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  1. 41
    Three-dimensional cartoon and surface representations of the evolution of 300 ns of simulation. Configurations generated by molecular dynamics of the most stable complexes from molecular docking between α-amylase (PDB ID 5VA9) and the peptides (a) DTVHDTDGQVLP, (b) ILPAQQGK, (c) TVSQTPIDIPIGLPVR, (d) TIAPACAPKPAR and (e) DEQSSEK. Letters: D—Aspartic acid, E—Glutamic acid, R—Arginine, K—Lysine, N—Asparagine, H—Histidine, Q—Glutamine, S—Serine, T—Threonine, A—Alanine, G—Glycine, V—Valine, P—Proline, L—Leucine, I—Isoleucine, W—Tryptophan, C—Cysteine. The peptides are derived from the cleavage of TTIp 56/287: model number 56 and conformation number 287 of trypsin inhibitor purified from tamarind seeds.

    Three-dimensional cartoon and surface representations of the evolution of 300 ns of simulation. Configurations generated by molecular dynamics of the most stable complexes from mol... Autor Larissa Aida Lemos de Souza (22331667)

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  2. 42
    In vitro anti-α-amylase activity of TTI compared to acarbose. The anti-α-amylase activity was verified using 30 µL of TTI, using starch as substrate. TTI: trypsin inhibitor isolated from tamarind seeds. <sup>abc</sup>Different lowercase letters indicate a statistical difference between the means (p < 0.05). <sup>ABC</sup>Similar uppercase letters indicate no statistical difference between the means (p > 0.05).

    In vitro anti-α-amylase activity of TTI compared to acarbose. The anti-α-amylase activity was verified using 30 µL of TTI, using starch as substrate. TTI: trypsin inhibitor isolate... Autor Larissa Aida Lemos de Souza (22331667)

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  3. 43
    Supporting information.

    Supporting information. Autor Larissa Aida Lemos de Souza (22331667)

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  4. 44
    Potential Interaction Energy for the peptide-α-amylase complexes for the last 50 ns of molecular dynamics simulation.

    Potential Interaction Energy for the peptide-α-amylase complexes for the last 50 ns of molecular dynamics simulation. Autor Larissa Aida Lemos de Souza (22331667)

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  5. 45
    RMSF and B-factor profiles of peptides-α-amylase complexes (a) DTVHDTDGQVPL, (b) ILPAQQGK, (c) TVSQTPIDIPIGLPVR, (d)TIAPACAPKPAR and (e) DEQSSEK. Each panel shows the RMSF plot, where the peaks represent the fluctuations of each residue throughout the simulation, highlighting the peptide (P), and a surface representation of the B-factor highlighting the rotated structure of the enzyme (on the right) and the peptide in shades of green at the interaction site (P, on the left). The peptides are highlighted in green, and α-amylase in gray with red. Letters: D—Aspartic acid, E—Glutamic acid, R—Arginine, K—Lysine, N—Asparagine, H—Histidine, Q—Glutamine, S—Serine, T—Threonine, A—Alanine, G—Glycine, V—Valine, P—Proline, L—Leucine, I—Isoleucine, W—Tryptophan, C—Cysteine. The peptides are derived from the cleavage of TTIp 56/287: model number 56 and conformation number 287 of tryps

    RMSF and B-factor profiles of peptides-α-amylase complexes (a) DTVHDTDGQVPL, (b) ILPAQQGK, (c) TVSQTPIDIPIGLPVR, (d)TIAPACAPKPAR and (e) DEQSSEK. Each panel shows the RMSF plot, wh... Autor Larissa Aida Lemos de Souza (22331667)

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  6. 46
    Parameters obtained from the HADDOCK Web Server in molecular docking for ten different docking orientations for the TTIp 56/287 – α-amylase complex.

    Parameters obtained from the HADDOCK Web Server in molecular docking for ten different docking orientations for the TTIp 56/287 – α-amylase complex. Autor Larissa Aida Lemos de Souza (22331667)

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  7. 47
    Three-dimensional stick model representation of the TVSQTPIDIPIGLPVR-α-amylase complex. Peptide illustrated in green and enzyme residues in red: (a) the interaction site highlighting key regions that promote complex stabilization and (b) electrostatic and van der Waals interactions between peptide-enzyme residue pairs, including conventional hydrogen bonding interactions between GLN04-TRP059, GLN04-ASP353, ILE11-GLY308, and ARG16-TRP284; hydrogen-carbon bonding interactions between GLN04-HIS305, GLN04-ASP352, and ARG16-LYS261; and alkyl-type interactions between LEU13-LYS257, LEU13-ALA260, VAL15-LYS257, and VAL15-LYS261. Letters: D—Aspartic acid, E—Glutamic acid, R—Arginine, K—Lysine, N—Asparagine, H—Histidine, Q—Glutamine, S—Serine, T—Threonine, A—Alanine, G—Glycine, V—Valine, P—Proline, L—Leucine, I—Isoleucine, W—Tryptophan, C—Cysteine. The peptides are derived from the clea

