참고문헌
- Adessi C, Soto C. Converting a peptide into a drug: Strategies to improve stability and bioavailability. Curr. Med. Chem. 9: 963-978 (2002) https://doi.org/10.2174/0929867024606731
- Akhavan T, Luhovyy BL, Brown PH, Cho CE, Anderson GH. Effect of premeal consumption of whey protein and its hydrolysate on food intake and postmeal glycemia and insulin responses in young adults. Am. J. Clin. Nutr. 91: 966-975 (2010) https://doi.org/10.3945/ajcn.2009.28406
- Appuhamy JA, Knoebel NA, Nayananjalie WA, Escobar J, Hanigan MD. Isoleucine and leucine independently regulate mTOR signaling and protein synthesis in MAC-T cells and bovine mammary tissue slices. J. Nutr. 142: 484-491 (2012) https://doi.org/10.3945/jn.111.152595
- Boirie Y, Dangin M, Gachon P, Vasson MP, Maubois JL, Beaufrere B. Slow and fast dietary proteins differently modulate postprandial protein accretion. Proc. Natl. Acad. Sci. USA 94: 14930-14935 (1997) https://doi.org/10.1073/pnas.94.26.14930
- Brubaker PL, Drucker DJ. Minireview: glucagon-like peptides regulate cell proliferation and apoptosis in the pancreas, gut, and central nervous system. Endocrinology 145: 2653-2659 (2004) https://doi.org/10.1210/en.2004-0015
- Calbet JA, Holst JJ. Gastric emptying, gastric secretion and enterogastrone response after administration of milk proteins or their peptide hydrolysates in humans. Eur. J. Nutr. 43: 127-139 (2004) https://doi.org/10.1007/s00394-004-0448-4
- Cho YM, Fujita Y, Kieffer TJ. Glucagon-like peptide-1: glucose homeostasis and beyond. Annu. Rev. Physiol. 76: 535-559 (2014) https://doi.org/10.1146/annurev-physiol-021113-170315
- Daniel H. Molecular and integrative physiology of intestinal peptide transport. Annu. Rev. Physiol. 66: 361-384 (2004) https://doi.org/10.1146/annurev.physiol.66.032102.144149
- DeFronzo RA, Ferrannini E. Insulin resistance: a multifaceted syndrome responsible for NIDDM, obesity, hypertension, dyslipidemia, and atherosclerotic cardiovascular disease. Diabetes Care 14: 173-194 (1991)
- Drucker DJ, Nauck MA. The incretin system: glucagon-like peptide-1 receptor agonists and dipeptidyl peptidase-4 inhibitors in type 2 diabetes. Lancet 368:1696-1705 (2006) https://doi.org/10.1016/S0140-6736(06)69705-5
- Dullius A, Goettert MI, de Souza CFV. Whey protein hydrolysates as a source of bioactive peptides for functional foods-Biotechnological facilitation of industrial scale-up. J. Func. Foods 42: 58-74 (2018) https://doi.org/10.1016/j.jff.2017.12.063
-
Fernandez A, Riera F.
${\beta}$ -Lactoglobulin tryptic digestion: A model approach for peptide release. Biochem. Eng. J. 70: 88-96 (2013) https://doi.org/10.1016/j.bej.2012.10.001 - FitzGerald RJ, Meisel H. Milk protein-derived peptide inhibitors of angiotensin-I-converting enzyme. Br. J. Nutr. 84: 33-37 (2000) https://doi.org/10.1017/S0007114500002221
- Frid AH, Nilsson M, Holst JJ, Bjorck IM. Effect of whey on blood glucose and insulin responses to composite breakfast and lunch meals in type 2 diabetic subjects. Am. J. Clin. Nutr. 82: 69-75 (2005) https://doi.org/10.1093/ajcn/82.1.69
- Gilbert ER, Wong EA, Webb Jr. KE. Peptide absorption and utilization: Implications for animal nutrition and health. J. Anim. Sci. 86: 2135-2155 (2008) https://doi.org/10.2527/jas.2007-0826
- Gooben K, Graber S. Longer term safety of dipeptidyl peptidase-4 inhibitors in patients with type 2 diabetes mellitus: systematic review and meta-analysis. Diabetes Obes. Metab. 14: 1061-1072 (2012) https://doi.org/10.1111/j.1463-1326.2012.01610.x
- Guo HY, Pang K, Zhang XY, Zhao L, Chen SW, Dong ML, Ren FZ. Composition, physicochemical properties, nitrogen fraction distribution, and amino acid profile of donkey milk. J Dairy Sci. 90: 1635-1643 (2007) https://doi.org/10.3168/jds.2006-600
- Halton TL, Hu FB. The effects of high protein diets on thermogenesis, satiety and weight loss: a critical review. J. Am. Coll. Nutr. 23: 373-85 (2004) https://doi.org/10.1080/07315724.2004.10719381
