LAPSE:2023.5311
Published Article
LAPSE:2023.5311
ACE Inhibitory Peptides from Bellamya bengalensis Protein Hydrolysates: In Vitro and In Silico Molecular Assessment
Tanmoy Kumar Dey, Roshni Chatterjee, Rahul Shubhra Mandal, Anadi Roychoudhury, Debjyoti Paul, Souvik Roy, Mirian Pateiro, Arun K. Das, Jose M. Lorenzo, Pubali Dhar
February 23, 2023
muscle meat is known for ethnopharmacological benefits. The present study focuses on the identification of ACE inhibitory peptides from the proteolytic digests of muscle protein of Bellamya bengalensis and its underlying mechanism. After ultrafiltration of 120 min alcalase hydrolysates (BBPHA120) to isolate the small peptide fraction (1 × 104 A.U.). These peptides were sequenced via de novo sequencing. Based on the apparent hydrophobicity (%), the IIAPTPVPAAH peptide was selected for further analysis. The sequence was commercially synthesized by solid-phase standard Fmoc chemistry (purity 95−99.9%; by HPLC). The synthetic peptide (IC50 value 8.52 ± 0.779 µg/mL) was used to understand the thermodynamics of the inhibition by checking the binding affinity of the peptide to ACE by isothermal titration calorimetry compared with lisinopril, and the results were further substantiated by in silico site-specific molecular docking analysis. The results demonstrate that this peptide sequence (IIAPTPVPAAH) can be used as a nutraceutical with potent ACE inhibition.
Keywords
alcalase, angiotensin-converting enzyme-inhibitory activity, cooperative ligand binding, gastropod snail, isothermal titration calorimetry, lisinopril, site-specific molecular docking, uncompetitive inhibition
Subject
Suggested Citation
Dey TK, Chatterjee R, Mandal RS, Roychoudhury A, Paul D, Roy S, Pateiro M, Das AK, Lorenzo JM, Dhar P. ACE Inhibitory Peptides from Bellamya bengalensis Protein Hydrolysates: In Vitro and In Silico Molecular Assessment. (2023). LAPSE:2023.5311
Author Affiliations
Dey TK: Laboratory of Food Science and Technology, Food and Nutrition Division, University of Calcutta, 20B, Judges Court Road, Alipore, Kolkata 700027, West Bengal, India; Center for Nanoscience and Nanotechnology, University of Calcutta, Kolkata 700073, West Be [ORCID]
Chatterjee R: Laboratory of Food Science and Technology, Food and Nutrition Division, University of Calcutta, 20B, Judges Court Road, Alipore, Kolkata 700027, West Bengal, India
Mandal RS: Biomedical Informatic Centre, National Institute of Cholera and Enteric Diseases, Scheme XM, P-33, CIT Road, Beliaghata, Kolkata 700010, West Bengal, India [ORCID]
Roychoudhury A: Department of Physiology, Serampur College (Autonomous), University of Calcutta, 8, William Carey Sarani, Maniktala, Serampore 712201, West Bengal, India
Paul D: Laboratory of Food Science and Technology, Food and Nutrition Division, University of Calcutta, 20B, Judges Court Road, Alipore, Kolkata 700027, West Bengal, India
Roy S: DBT-Interdisciplinary Programme of Life Sciences (DBT-IPLS), Modern Biology Wing, University of Calcutta, 35, Ballygunge Circular Road, Kolkata 700019, West Bengal, India
Pateiro M: Centro Tecnológico de la Carne de Galicia, Avd. Galicia nº 4, Parque Tecnológico de Galicia, 32900 San Cibrao das Viñas, Spain [ORCID]
Das AK: Eastern Regional Station, ICAR-Indian Veterinary Research Institute, 37 Belgachia Road, Kolkata 700037, West Bengal, India [ORCID]
Lorenzo JM: Centro Tecnológico de la Carne de Galicia, Avd. Galicia nº 4, Parque Tecnológico de Galicia, 32900 San Cibrao das Viñas, Spain; Área de Tecnología de los Alimentos, Facultad de Ciencias de Ourense, Universidad de Vigo, 32004 Ourense, Spain [ORCID]
Dhar P: Laboratory of Food Science and Technology, Food and Nutrition Division, University of Calcutta, 20B, Judges Court Road, Alipore, Kolkata 700027, West Bengal, India; Center for Nanoscience and Nanotechnology, University of Calcutta, Kolkata 700073, West Be
Journal Name
Processes
Volume
9
Issue
8
First Page
1316
Year
2021
Publication Date
2021-07-29
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ISSN
2227-9717
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PII: pr9081316, Publication Type: Journal Article
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LAPSE:2023.5311
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doi:10.3390/pr9081316
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