Table 1.
Screening of top eight selected peptides using Peptide Ranker and ToxinPred tools.
Table 2.
Binding scores (in kcal/mol) and Z-scores (in parenthesis) of top eight hypoglycemic peptides with selected receptor proteins.
Fig 1.
Protein-peptide interactions between P6 and pancreatic α-amylase.
(a) Receptor protein is represented in green with red interacting residues, and peptide P6 is shown in magenta with interacting residues. (b) Residual interactions between P6 and protein complex; hydrogen bonds are represented in blue, salt bridges are shown by red colored lines. Other amino acids representative properties are shown by different colors (i.e., aliphatic: grey, positive: blue, negative: red, Cys: yellow, aromatic: pink, Pro and Gly: orange, and neutral: green).
Fig 2.
Protein-peptide interactions between P6 and insulin-like growth factor 1 receptor.
(a) Receptor protein is represented in green with interacting residues in magenta. The peptide P6 is shown in red with its interacting residues in yellow. (b) Residual interactions between P6 and protein complex; hydrogen bonds are represented in blue, salt bridges are shown by red colored lines. Other amino acids representative properties are shown by different color (i.e., aliphatic: grey, positive: blue, negative: red, Cys: yellow, aromatic: pink, Pro and Gly: orange, and neutral: green).
Fig 3.
Protein-peptide interactions between P6 and aldose reductase.
(a) Receptor protein is represented in green with cyan interacting residues. The peptide P6 is shown in red with its interacting residues in magenta. (b) Residual interactions between P6 and protein complex. Hydrogen bonds are represented in blue, salt bridges are shown by red colored lines. Other amino acids representative properties are shown by different colors (i.e., aliphatic: grey, positive: blue, negative: red, Cys: yellow, aromatic: pink, Pro and Gly: orange, and neutral: green).
Fig 4.
Protein-peptide interactions between P6 and dipeptidyl peptidases-4.
(a) Receptor protein is represented in green with cyan interacting residues. The peptide P6 is shown in red with its interacting residues in magenta. (b) Residual interactions between P6 and protein complex. Hydrogen bonds are represented in blue, salt bridges are shown by red colored lines. Other amino acids representative properties are shown by different colors (i.e., aliphatic: grey, positive: blue, negative: red, Cys: yellow, aromatic: pink, Pro and Gly: orange, and neutral: green).
Fig 5.
Protein-peptide interactions between P6 and glucokinase.
(a) Receptor protein is represented in green with magenta interacting residues. The peptide P6 is shown in red with its interacting residues. (b) Residual interactions between P6 and protein complex. Hydrogen bonds are represented in blue, salt bridges are shown by red colored lines. Other amino acids representative properties are shown by different colors (i.e., aliphatic: grey, positive: blue, negative: red, Cys: yellow, aromatic: pink, Pro and Gly: orange, and neutral: green).
Fig 6.
Protein-peptide interactions between P6 and Jun N-terminal kinase1.
(a) Receptor protein is represented in green with magenta interacting residues. The peptide P6 is shown in red with its interacting residues. (b) Residual interactions between P6 and protein complex. Hydrogen bonds are represented in blue, salt bridges are shown by red colored lines. Other amino acids representative properties are shown by different colors (i.e., aliphatic: grey, positive: blue, negative: red, Cys: yellow, aromatic: pink, Pro and Gly: orange, and neutral: green).
Fig 7.
Protein-peptide interactions between P5 and Jun N-terminal kinase1.
(a) Receptor protein is represented in green with cyan interacting residues. The peptide P5 is shown in magenta with its interacting residues. (b) Residual interactions between P5 and protein complex. Hydrogen bonds are represented in green color.
Fig 8.
Protein-peptide interactions between P2 and maltase-glucoamylase.
(a) Receptor protein is represented in green with cyan interacting residues. Peptide P2 is shown in red with its interacting residues in magenta. (b) Residual interactions between P2 and receptor complex in which hydrogen bond are represented as green dotted lines.
Fig 9.
Protein-peptide interactions between P6 and PPAR-γ.
(a) Receptor protein is represented in green with its interacting residues. The peptide P6 is shown in red with its interacting residues in magenta. (b) Residual interactions between P6 and PPAR-γ complex. Hydrogen bonds are represented in blue, salt bridges are shown by red colored lines. Other amino acids representative properties are shown by different colors (i.e., aliphatic: grey, positive: blue, negative: red, Cys: yellow, aromatic: pink, Pro and Gly: orange, and neutral: green).
Fig 10.
Protein-peptide interactions between P2 and adiponectin.
(a) Receptor protein is represented in green with cyan interacting residues. The peptide P2 is shown in red with its interacting residues in magenta. (b) Hydrogen bond residual interactions between P2 and adiponectin complex are represented as green dotted lines.
Fig 11.
Protein-peptide interactions between P2 and GLUT1.
(a) Receptor protein is represented in green with cyan interacting residues. The peptide P2 is shown in red with its interacting residues in magenta. (b) Hydrogen bond residual interactions between P2 and GLUT1 complex are represented as green dotted lines.
Fig 12.
MD simulation showing RMSD trajectories.
The MD simulation of the docked complex of (a) P6- insulin-like growth factor 1 receptor and (b) P2- maltase-glucoamylase.
Fig 13.
Histograms of protein-peptide contact.
(a) Insulin-like growth factor 1 receptor complexed with P6; (b) maltase-glucoamylase complexed with P2.
Fig 14.
Molecular Mechanics Generalized Born Surface Area (MM-GBSA) calculated before and after the simulation.
IGF1: Insulin-like growth factor 1 receptor; MGA: maltase-glucoamylase.