In silico analysis and antihypertensive effect of ACE-inhibitory peptides from smooth-hound viscera protein hydrolysate: Enzyme-peptide interaction study using molecular docking simulation

Smooth-hound viscera proteins were enzymatically hydrolyzed, using Esperase®, and the resulting hydrolysate was fractionated by ultrafiltration through four membranes with decreasing molecular weight (MW) cut-offs. Five fractions were obtained, FI (>50 kDa), FII (5–50 kDa), FIII (3–5 kDa), FIV (1–3 kDa) and FV (<1 kDa). Their RP-HPLC peptide profile, amino acid compositions, and ACE-inhibitory activity were investigated and compared to the non-fractionated hydrolysate. Data showed that fractions with low MW peptides contained the highest amounts of hydrophobic amino acids (39.63 and 41.68% in FIV and FV, respectively). In addition, FIV and FV exhibited the strongest ACE-inhibitory activity with respective IC50 of 101.61 and 92.75 μg/ml. Moreover, they showed interesting blood pressure-lowering results in hypertensive rats after 4 h of oral administration (200 mg/kg body weight). Both fractions were then fractionated by RP-HPLC and eluted peptides were analyzed by nanoLC–MS/MS. The molecular docking study of IAGPPGSAGPAG, VVPFEGAV, PLPKRE, and PTVPKRPSPT showed that peptides were able to bind ACE through a complex of hydrophobic, hydrogen bonds, van der Waals and electrostatic interactions, as well as to interact with the three residues coordinating with Zn2+. Hence, this study provides a useful bioprocess for the use of smooth-hound byproducts as a natural source of hypotensive agents.

Bibliographic Details

Main Authors:	Abdelhedi, Ola, Nasri, Rim, Jridi, Mourad, Mora, Leticia, Oseguera-Toledo, Miguel Eduardo, Aristoy, María Concepción, Amara, Ibtissen Ben, Toldrá Vilardell, Fidel, Nasri, Moncef
Other Authors:	Generalitat Valenciana
Format:	artículo biblioteca
Language:	English
Published:	Elsevier 2017-04-28
Subjects:	Smooth-hound viscera, Ultra-filtration process, ACE-inhibitory, Peptides, Molecular docking,
Online Access:	http://hdl.handle.net/10261/155318 http://dx.doi.org/10.13039/501100003359 http://dx.doi.org/10.13039/501100003339
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