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Activity prediction and molecular mechanism of bovine blood derived angiotensin I-converting enzyme inhibitory peptides.

Zhang T, Nie S, Liu B, Yu Y, Zhang Y, Liu J - PLoS ONE (2015)

Bottom Line: To accelerate the progress of peptide identification, a three layer back propagation neural network model was established to predict the ACE-inhibitory activity of pentapeptides derived from bovine hemoglobin by simulated enzyme digestion.The pentapeptide WTQRF has the best predicted value with experimental IC50 23.93 μM.The potential molecular mechanism of the WTQRF / ACE interaction was investigated by flexible docking.

View Article: PubMed Central - PubMed

Affiliation: Laboratory of Nutrition and Functional Food, Jilin University, Changchun, Jilin, China.

ABSTRACT
Development of angiotensin I-converting enzyme (ACE, EC 3.4.15.1) inhibitory peptides from food protein is under extensive research as alternative for the prevention of hypertension. However, it is difficult to identify peptides released from food sources. To accelerate the progress of peptide identification, a three layer back propagation neural network model was established to predict the ACE-inhibitory activity of pentapeptides derived from bovine hemoglobin by simulated enzyme digestion. The pentapeptide WTQRF has the best predicted value with experimental IC50 23.93 μM. The potential molecular mechanism of the WTQRF / ACE interaction was investigated by flexible docking.

No MeSH data available.


Related in: MedlinePlus

WTQRF binding with the active site of ACE, the conformation extracted from docking result.
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pone.0119598.g004: WTQRF binding with the active site of ACE, the conformation extracted from docking result.

Mentions: Interactions between ACE and inhibitor are fundamental to ACE-inhibitory processes. In this work, docking is used to predict the preferred orientation of WTQRF to ACE when they bound to each other to form a stable complex. The free energy of binding represents the binding affinity between ACE and WTQRF. The molecular docking study of WTQRF presenting within the ACE catalytic site in the presence of the cofactor showed the best pose with potential binding energy:- 749.747 kj / mol. It is indicated that the ligand bind tightly to the receptor and the ACE-WTQRF complex is stable. As we know, ligand-protein affinities are influenced by non-covalent intermolecular interactions between the two molecules. The best pose of WTQRF was stabilized mainly by hydrophobic and hydrophilic interactions (Fig. 4), electrostatic interactions (Electrostatic energy:- 154.728 kj / mol; Van der Waals energy:- 898.743 kj / mol) and hydrogen bond (Table 5).


Activity prediction and molecular mechanism of bovine blood derived angiotensin I-converting enzyme inhibitory peptides.

Zhang T, Nie S, Liu B, Yu Y, Zhang Y, Liu J - PLoS ONE (2015)

WTQRF binding with the active site of ACE, the conformation extracted from docking result.
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4358945&req=5

pone.0119598.g004: WTQRF binding with the active site of ACE, the conformation extracted from docking result.
Mentions: Interactions between ACE and inhibitor are fundamental to ACE-inhibitory processes. In this work, docking is used to predict the preferred orientation of WTQRF to ACE when they bound to each other to form a stable complex. The free energy of binding represents the binding affinity between ACE and WTQRF. The molecular docking study of WTQRF presenting within the ACE catalytic site in the presence of the cofactor showed the best pose with potential binding energy:- 749.747 kj / mol. It is indicated that the ligand bind tightly to the receptor and the ACE-WTQRF complex is stable. As we know, ligand-protein affinities are influenced by non-covalent intermolecular interactions between the two molecules. The best pose of WTQRF was stabilized mainly by hydrophobic and hydrophilic interactions (Fig. 4), electrostatic interactions (Electrostatic energy:- 154.728 kj / mol; Van der Waals energy:- 898.743 kj / mol) and hydrogen bond (Table 5).

Bottom Line: To accelerate the progress of peptide identification, a three layer back propagation neural network model was established to predict the ACE-inhibitory activity of pentapeptides derived from bovine hemoglobin by simulated enzyme digestion.The pentapeptide WTQRF has the best predicted value with experimental IC50 23.93 μM.The potential molecular mechanism of the WTQRF / ACE interaction was investigated by flexible docking.

View Article: PubMed Central - PubMed

Affiliation: Laboratory of Nutrition and Functional Food, Jilin University, Changchun, Jilin, China.

ABSTRACT
Development of angiotensin I-converting enzyme (ACE, EC 3.4.15.1) inhibitory peptides from food protein is under extensive research as alternative for the prevention of hypertension. However, it is difficult to identify peptides released from food sources. To accelerate the progress of peptide identification, a three layer back propagation neural network model was established to predict the ACE-inhibitory activity of pentapeptides derived from bovine hemoglobin by simulated enzyme digestion. The pentapeptide WTQRF has the best predicted value with experimental IC50 23.93 μM. The potential molecular mechanism of the WTQRF / ACE interaction was investigated by flexible docking.

No MeSH data available.


Related in: MedlinePlus