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
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 consti...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
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Public Library of Science
2019
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| Online Access: | http://psasir.upm.edu.my/id/eprint/80141/ http://psasir.upm.edu.my/id/eprint/80141/1/Identification%2C%20structure-activity%20relationship%20and%20in%20silico%20molecular%20docking%20analyses%20of%20five%20novel%20angiotensin%20I-converting%20enzyme%20%28ACE%29inhibitory%20peptides%20from%20stone%20fish%20%28Actinopyga%20lecanora%29%20hydrolysates.pdf |
| _version_ | 1848858839953178624 |
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| author | Auwal, Shehu Muhammad Zainal Abidin, Najib Saari, Nazamid Zarei, Mohammad Tan, Chin Ping Saari, Nazamid |
| author_facet | Auwal, Shehu Muhammad Zainal Abidin, Najib Saari, Nazamid Zarei, Mohammad Tan, Chin Ping Saari, Nazamid |
| author_sort | Auwal, Shehu Muhammad |
| building | UPM Institutional Repository |
| collection | Online Access |
| description | 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. |
| first_indexed | 2025-11-15T12:19:50Z |
| format | Article |
| id | upm-80141 |
| institution | Universiti Putra Malaysia |
| institution_category | Local University |
| language | English |
| last_indexed | 2025-11-15T12:19:50Z |
| publishDate | 2019 |
| publisher | Public Library of Science |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | upm-801412020-09-30T02:31:10Z http://psasir.upm.edu.my/id/eprint/80141/ 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 Auwal, Shehu Muhammad Zainal Abidin, Najib Saari, Nazamid Zarei, Mohammad Tan, Chin Ping Saari, Nazamid 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. Public Library of Science 2019 Article PeerReviewed text en http://psasir.upm.edu.my/id/eprint/80141/1/Identification%2C%20structure-activity%20relationship%20and%20in%20silico%20molecular%20docking%20analyses%20of%20five%20novel%20angiotensin%20I-converting%20enzyme%20%28ACE%29inhibitory%20peptides%20from%20stone%20fish%20%28Actinopyga%20lecanora%29%20hydrolysates.pdf Auwal, Shehu Muhammad and Zainal Abidin, Najib and Saari, Nazamid and Zarei, Mohammad and Tan, Chin Ping and Saari, Nazamid (2019) 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, 14 (5). pp. 1-18. ISSN 1932-6203 10.1371/journal.pone.0197644 |
| spellingShingle | Auwal, Shehu Muhammad Zainal Abidin, Najib Saari, Nazamid Zarei, Mohammad Tan, Chin Ping Saari, Nazamid 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 |
| title | 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 |
| title_full | 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 |
| title_fullStr | 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 |
| title_full_unstemmed | 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 |
| title_short | 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 |
| title_sort | 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 |
| url | http://psasir.upm.edu.my/id/eprint/80141/ http://psasir.upm.edu.my/id/eprint/80141/ http://psasir.upm.edu.my/id/eprint/80141/1/Identification%2C%20structure-activity%20relationship%20and%20in%20silico%20molecular%20docking%20analyses%20of%20five%20novel%20angiotensin%20I-converting%20enzyme%20%28ACE%29inhibitory%20peptides%20from%20stone%20fish%20%28Actinopyga%20lecanora%29%20hydrolysates.pdf |