Title
Enzyme inhibition kinetics and molecular interactions of patatin peptides with angiotensin I-converting enzyme and renin
Author
Yu Fu, Adeola M. Alashi, Jette F. Young, Margrethe Therkildsen, Rotimi E. Aluko
Year
2017
Journal
International Journal of Biological Macromolecules Volume 101, August 2017, Pages 207-213
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
Instrument
FP-6300
Keywords
ACE, Renin, Patatin peptides, Kinetics, Molecular docking