochemistry. 2004; 43:1254-63. doi: 10.1021/bi034515p

Paper title : Pseudosubstrate peptides inhibit Akt and induce cell growth inhibition.

Doi : https://doi.org/10.1021/bi034515p

Abstract : We have designed peptide inhibitors that potently inhibit Akt both in vitro and inside cells. These peptide inhibitors are selective for Akt versus other closely related kinases. The peptides inhibit the in vitro phosphorylation of a biotinylated Bad peptide by Akt with potency up to 100 nM. We have shown that the binding between Akt1 and these peptide inhibitors requires MgATP. Mutating the two putative Akt phosphorylation sites to Ala (nonsubstrate) in these peptides increases the inhibitory potency while mutating the sites to aspartic acid (phosphorylation mimetic) reduces the potency. When delivered into cells, these peptide inhibitors can inhibit cellular Akt activity and cell growth. Thus, these Akt-specific peptide inhibitors provide prototypes for peptide mimetic drugs as well as very useful tools to dissect cellular functions of Akt.