Activity Prediction and Molecular Mechanism of Bovine Blood Derived Angiotensin I-Converting Enzyme Inhibitory Peptides

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 ident...

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Detalles Bibliográficos
Autores principales: Zhang, Ting, Nie, Shaoping, Liu, Boqun, Yu, Yiding, Zhang, Yan, Liu, Jingbo
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2015
Materias:
Research Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4358945/
https://www.ncbi.nlm.nih.gov/pubmed/25768442
http://dx.doi.org/10.1371/journal.pone.0119598
Descripción
Sumario: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 IC(50) 23.93 μM. The potential molecular mechanism of the WTQRF / ACE interaction was investigated by flexible docking.

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