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We present capillary electrophoresis-mass spectrometry (CE-MS) in combination with advanced chemometric tools for the analysis of bioactive compounds in food, in particular for the identification of antihypertensive peptides in a nutraceutical derived from a bovine milk protein hydrolysate. Different extracts of the nutraceutical were analyzed by CE-MS, and the electropherograms were processed using a novel data analysis workflow that included regions of interest (ROIs) compression and multivariate curve resolution alternating least squares (MCR-ALS). MCR-ALS permitted the description of the nutraceutical extract as ten characteristic components with their electrophoretic profiles and mass spectra. Twenty-two compounds were tentatively identified as antihypertensive bovine casein fragments through a mass search in a database of bioactive peptides. The identity of 17 antihypertensive peptides was reliably confirmed by capillary electrophoresis-tandem mass spectrometry. The proposed analytical approach demonstrated the potential to obtain a characteristic and activity-related fingerprint for quality control and authentication of the antihypertensive nutraceutical.
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http://dx.doi.org/10.1016/j.chroma.2018.10.018 | DOI Listing |
PLoS One
September 2025
Department of Biostatistics, Faculty of Medicine, Malatya Turgut Özal University, Malatya, Turkey.
Polycystic ovary syndrome (PCOS) is a multifactorial endocrine disorder associated with vascular dysfunction and increased cardiovascular risk. This study aims to investigate the dysregulation of vascular tone in PCOS, focusing on the imbalance between vasodilators (nitric oxide [NO] and apelin) and vasoconstrictors (noradrenaline and reduced prostacyclin). By examining these factors, the study seeks to elucidate their contribution to endothelial dysfunction and cardiovascular complications in PCOS patients.
View Article and Find Full Text PDFFood Chem
August 2025
College of Food Science and Engineering, Ocean University of China, Qingdao 266404, China. Electronic address:
Food-derived angiotensin-converting enzyme (ACE)-inhibitory peptide plays key roles in hypertension prevention, however, their activity is dependent on specific sequence composition. This study aims to enhance peptide activity using a module substitution strategy. Molecular docking and activity assays identified MF as a low- and FP as a high-contribution dipeptide module within MFPWP.
View Article and Find Full Text PDFFood Chem
September 2025
Institute of Food and Drug Research for One Health, Ludong University, Yantai, People's Republic of China; School of Food Engineering, Ludong University, Yantai, People's Republic of China. Electronic address:
Food-derived bioactive peptides exhibit therapeutic potentials in hypertension management in recent years. This review firstly synthesizes findings from a total of 62 relevant studies concerning the potentials of both plant- and animal-derived peptides. Secondly, the molecular targets and acting mechanisms underlying the antihypertensive effects of food-derived peptides are discussed.
View Article and Find Full Text PDFJ Agric Food Chem
September 2025
Department of Agricultural, Food and Nutritional Sciences, 4-10 Ag/For Building, University of Alberta, Edmonton, Alberta T6G 2P5, Canada.
IRW, an antihypertensive peptide derived from ovotransferrin, has been shown to lower blood pressure in spontaneously hypertensive rats (SHRs) by upregulating angiotensin-converting enzyme 2 (ACE2). ACE2 is cardioprotective and a well-documented inhibitor of apoptosis. This study aims to investigate the anti-apoptotic effects of IRW and its underlying mechanism in SHRs' vasculature.
View Article and Find Full Text PDFPrev Nutr Food Sci
August 2025
Department of Pharmaceutical Biology, School of Pharmacy, Bandung Institute of Technology, West Java 40132, Indonesia.
Peptides produced from soybean tempeh that inhibit angiotensin-converting enzyme (ACE) provide a promising source of novel antihypertensive agents. This study utilized two cysteine proteases (papain and bromelain) to generate ACE inhibitory peptides from the protein hydrolysate of soybean tempeh. The trials were arranged using a Box-Behnken design to achieve optimal hydrolysis conditions.
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