Identification, structure-activity relationship and in silico molecular docking analyses of five novel angiotensin I-converting enzyme (ACE)-inhibitory peptides from stone fish (Actinopyga lecanora) hydrolysates

Shehu Muhammad Auwal; Najib Zainal Abidin; Mohammad Zarei; Chin Ping Tan; Nazamid Saari

doi:10.1371/journal.pone.0197644

Identification, structure-activity relationship and in silico molecular docking analyses of five novel angiotensin I-converting enzyme (ACE)-inhibitory peptides from stone fish (Actinopyga lecanora) hydrolysates

PLoS One. 2019 May 30;14(5):e0197644. doi: 10.1371/journal.pone.0197644. eCollection 2019.

Authors

Shehu Muhammad Auwal^{1

2}, Najib Zainal Abidin¹, Mohammad Zarei³, Chin Ping Tan⁴, Nazamid Saari¹

Affiliations

¹ Department of Food Science, Faculty of Food Science and Technology, Universiti Putra Malaysia, Serdang, Selangor, Malaysia.
² Department of Biochemistry, Faculty of Basic Medical Sciences, Bayero University, Kano, Nigeria.
³ Department of Food Science and Technology, School of Industrial Technology, Faculty of Applied Sciences, Universiti Teknologi MARA, Shah Alam, Selangor, Malaysia.
⁴ Department of Food Technology, Faculty of Food Science and Technology, Universiti Putra Malaysia, Serdang, Selangor, Malaysia.

Abstract

Stone fish is an under-utilized sea cucumber with many health benefits. Hydrolysates with strong ACE-inhibitory effects were generated from stone fish protein under the optimum conditions of hydrolysis using bromelain and fractionated based on hydrophobicity and isoelectric properties of the constituent peptides. Five novel peptide sequences with molecular weight (mw) < 1000 daltons (Da) were identified using LC-MS/MS. The peptides including Ala-Leu-Gly-Pro-Gln-Phe-Tyr (794.44 Da), Lys-Val-Pro-Pro-Lys-Ala (638.88 Da), Leu-Ala-Pro-Pro-Thr-Met (628.85 Da), Glu-Val-Leu-Ile-Gln (600.77 Da) and Glu-His-Pro-Val-Leu (593.74 Da) were evaluated for ACE-inhibitory activity and showed IC50 values of 0.012 mM, 0.980 mM, 1.310 mM, 1.440 mM and 1.680 mM, respectively. The ACE-inhibitory effects of the peptides were further verified using molecular docking study. The docking results demonstrated that the peptides exhibit their effect mainly via hydrogen and electrostatic bond interactions with ACE. These findings provide evidence about stone fish as a valuable source of raw materials for the manufacture of antihypertensive peptides that can be incorporated to enhance therapeutic relevance and commercial significance of formulated functional foods.

Publication types

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

MeSH terms

Amino Acid Sequence
Angiotensin-Converting Enzyme Inhibitors / chemistry*
Angiotensin-Converting Enzyme Inhibitors / pharmacology*
Animals
Chromatography, Liquid
Fishes* / metabolism
Hydrophobic and Hydrophilic Interactions
Molecular Docking Simulation*
Molecular Dynamics Simulation*
Molecular Structure
Peptides / chemistry*
Peptides / pharmacology*
Protein Conformation
Protein Hydrolysates / chemistry*
Protein Hydrolysates / pharmacology*
Structure-Activity Relationship
Tandem Mass Spectrometry

Substances

Angiotensin-Converting Enzyme Inhibitors
Peptides
Protein Hydrolysates

Grants and funding

This work was supported by Grant No. 02-01-04-SF 2309; https://ernd.mosti.gov.my. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.