The possible tole of food-derived bioactive peptides in reducing the risk of cardiovascular disease

Department of Pharmaceutics, College of Pharmacy, University of Minnesota, Minneapolis, MN 55455, USA.
The Journal of Nutritional Biochemistry (Impact Factor: 3.79). 06/2008; 19(10):643-54. DOI: 10.1016/j.jnutbio.2007.11.010
Source: PubMed


Vascular diseases such as atherosclerosis, stroke or myocardial infarction are a significant public health problem worldwide. Attempts to prevent vascular diseases often imply modifications and improvement of causative risk factors such as high blood pressure, obesity, an unfavorable profile of blood lipids or insulin resistance. In addition to numerous preventive and therapeutic drug regimens, there has been increased focus on identifying dietary compounds that may contribute to cardiovascular health in recent years. Food-derived bioactive peptides represent one such source of health-enhancing components. They can be released during gastrointestinal digestion or food processing from a multitude of plant and animal proteins, especially milk, soy or fish proteins. Biologically active peptides are considered to promote diverse activities, including opiate-like, mineral binding, immunomodulatory, antimicrobial, antioxidant, antithrombotic, hypocholesterolemic and antihypertensive actions. By modulating and improving physiological functions, bioactive peptides may provide new therapeutic applications for the prevention or treatment of chronic diseases. As components of functional foods or nutraceuticals with certain health claims, bioactive peptides are of commercial interest as well. The current review centers on bioactive peptides with properties relevant to cardiovascular health.

