title: Enzyme inhibition kinetics and molecular interactions of patatin peptides with angiotensin I-converting enzyme and renin.
abstract: In this work, the inhibitory effects of potato patatin-derived peptides Trp-Gly (WG) and Pro-Arg-Tyr (PRY) on angiotensin I-converting enzyme (ACE) and renin activities were investigated using kinetics, intrinsic fluorescence and molecular docking. The results indicated that PRY was a more potent ACE- and renin-inhibitory peptide than WG. Enzyme inhibition kinetics showed that WG and PRY inhibited ACE activity through mixed-type and competitive modes, respectively. The inhibitory mechanism of WG and PRY towards renin was determined to be mixed-type. PRY exhibited stronger affinity towards ACE and renin molecules, when compared to WG as determined by intrinsic fluorescence intensity. Molecular docking data confirmed that the higher inhibitory potency of PRY might be attributed to formation of more hydrogen bonds with the enzyme's active site or non-active sites that distorted the configuration necessary for catalysis.
authors.affiliation: Department of Food Science, Aarhus University, Blichers Allé 20, 8830, Tjele, Denmark.
authors.forename: Yu
authors.initials: Y
authors.lastname: Fu
authors.affiliation: Department of Human Nutritional Sciences, University of Manitoba, Winnipeg, MB, R3T 2N2, Canada.
authors.forename: Adeola M
authors.initials: AM
authors.lastname: Alashi
authors.affiliation: Department of Food Science, Aarhus University, Blichers Allé 20, 8830, Tjele, Denmark.
authors.forename: Jette F
authors.initials: JF
authors.lastname: Young
authors.affiliation: Department of Food Science, Aarhus University, Blichers Allé 20, 8830, Tjele, Denmark.
authors.forename: Margrethe
authors.initials: M
authors.lastname: Therkildsen
authors.affiliation: Department of Human Nutritional Sciences, University of Manitoba, Winnipeg, MB, R3T 2N2, Canada. Electronic address: rotimi.aluko@umanitoba.ca.
authors.forename: Rotimi E
authors.initials: RE
authors.lastname: Aluko
mesh_terms: D000806:Angiotensin-Converting Enzyme Inhibitors / Q000378:metabolism* / Q000494:pharmacology*; D002265:Carboxylic Ester Hydrolases / Q000737:chemistry*; D020134:Catalytic Domain; D006801:Humans; D007700:Kinetics; D062105:Molecular Docking Simulation; D010446:Peptide Fragments / Q000378:metabolism / Q000494:pharmacology*; D007703:Peptidyl-Dipeptidase A / Q000737:chemistry / Q000378:metabolism*; D010940:Plant Proteins / Q000737:chemistry*; D012083:Renin / Q000737:chemistry / Q000378:metabolism*; D000092502:Renin Inhibitors
chemical_list: D000806:Angiotensin-Converting Enzyme Inhibitors; D002265:Carboxylic Ester Hydrolases; D010446:Peptide Fragments; D007703:Peptidyl-Dipeptidase A; D010940:Plant Proteins; D012083:Renin; D000092502:Renin Inhibitors; C043222:patatin protein, Solanum tuberosum
keywords: ACE; Kinetics; Molecular docking; Patatin peptides; Renin