    Three-dimensional stick model representation of the TVSQTPIDIPIGLPVR-α-amylase complex. Peptide illustrated in green and enzyme residues in red: (a) the interaction site highlighti... Autor Larissa Aida Lemos de Souza (22331667)

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  8. 48
    Molecular structures in the molecular surface representation of the TTIp 56/287 (green) – α-amylase (gray and red) complexes. The structures were obtained from molecular docking with orientational docking of the numbered sequences, with the first two sequences exhibiting the highest HS highlighted in red. (a) DTVHDTDGQV, (b) PLNNAGQYYI, (c) LPAQQGKGGG, (d) LGLSNDDDGN, (e) PIDIPIGLPVRSF, (f) TTALSLNIEFTI, (g) EKGYTVPKLSDDF, (h) SSAPFKLKQFEEDYKLVYCSK, (i) SESGERKCVDLG and (j) KKVDEESSEEWSIV. TTIp 56/287: model number 56 and conformation number 287 of the trypsin inhibitor purified from tamarind seeds. Letters: D—Aspartic acid, E—Glutamic acid, R—Arginine, K—Lysine, N—Asparagine, H—Histidine, Q—Glutamine, S—Serine, T—Threonine, A—Alanine, G—Glycine, V—Valine, P—Proline, L—Leucine, I—Isoleucine, W—Tryptophan, C—Cysteine. TTIp 56/287: model number 56 and conformation number 2

    Molecular structures in the molecular surface representation of the TTIp 56/287 (green) – α-amylase (gray and red) complexes. The structures were obtained from molecular docking wi... Autor Larissa Aida Lemos de Souza (22331667)

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  9. 49
    Three-dimensional stick model representation of the TIAPACAPKPAR-α-amylase complex. Peptide illustrated in green and enzyme residues in red: (a) the interaction site highlighting key regions that promote complex stabilization and (b) electrostatic and van der Waals interactions between peptide-enzyme residue pairs, including conventional hydrogen bonding interactions between PRO10-LYS200, ILE02-GLN063, and ARG12-ASP300; amide-pi stacking between ILE02-TRP059; pi-alkyl bonds between PRO10-TYR15, ALA03-TRP059, PRO04-TRP058, and PRO04-059; and salt bridge interactions between ARG12-ASP300 and ARG12-ASP356. Letters: D—Aspartic acid, E—Glutamic acid, R—Arginine, K—Lysine, N—Asparagine, H—Histidine, Q—Glutamine, S—Serine, T—Threonine, A—Alanine, G—Glycine, V—Valine, P—Proline, L—Leucine, I—Isoleucine, W—Tryptophan, C—Cysteine. The peptides are derived from the cleavage of TTIp 56/28

    Three-dimensional stick model representation of the TIAPACAPKPAR-α-amylase complex. Peptide illustrated in green and enzyme residues in red: (a) the interaction site highlighting k... Autor Larissa Aida Lemos de Souza (22331667)

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  10. 50
    Chromatographic profile of F2 and molecular mass estimation of TTI. 35 mg of F2 were applied to Trypsin-Sepharose CNBr 4B affinity chromatography. a) The column was previously equilibrated with 50 mM Tris-HCl buffer, pH 7.5, and elution of unretained material (before the arrow) was performed with the same buffer. Proteins adsorbed on the matrix (starting from the arrow) were eluted with HCl (5 mM), and aliquots of F2 (5 mL) were monitored at 280 nm. The antitryptic activity of the protein peak was verified using 100 µL of TTI, using BapNA as substrate. b) Discontinuous and denaturing polyacrylamide gel (SDS-PAGE) at 12% stained with Comassie Blue. M: marker; CE: crude extract; F2: fraction 2 (precipitate 2 with ammonium sulfate in 30-60%). TTI: trypsin inhibitor isolated from tamarind seeds. The arrow represents the addition of HCl.

