English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/155318
logo share SHARE logo core CORE   Add this article to your Mendeley library MendeleyBASE

Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE
Exportar a otros formatos:


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

AuthorsAbdelhedi, Ola; Nasri, Rim; Jridi, Mourad; Mora, Leticia CSIC ORCID; Oseguera-Toledo, Miguel Eduardo; Aristoy, María Concepción CSIC ORCID; Amara, Ibtissen Ben; Toldrá Vilardell, Fidel CSIC ORCID; Nasri, Moncef
KeywordsSmooth-hound viscera
Ultra-filtration process
Molecular docking
Issue Date28-Apr-2017
CitationProcess Biochemistry 58: 145-159 (2017)
AbstractSmooth-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.
Publisher version (URL)https://doi.org/10.1016/j.procbio.2017.04.032
Appears in Collections:(IATA) Artículos
Files in This Item:
File Description SizeFormat 
Process Biochem_2017_ 58_145-159.pdfArtículo principal2,02 MBAdobe PDFThumbnail
Show full item record
Review this work

Related articles:

WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.