The ebw peptide has four amino acid substitutions in comparison to pM2c, but in general the electronic density distribution was not significantly affected. Conversely, the replacement of tyrosine (Y) by alanine (A) and serine (S) by glycine (G) reduced drastically the volume in the right moiety of ebw, affecting its molecular shape when compared to the other two peptides grouped in the same cluster. The t0v peptide has only one substitution in comparison to pM2c sequence, an isoleucine (I)

instead of alanine (A), both are hydrophobic residues. Even isoleucine having a larger side chain than alanine the molecular shape was not severely affected. The MLP property Akt phosphorylation gives the information of molecular hydrophilic/hydrophobic balance and can also be explained

using a color scheme, where blue color corresponds to hydrophilic regions and green color to hydrophobic regions. The lipophilicity can be numerically expressed by the calculated n-octanol/water selleck inhibitor partition coefficient (ClogP). And, the three peptides models presented low ClogP values, indicating a more hydrophilic character. There is a gradient regarding the ClogP values: ebw (ClogP = −1.03) < pM2c (ClogP = −0.57) < t0v (ClogP = 0.77). In Fig. 6 are presented the findings discussed till now. The blue group, which shares 47% similarity, has six peptides models, as follows: jyj (YAVQYSC), z24 (YAINYNC), gka (YSCVYSC), s44 (YACLYSC), hzr (YALVYSC), iiu (YALHYSC). The RMSD value was also lower than 1 Å this website (0.44 Å) for this cluster. The substitution at fourth position seems to be the main difference, particularly for the peptide iiu, which has a histidine residue (positive charged) in this place. The blue color on this region can be visualized through the MEP property (Fig. 7). pM2c has a glycine (G) as fourth amino acid residue, which has hydrogen

as side chain (non-substituted). The peptides jyj and z24 present a glutamine (Q) and asparagine (N) residue, respectively, in that position. These residues are polar and uncharged. On the other hand, the peptides gka, s44, and hzr have hydrophobic amino acids at fourth position (valine, V; leucine, L). Despite that, the character more hydrophilic remained also for this group, the ClogP values ranged from −1.85 to 0.81. The green group (similarity 66%) is composed by the peptides kxo (YIIGYFC) and bbp (YIIGYYC), and presented RMSD value equal to 0.51 Å. This grouping was a little bit more distant than the rest of data set probably due to the substitution of the sixth amino acid residue. These two peptides have hydrophobic and bulky residues in this position, like phenylalanine (F) and tyrosine (Y), providing also higher ClogP values (3.17 for bbp and 3.47 for kxo) (see Fig. 8). The pM2c peptide has a serine (S) in this position, which is a polar uncharged residue.