The development of bioactive peptides from dietary proteins as a dipeptidyl peptidase IV inhibitor for the management of type 2 diabetes

[1] Kahn CR. Banting lecture. Insulin action, diabetogenes, and the cause of type II diabetes. Diabetes 1994; 43: 1066–84. [2] Robertson RP. Antagonist: diabetes and insulin resistance-philosophy, science, and the multiplier hypothesis. J Lab Clin Med 1995; 125: 560–4. [3] Mohammadi S, Hosseinzadeh-Attar MJ, Hosseinnezhad A, Hosseini SH, Eshraghian MR, Nezhad MK, et al. Compare the effects of different visfatin concentration on cardiovascular risk factors, adi- ponectin and insulin resistance in patients with T2DM. Diabetes Metab Syndr Clin Res Rev 2011; 5: 71–5. [4] Global burden of diabetes. International Diabetes Federation. Diabetes atlas sixth edition update 2014. Available at http://www.idf.org/diabetesatlas/update-2014. [5] Ben-Avraham S, Harman-Boehm I, Schwarzfuchs D, Shai I. Dietary strategies for patients in the era of multi-approaches; review and results from the Dietary Intervention Randomized Controlled Trial (DIRECT). Diabetes Res Clin Pract 2009; 86: S41–8. [6] Cunningham DF, O'Connor B. Proline specific peptidase. Biochim Biophys Acta 1997; 1343: 160–86. [7] Darmoul D, Voisin T, Couvineau A, Rouyer-Fessard C, Salomon R, Wang YX, et al. Regional expression of epithelial dipeptidyl pep- tidase IV in the human intestines. Biochem Biophys Res Commun 1994;203:1224–29. [8] Lambeir AM, Durinx C, Proost P, Van Damme J, Scharpe S, De Meester I. Kinetic study of the processing by dipeptidyl-peptidase IV/CD26 of neuropeptides involved in pancreatic insulin secretion. FEBS Lett 2001; 507: 327–30. [9] Drucker DJ. The biology of incretin hormones. Cell Metab 2006; 3: 153–65. [10] Ahren B. GLP-1 and extra-islet effects. Horm Metab Res 2004; 36: 842–45. [11] De León DD, Crutchlow MF, Ham JYN, Stoffers AS. Role of glucagon-like peptide-1 in the pathogenesis and treatment of diabetes mellitus. Int J Biochem Cell Biol 2006; 38: 845–59. [12] Hansotia T, Drucker DJ. GIP and GLP-1 as incretin hormones: lessons from single and double incretin receptor knockout mice. Regul Pept 2005; 128: 125–34. [13] Vilsboll T, Holst JJ. Incretins, insulin secretion and type 2 diabetes. Diabetologia 2004; 47: 357–66. [14] Nauck MA, Homberger E, Siegel EG, Allen RC, Eaton P, Ebert R, et al. Incretin effects of increasing glucose loads in man calculated from venous insulin and C-protein responses. J Clin Endocrinol Metab 1986; 63: 492–8. [15] Nauck MA, Heimesaat MM, Orskov C, Holst JJ, Ebert R, Creutzfeldt W. Preserved incretin activity of glucagon-like peptide 1 [7-36 amide] but not of synthetic human GIP in patients with type 2 diabetes. J Clin Invest 1993; 91: 301–7. [16] Mentlein R, Gallwitz B, Schmidt WE. Dipeptidyl-peptidase IV hydrolysates gastric inhibitory polypeptide, glucagon-like peptide-1 (7-36) amide, and peptide histidine methionine and is responsible for their degradation in human serum. Eur J Biochem 1993; 214: 82935. [17] Drucker DJ. Dipeptidyl peptidase-4 inhibition and the treatment of type 2 diabetes. Diabetes Care 2007; 30: 1335–43. [18] Deacon CF, Holst JJ. Dipeptidyl peptidase IV inhibitors: a promising new therapeutic approach for the management of type 2 diabetes. Int J Biochem Cell B 2006; 38: 831–44. [19] Villhauer