## 3 Results and Discussion
### Molecular Docking Analysis between Ligands (ACA, MAY, and LUT) with Maltase-Glucoamylase (MGA)  
The binding energy of the ACA, MAY, and LUT with NtMGAM were obtained through molecular docking analysis. A negative value of the binding energy in the coupling indicates that the systems are stable and that there is a favorable interaction between the protein and ligands in the active site. The obtained values for the binding energy were \(-7.8\) kcal/mol for ACA, \(-9.1\) kcal/mol for MAY, and \(-7.7\) kcal/mol for LUT. As can be observed, all the binding affinity values are negatives, which is a characteristic of stable  
Figure 3: Electrostatic potential mapped on the electron density surface for (**A**) acarbose (ACA), (**B**) maysin (MAY) and (**C**) luteolin (LUT) calculated at the M06/6-31G(d) level of theory. The color range represents values from \(-4.000\times\)\(10^{-2}\) to \(5.000\times\)\(10^{-2}\): blue = hydrogen donor zones and red = hydrogen acceptor zones. complexes. Of the new alternatives for diabetes proposed in this work (MAY or LUT), the MAY presented the greatest binding energy absolute value with the active site, even greater than the obtained value for the acarbose (ACA), which is the most used treatment for diabetes. As is well known, the greater the affinity of the ligand for the protein, the easier the binding between them. This is important because the drug binding to a protein stimulates the physiological response that characterizes the action of the drug, which means that a series of biochemical events promote a biological or pharmacological effect [68]. When the ACA molecule is in contact with the active site of NtMGAM, the coupling study showed thirteen amino acids involved in the molecular interactions, where only four of them are connected in the protein sequence (Asp443-Met444 and Phe575-Ala576). With high hydrophilic character are aspartic acid (Asp203, Asp327, and Asp542), threonine (Thr205 and Thr544), tyrosine (Tyr299), Arg526, and histidine (His600), and with hydrophobic character is tryptophan (Trp539). While for the MAY ligand, the active site of the NtMGAM is formed by the following residues: Arg202, Thr204-Thr205, Tyr299, Asp327, Lys480, and Asp542 presented a hydrophilic character, and the residue Trp406 registered a hydrophobic character. Once the NtMGAM interacts with the LUT ligand, the active site is formed by the following residues: Ile364, Trp406, and Phe575 (hydrophobic), Tyr299, Asp443, Arg526, and Gln603 (hydrophilic). The amino acids identified in the interaction site for ACA ligand with the NtMGAM, coincide with some of the amino acids of the active site obtained by X-ray diffraction reported by [PERSON], et al. [69] (See Table 1). These amino acids are indicated in bold). In these couplings, the amino acid Asp203 is present, which is of great importance for the binding of the ligands in the protein. The schematic structure of the active site and the binding energies are shown in Figure 4.  
In addition, an analysis of the formation of hydrogen bonds between the active site of the NtMGAM and the ligands were carried out. In the case of the ACA, four hydrogen bonds were formed with Asp203, Asp443, and His600. In the interaction between MAY and NtMGAM, two hydrogen bonds were observed with the Asp327 and Thr205. Finally, the LUT ligand generated two hydrogen bonds with the residue Asp443, and a \(\pi\)-\(\pi\) interaction with the Tyr605 was obtained (Figure 5). In general, all the ligands are fully compliant with the Lipinski rule [70; 71], which states that if five or fewer hydrogen bonds are present, the ligands could have good absorption and permeability.