    Chromatographic profile of F2 and molecular mass estimation of TTI. 35 mg of F2 were applied to Trypsin-Sepharose CNBr 4B affinity chromatography. a) The column was previously equi... Autor Larissa Aida Lemos de Souza (22331667)

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  11. 51
    Computational prediction of bioactive potential, cell penetration capacity, half-life in the simulated intestinal environment, and peptide stability.

    Computational prediction of bioactive potential, cell penetration capacity, half-life in the simulated intestinal environment, and peptide stability. Autor Larissa Aida Lemos de Souza (22331667)

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  12. 52
    Three-dimensional stick model representation of the DTVHDTDGQVPL-α-amylase complex. Peptide illustrated in green and enzyme residues in red: (a) the interaction site highlighting key regions that promote complex stabilization and (b) electrostatic interactions between peptide-enzyme residue pairs, including charge-charge interactions (salt bridges) between ASP01-GLU149, ASP05-LYS200 and ASP07-LYS200; conventional hydrogen bonds between HIS04-HIS201, GLN09-GLN063 and LEU12-SER108; and hydrogen-carbon bond between ASP01-GLU149. Letters: D—Aspartic acid, E—Glutamic acid, R—Arginine, K—Lysine, N—Asparagine, H—Histidine, Q—Glutamine, S—Serine, T—Threonine, A—Alanine, G—Glycine, V—Valine, P—Proline, L—Leucine, I—Isoleucine, W—Tryptophan, C—Cysteine. The peptides are derived from the cleavage of TTIp 56/287: model number 56 and conformation number 287 of trypsin inhibitor purified fr

    Three-dimensional stick model representation of the DTVHDTDGQVPL-α-amylase complex. Peptide illustrated in green and enzyme residues in red: (a) the interaction site highlighting k... Autor Larissa Aida Lemos de Souza (22331667)

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  13. 53
    Primary data obtained from the scoring process after molecular docking for each peptide-α-amylase complex.

    Primary data obtained from the scoring process after molecular docking for each peptide-α-amylase complex. Autor Larissa Aida Lemos de Souza (22331667)

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  14. 54
    Examining the Impact of Side-Chain Chirality on Conformation of a Helical Poly(3‑(<i>S</i>‑1-ethylhexyl)esterfuran)

    Examining the Impact of Side-Chain Chirality on Conformation of a Helical Poly(3‑(<i>S</i>‑1-ethylhexyl)esterfuran) Autor Dhruv Sharma (10219121)

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  15. 55
    Molecular models at two viewing angles of TTIp 56/287 for molecular docking study with α-amylase (PDB ID 5VA9). The numbers indicate the amino acid sequences used in docking: 1 (DTVHDTDGQV), 2 (PLNNAGQYYI), 3 (LPAQQGKGGG), 4 (LGLSNDDDGN), 5 (PIDIPIGLPVRSF), 6 (TTALSLNIEFTI), 7 (EKGYTVPKLSDDF), 8 (SSAPFKLKQFEEDYKLVYCSK), 9 (SESGERKCVDLG) and 10 (KKVDEESSEEWSIV). TTIp 56/287: model number 56 and conformation number 287 of the purified tamarind seed trypsin inhibitor.

    Molecular models at two viewing angles of TTIp 56/287 for molecular docking study with α-amylase (PDB ID 5VA9). The numbers indicate the amino acid sequences used in docking: 1 (DT... Autor Larissa Aida Lemos de Souza (22331667)

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  16. 56
    Root mean square deviation (RMSD) over 300 ns of molecular dynamics simulations of the peptides-α-amylase complexes. Different colors identify peptides, the x-axis represents the simulation time (ns), and the y-axis indicates the RMSD value (nm). Letters: D—Aspartic acid, E—Glutamic acid, R—Arginine, K—Lysine, N—Asparagine, H—Histidine, Q—Glutamine, S—Serine, T—Threonine, A—Alanine, G—Glycine, V—Valine, P—Proline, L—Leucine, I—Isoleucine, W—Tryptophan, C—Cysteine. The peptides are derived from the cleavage of TTIp 56/287: model number 56 and conformation number 287 of trypsin inhibitor purified from tamarind seeds.

    Root mean square deviation (RMSD) over 300 ns of molecular dynamics simulations of the peptides-α-amylase complexes. Different colors identify peptides, the x-axis represents the s... Autor Larissa Aida Lemos de Souza (22331667)

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  17. 57
    Historical Data Mining Deep Dive into Machine Learning-Aided 2D Materials Research in Electrochemical Applications

    Historical Data Mining Deep Dive into Machine Learning-Aided 2D Materials Research in Electrochemical Applications Autor Krittapong Deshsorn (16812784)

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