EB, Brinkman JA, Naderi GB, Burkey BF, Dunning BE, Prasad K, et al. 1-[[(3-Hydroxy-1-adamantyl)amino]acetyl]-2- cyano-(5r)-pyrrolidine: a potent, selective, and orally bioavailable dipeptidyl peptidase IV inhibitor with antihyperglycemic properties. J Med Chem 2003; 46: 2774–89. [20] Krushner P, Gorrell M. DPP-4 inhibitors in type 2 diabetes: importance of selective enzyme inhibition and implications for clinical use. J Fam Pract 2010; 59: 2. [21] Scheen A. Gliptins (dipeptidyl peptidase-4 inhibitors) and risk of acute pancreatitis. Expert Opin Drug Saf 2013; 12: 545–57. [22] Kamau SM, Lu RR, Chen W, Liu XM, Tian FW, Shen Y, et al. Functional significance of bioactive peptides derived from milk proteins. Food Rev Int 2010; 26: 386–401. [23] Shahidi F, Zhong Y. Bioactive peptides. J AOAC Int 2008; 91: 91431. [24] Lacroix IME, Li-Chan ECY. Isolation and characterization of pep- tides with dipeptidyl peptidase-IV inhibitory activity from pepsin- treated bovine whey proteins. Peptides 2014; 54: 39–48. [25] Nongonierma AB, FitzGerald RJ. Susceptibility of milk protein- derived peptides to dipeptidyl peptidase IV (DPP-IV) hydrolysis. Food Chem 2014; 145: 845–52. [26] Hatanaka T, Inoue Y, Arima J, Kumagai Y, Usuki H, Kawakami K, et al. Production of dipeptidyl peptidase IV inhibitory peptides from defatted rice bran. Food Chem 2012; 134: 797–802. [27] Velarde-Salcedo AJ, Barrera-Pacheco A, Lara-Gonzalez de Mejia E, Barba de la Rosa A. In vitro inhibition of dipeptidyl peptidase IV by peptides derived from the hydrolysis of amaranth (Amaranthus hypochondriacus L.) proteins. Food Chem 2013; 136: 758–64. [28] Huang SL, Jao CL, Ho KP, Hsu KC. Dipeptidyl-peptidase IV inhibitory activity of peptides from tuna cooking juice hydrolysates. Peptides 2012; 35: 114–21. [29] Li-Chan ECY, Huang SL, Jao CL, Ho KP, Hsu KC. Peptides derived from Atlantic salmon skin gelatin as dipeptidyl-peptidase IV inhibitors. J Agr Food Chem 2012; 60: 973–78. [30] Manders RJF, Wagenmakers AJM, Koopman R, Zorenc AHG, Men- heere PPCA, Schaper NC, et al. Co-ingestion of a protein hydro- lysate and amino acid mixture with carbohydrate improves plasma glucose disposal in patients with type 2 diabetes. Am J Clin Nutr 2005; 82: 76–83. [31] Uenishi H, Kabuki T, Seto Y, Serizawa A, Nakajima H. Isolation and identification of casein-derived dipeptidyl-pepdiase-4 (DPP-4)- inhibitory peptide LPQNIPPL from gouda-type cheese and its effect on plasma glucose in rats. Int Dairy J 2012; 22: 24–30. [32] Huang SL, Hung CC, Jao CL, Tung YS, Hsu KC. Porcine skin gelatin hydrolysate as a dipeptidyl peptidase IV inhibitor improves glycemic control in streptozotocin-induced diabetic rats. J Funct Foods 2014; 11: 235–42. [33] Aart VA, Catharina MJ, Zeeland-Wolbers V, Maria LA, Gilst V, Hendrikus W, et al. Egg protein hydrolysates. 