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Available from: Kati Erdmann, Jan 28, 2015
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    • "Functional food derived from bioactive peptides is one of the healthy and beneficial food sources, such as bovine or goat milk, and various meat, fish or plants. Those foods have provided neonates and adults with important physiological mechanism[8]. This peptide was suggested as immunomodulatory and antiinflammatory agents[9]. "
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    ABSTRACT: Objective: To observe the protective effect of goat milk alpha (S2)-casein (CSN1S2) protein on ileum microstructure and inflammation in rat-complete Freund's adjuvant-induced rheumatoid arthritis model. Methods: Twenty four male Wistar rats were divided into six groups of two models. The body weight, food intake and albumin level of all subjects were calculated. The ileum microstructures were analyzed by scanning electron microscopy. Histopathological analysis was observed by hematoxylin-eosin staining and the level expressions of immunoglobulin E, secretory immunoglobulin A, interleukin-17, interleukin-10, Ki-67 and caspase-9 were measured by using western blotting. Results: CSN1S2 protein of milk or yogurt could repair the ileum villi of rat arthritis group similar to the normal. The level expressions showed the immunoglobulin E, secretory immunoglobulin A, interleukin-17 and caspase-9 decreased in milk CSN1S2 protein and yogurt CSN1S2 protein rat groups. The level expression of interleukin-10 was increased, and also Ki-67 was significantly increased in milk CSN1S2 protein and yogurt CSN1S2 protein rat groups. CSN1S2 protein of milk and yogurt could increase the body weight and albumin significantly, meanwhile food intake increased but not significantly. Conclusions: CSN1S2 protein of goat milk and yogurt could repair the ileum microstructure, suppress inflammatory process and also increase the body weight, food intake and albumin level. This result indicates that goat CSN1S2 protein may protect the ileum disorder in rheumatoid arthritis disease.
    Asian Pacific Journal of Tropical Disease 07/2015; 5(7). DOI:10.1016/S2222-1808(15)60837-4
    • "A wide range of antioxidant peptides have already been isolated from fish processing products and by-products such as yellowfin sole skin gelatin hydrolysate, yellowfin sole frame protein hydrolysate, Alaska pollack skin gelatin hydrolysate and Alaska pollack frame protein hydrolysate (Di Bernardini et al., 2011). The exact mechanism by which peptides display antioxidant activity was not totally elucidated, but it was reported that protein hydrolysates and peptides can act as radical scavengers as well as transition metal chelators and exert antioxidant activities against enzymatic (lipoxygenase-mediated) and non-enzymatic peroxidation of lipid and fats (Sarmadi and 449 Two fish protein hydrolysates Ismail, 2010; Erdmann et al., 2008). Furthermore, it has been suggested that these properties could be mediated by improvement of antioxidant enzymatic system like superoxide dismutase, catalase, glutathione peroxidase activities as well as non-enzymatic system like vitamin E, glutathione (You et al., 2011; Parthasarathy et al., 2000). "
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    ABSTRACT: Purpose – The purpose of this study was to evaluate the antioxidant and hypocholesterolemic activities of sardine and bogue protein hydrolysates in cholesterol-fed rats. Design/methodology/approach – In total, 18 male Wistar rats (220 ± 10 g) fed 20 per cent casein, 1 per cent cholesterol and 0.5 per cent cholic acid were divided into three groups and received a daily gavage of 250 mg of sardine (SPH) or bogue (BPH) protein hydrolysates for 30 days. The third group, named control group (CG), received in the same conditions water. Lipoproteins were fractionated by size-exclusion fast protein liquid chromatography, and serum lipids, apolipoproteins and lipoproteins were assayed. Findings – In SPH and BPH groups, serum total cholesterol concentrations were — 66 per cent lower than in CG. This corresponded to the decreased very low-density lipoprotein-C in the former groups. Moreover, BPH treatment reduced low-density lipoprotein-C compared with CG and SPH groups. Compared with CG, serum phospholipids were reduced by SPH and BPH. Furthermore, BPH increased significantly APOA4 and sphingomyelin but lowered phosphatidylcholine. In the latter group, serum lecithin cholesterol acyltransferase activity was +23 per cent higher, but with SPH, this activity was —35 per cent reduced compared with CG. Apolipoprotein A-I contents were similar in the three groups. Compared with CG, hydroperoxide and lipid peroxidation contents in serum and lipoprotein fractions were reduced by SPH and BPH. Compared with CG, serum superoxide dismutase and glutathione peroxidase activities were increased in the treated groups, particularly in the BPH group. Originality/value – These results suggest that sardine protein hydrolysates and particularly those of bogue could be a very useful natural compound to prevent hypercholesterolemia by both improving the lipid profle and modulating oxidative stress in cholesterol-fed rats.
    Nutrition & Food Science 05/2015; 45(3):448-466. DOI:10.1108/NFS-11-2014-0096
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    • "A relationship exists between food peptides and cholesterol metabolism. They can act on the key enzyme of cholesterol synthesis (3-hydroxy-3-methylglutaryl coenzyme A reductase–HMG-CoA reductase) and/or are capable of inhibiting the absorption of dietary cholesterol, inhibiting cholesterol transport proteins or disrupting the cholesterol micelles in the lumen (Dziuba, Iwaniak, & Minkiewicz, 2003; Erdmann, Cheung, & Schroder, 2008; Zhang et al., 2012). "
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    ABSTRACT: This study aimed to assess the hypocholesterolemic activity of peptides obtained by in vitro simulated human digestion of cowpea bean proteins; moreover, we have screened the bioactive peptides through chromatographic separation by RP-HPLC of the 3 kDa molecular mass cut-off fraction of hydrolyzed isolated cowpea protein. Micellar solubility of cholesterol was measured after adding 35 μg mL− 1 of each fraction on in vitro prepared intestine-like micelles. The inhibiting activity of each fraction (50 μg mL− 1) also was tested on the enzyme 3-hydroxy-3-methylglutaryl coenzyme A reductase (HMG-CoA reductase). The whole hydrolysate was analyzed by ‘de novo’ mass spectrometry peptide sequencing (RP-HPLC-MS2) and the top score candidate peptide sequences were further analyzed by computational modeling. All collected fractions inhibited the initial HMG-CoA reductase activity by 47.8 to 57.1%. They also reduced cholesterol micellar solubilization, with fraction 1 being the most effective (71.7%). The peptide conserved domains may interact with the phosphatidylcholine added in the reaction of the cholesterol micelles. According with a computational prediction, the only peptide able to bind significantly the HMG-CoA reductase was GCTLN. This is the first report of peptide fractions from cowpea bean protein released by human digestion enzymes (pepsin followed by pancreatin) assigned to its cholesterol-lowering effect. These routes may define their action in lipid metabolism.
    Food Research International 04/2015; DOI:10.1016/j.foodres.2015.04.020 · 2.82 Impact Factor
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