Angiotensin Converting Enzyme (ACE)-Peptide Interactions: Inhibition Kinetics, In Silico Molecular Docking and Stability Study of Three Novel Peptides Generated from Palm Kernel Cake Proteins

Mohammad Zarei; Najib Bin Zainal Abidin; Shehu Muhammad Auwal; Shyan Yea Chay; Zaibunnisa Abdul Haiyee; Adi Md Sikin; Nazamid Saari

doi:10.3390/biom9100569

Angiotensin Converting Enzyme (ACE)-Peptide Interactions: Inhibition Kinetics, In Silico Molecular Docking and Stability Study of Three Novel Peptides Generated from Palm Kernel Cake Proteins

Biomolecules. 2019 Oct 4;9(10):569. doi: 10.3390/biom9100569.

Authors

Mohammad Zarei¹, Najib Bin Zainal Abidin², Shehu Muhammad Auwal³, Shyan Yea Chay², Zaibunnisa Abdul Haiyee⁴, Adi Md Sikin⁴, Nazamid Saari⁵

Affiliations

¹ Department of Food Science and Technology, School of Industrial Technology, Faculty of Applied Sciences, Universiti Teknologi MARA, Shah Alam 40450, Selangor, Malaysia. mzarei.mail@gmail.com.
² Department of Food Science, Faculty of Food Science and Technology, Universiti Putra Malaysia, Serdang 43400, Selangor, Malaysia.
³ Department of Biochemistry, Faculty of Basic Medical Sciences, Bayero University, Kano 700231, Nigeria.
⁴ Department of Food Science and Technology, School of Industrial Technology, Faculty of Applied Sciences, Universiti Teknologi MARA, Shah Alam 40450, Selangor, Malaysia.
⁵ Department of Food Science, Faculty of Food Science and Technology, Universiti Putra Malaysia, Serdang 43400, Selangor, Malaysia. nazamid@upm.edu.my.

Abstract

Three novel peptide sequences identified from palm kernel cake (PKC) generated protein hydrolysate including YLLLK, WAFS and GVQEGAGHYALL were used for stability study against angiotensin-converting enzyme (ACE), ACE-inhibition kinetics and molecular docking studies. Results showed that the peptides were degraded at different cleavage degrees of 94%, 67% and 97% for YLLLK, WAFS and GVQEGAGHYALL, respectively, after 3 h of incubation with ACE. YLLLK was found to be the least stable (decreased ACE-inhibitory activity) compared to WAFS and GVQEGAGHYALL (increased ACE-inhibitory activity). YLLLK showed the lowest K_i (1.51 mM) in inhibition kinetics study when compared to WAFS and GVQEGAGHYALL with K_i of 2 mM and 3.18 mM, respectively. In addition, ACE revealed the lowest Kmapp and Vmaxapp and higher catalytic efficiency (CE) in the presence of YLLLK at different concentrations, implying that the enzyme catalysis decreased and hence the inhibition mode increased. Furthermore, YLLLK showed the lowest docking score of -8.224 and seven interactions with tACE, while peptide GVQEGAGHYALL showed the higher docking score of -7.006 and five interactions with tACE.

Keywords: angiotensin converting enzyme inhibitory activity; kinetics; molecular docking; peptide.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Animals
Catalysis
Catalytic Domain / drug effects
Gene Expression Regulation / drug effects
Humans
Hydrolysis
Kinetics
Models, Molecular
Molecular Docking Simulation
Palm Oil / metabolism*
Peptide Fragments / chemistry
Peptide Fragments / pharmacology*
Peptidyl-Dipeptidase A / chemistry*
Peptidyl-Dipeptidase A / metabolism*
Plant Proteins / chemistry*

Substances

Peptide Fragments
Plant Proteins
Palm Oil
ACE protein, human
Peptidyl-Dipeptidase A