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Characterization of ACE Inhibitory Peptides from Mactra veneriformis Hydrolysate by Nano-Liquid Chromatography Electrospray Ionization Mass Spectrometry (Nano-LC-ESI-MS) and Molecular Docking

by Rui Liu 1,2,3,4,†, Yunhan Zhu 1,†, Jiao Chen 5, Hao Wu 1,2,3,4,*, Lei Shi 1,2,3,4, Xinzhi Wang 1,2,3,4 and Lingchong Wang 1,2,3,4
1
Jiangsu Key Laboratory of Research and Development in Marine Bio-resource Pharmaceutics, Nanjing University of Chinese Medicine, Nanjing, Jiangsu 210023, China
2
National and Local Collaborative Engineering Center of Chinese Medicinal Resources Industrialization and Formulae Innovative Medicine, Nanjing University of Chinese Medicine, Nanjing, Jiangsu 210023, China
3
Jiangsu Collaborative Innovation Center of Chinese Medicinal Resources Industrialization, Nanjing University of Chinese Medicine, Nanjing, Jiangsu 210023, China
4
College of Pharmacy, Nanjing University of Chinese Medicine, Nanjing, Jiangsu 210023, China
5
China Pharmaceutical University, Nanjing, Jiangsu 210009, China
*
Author to whom correspondence should be addressed.
These authors contributed equally to this work.
Mar. Drugs 2014, 12(7), 3917-3928; https://doi.org/10.3390/md12073917
Received: 27 February 2014 / Revised: 12 May 2014 / Accepted: 15 May 2014 / Published: 30 June 2014
Food-derived bioactive compounds are gaining increasing significance in life sciences. In the present study, we identified angiotensin I-converting enzyme (ACE)-inhibitory peptides from Mactra veneriformis hydrolysate using a nano-LC-MS/MS method. Mactra veneriformis hydrolysate was first separated into four fractions (F1–F4) based on molecular weight by ultrafiltration. The fraction with molecular weight lower than 1 kDa (F1) showed the highest ACE inhibitory activity. F1 was then analyzed by a high throughput nano-LC-MS/MS method and sequences of peptides in F1 were calculated accordingly. The 27 peptides identified as above were chemically synthesized and tested for ACE-inhibitory activity. The hexapeptide VVCVPW showed the highest potency with an IC50 value of 4.07 μM. We then investigated the interaction mechanism between the six most potent peptides and ACE by molecular docking. Our docking results suggested that the ACE inhibitory peptides bind to ACE via interactions with His383, His387, and Glu411 residues. Particularly, similar to the thiol group of captopril, the cysteine thiol group of the most potent peptide VVCVPW may play a key role in the binding of this peptide to the ACE active site. View Full-Text
Keywords: ACE inhibitory peptide; characterization; nano-LC-MS/MS; molecular docking; Mactra veneriformis ACE inhibitory peptide; characterization; nano-LC-MS/MS; molecular docking; Mactra veneriformis
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Liu, R.; Zhu, Y.; Chen, J.; Wu, H.; Shi, L.; Wang, X.; Wang, L. Characterization of ACE Inhibitory Peptides from Mactra veneriformis Hydrolysate by Nano-Liquid Chromatography Electrospray Ionization Mass Spectrometry (Nano-LC-ESI-MS) and Molecular Docking. Mar. Drugs 2014, 12, 3917-3928.

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