2009; Patent WO 2009/128713 2009. [34] Pieter BJW. Protein hydrolysate enriched in peptides inhibiting DPP-IV and their use. 2006; Patent WO 2006/068480 2006. [35] Cheung IWY, Nakayama S, Hsu MNK, Samaranayaka AGP, Li-Chan ECY. Angiotensin-I converting enzyme inhibitory activity of hy- drolysates from oat (Avena sativa) proteins by in silico and in vitro analyses. J Agr Food Chem 2009; 57: 9234–42. [36] Minkiewicz P, Dziuba J, Michalska J. Bovine meat proteins as potential precursors of biologically active peptides-a computational study based on the BIOPEP database. Food Sci Tech Int 2011; 17: 39–45. [37] Lacroix IME, Li-Chan ECY. Evaluation of the potential of dietary proteins as precursors of dipeptidyl peptidase (DPP)-IV inhibitors by an in silico approach. J Funct Foods 2012; 4: 403–22. [38] Nongonierma AB, FitzGerald RJ. An in silico model to predict the potential of dietary proteins as sources of dipeptidyl peptidase IV (DPP-IV) inhibitory peptides. Food Chem 2014; 165: 489–98. [39] Meisel H. Biochemical properties of regulatory peptides derived from milk proteins. Biopolymers 1997; 43: 119–28. [40] Uchida M, Ohshiba Y, Mogami O. Novel dipeptidyl peptidase-4- inhibiting peptide derived from ß-lactoglobulin. J Pharmacol Sci 2011; 117: 63–6. [41] Tulipano G, Sibilia V, Caroli AM, Cocchi D. Whey proteins as source of dipeptidyl dipeptidase IV (dipeptidyl peptidase-4) inhibitors. Peptides 2011; 835–8. [42] Gallego M, Aristoy MC, Toldra F. Dipeptidyl peptidase IV inhibitory peptides generated in Spanish dry-cured ham. Meat Sci 2014; 96: 757–61. [43] Umezawa H, Aoyagi T, Ogawa K, Naganawa H, Hamada M, Takeuchi T. Diprotins A and B, inhibitors of dipeptidyl aminopepti- dase IV, produced by bacteria. J Antibiot 1984; 37: 422–425. [44] Nongonierma AB, FitzGerald RJ. Inhibition of dipeptidyl peptidase IV (DPP-IV) by tryptophan containing dipeptides. Food Funct 2013; 4: 1843–9. [45] Silveira ST, Martinez-Maqueda D, Recio I, Hernandez-Ledesma B. Dipeptidyl peptidase-IV inhibitory peptides generated by tryptic hydrolysis of a whey protein concentration rich in ß-lactoglobulin. Food Chem 2013; 141: 1072–7. [46] Nongoneirma AB, FitzGerald RJ. Dipeptidyl peptidase IV inhibitory and antioxidative properties of milk protein-derived dipeptides and hydrolysates. Peptides 2013; 39: 157–63. [47] Hira T, Mochida T, Miyachita K, Hara H. GLP-1 secretin is enhanced directly in the ileum but indirectly in the duodenum by a newly identified potent stimulator, zein hydrolysate, in rats. Am J Physiol Gastrointest Liver Physiol 2009; 297: G663–71. [48] Mochida T, Hira T, Hara H. The corn protein, zein hydrolysate, administered into ileum attenuates hyperglycemia via its dual action on glucagon-like peptide-1 secretion and dipeptidyl peptidase-IV activity in rats. Endocrinology 2010; 151: 3095–104. [49] Power O, Hallihan A, Jakeman P. Human insulinotropic response to oral ingestion of native and hydrolysed whey protein. Amino Acids 2009; 37: 333–9. [50] Arihara K. Strategies for designing novel functional meat products. Meat Sci 2006; 74: 219–29. [51] Dziuba J, Minkiewicz P, Nalşcz D, Iwaniak A. Database of biologically active peptide sequences. Nahrung 1999; 43: 190–95. [52] Lafarga T, O'Connor P, Hayes M. Identification of novel dipeptidyl peptidase-IV and angiotensin-I-converting enzyme inhibitory pep- tides from meat proteins using in silico analysis. Peptides 2014; 59: 53–62. [53] Nongonierma AB, Mooney C, Shields DC, FitzGerald RJ. In silico approaches to predict the potential of milk protein-derived peptides as dipeptidyl peptidase IV (DPP-IV) inhibitors. Peptides 2014; 57: 43–51. [54] Dziuba J, Iwaniak A, Minkiewicz P. Computer-aided characteristics of proteins as potential precursors of bioactive peptides. Polimery 2003; 48: 50–3.