- Hruby VJ, Balse PM. Conformational and topographical considerations in designing agonist peptidomimetics from peptide leads. Curr. Med. Chem. 7: 945-970 (2000) https://doi.org/10.2174/0929867003374499
- Hsieh CH, Wang TY, Hung CC, Jao CL, Hsieh YL, Wu SX, Hsu KC. In silico, in vitro and in vivo analyses of dipeptidyl peptidase IV inhibitory activity and the antidiabetic effect of sodium caseinate hydrolysate. Food Func. 7: 1122-1128 (2016) https://doi.org/10.1039/C5FO01324K
- Hunziker D, Hennig M, Peters JU. Inhibitors of dipeptidyl peptidase IV - recent advances and structural views. Curr. Topics Med. Chem. 5: 1623-1637 (2005) https://doi.org/10.2174/156802605775009685
- Lacroix IME, Li-Chan ECY. Dipeptidyl peptidase-IV inhibitory activity of dairy protein hydrolysates. Int. Dairy J. 25: 97-102 (2012) https://doi.org/10.1016/j.idairyj.2012.01.003
- Lara-Villoslada F, Olivares M, Xaus J. The balance between caseins and whey proteins in cow's milk determines its allergenicity. J. Dairy Sci. 88: 1654-1660 (2005) https://doi.org/10.3168/jds.S0022-0302(05)72837-X
- Layman DK, Evans EM, Erickson D, Seyler J, Weber J, Bagshaw D, Griel A, Psota T, Kris-Etherton P. A moderate protein diet produces sustained weight loss and long-term changes in body composition and blood lipids in obese adults. J. Nutr. 139: 514-521 (2009) https://doi.org/10.3945/jn.108.099440
- Layman DK, Walker DA. Potential importance of leucine in treatment of obesity and the metabolic syndrome. J. Nutr. 136: 319S-23S (2006) https://doi.org/10.1093/jn/136.1.319S
- Marya, Khan H, Nabavi SM, Habtemariam S. Anti-diabetic potential of peptides: future prospects as therapeutic agents. Life Sci. 193: 153-158 (2018) https://doi.org/10.1016/j.lfs.2017.10.025
- Mennella C, Visciano M, Napolitano A, Del Castillo MD, Fogliano V. Glycation of lysine-containing dipeptides. J. Pept. Sci.12: 291-296 (2006) https://doi.org/10.1002/psc.722
- Mentlein R. Therapeutic assessment of glucagons-like peptide-1 agonists compared with dipeptidyl peptidase IV inhibitors as potential antidiabetic drugs. Expert Opin. Invest. Drugs 14: 57-64 (2005) https://doi.org/10.1517/13543784.14.1.57
- Nielsen, SD, Beverly, RL, Qu Y, Dallas DC. Milk bioactive peptide database: A comprehensive database of milk protein-derived bioactive peptides and novel visualization. Food Chem. 232: 673-682 (2017) https://doi.org/10.1016/j.foodchem.2017.04.056
- Nilsson M, Holst JJ, Bjorck IM. Metabolic effects of amino acid mixtures and whey protein in healthy subjects: studies using glucose-equivalent drinks. Am. J. Clin. Nutr. 85: 996-1004 (2007) https://doi.org/10.1093/ajcn/85.4.996
- Nilsson M, Stenberg M, Frid AH, Holst JJ, Bjorck IM: Glycemia and insulinemia in healthy subjects after lactose-equivalent meals of milk and other food proteins: the role of plasma amino acids and incretins. Am. J. Clin. Nutr. 80: 1246-1253 (2004) https://doi.org/10.1093/ajcn/80.5.1246
- Nongonierma AB, FitzGerald RJ. The scientific evidence for the role of milk protein-derived bioactive peptides in humans: A review. J. Func. Foods 17: 640-656 (2015) https://doi.org/10.1016/j.jff.2015.06.021
- 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. 165: 489-498 (2014a) https://doi.org/10.1016/j.foodchem.2014.05.090
- Nongonierma AB, FitzGerald RJ. Susceptibility of milk protein-derived peptides to dipeptidyl peptidase IV (DPP-IV) hydrolysis. Food Chem. 145: 845-852 (2014b) https://doi.org/10.1016/j.foodchem.2013.08.097
- Nongonierma AB, FitzGerald RJ. Dipeptidyl peptidase IV inhibitory properties of a whey protein hydrolysate: Influence of fractionation, stability to simulated gastrointestinal digestion and food-drug interaction. Int. Dairy J. 32: 33-39 (2013b) https://doi.org/10.1016/j.idairyj.2013.03.005
- Ohnuma K, Takahashi N, Yamochi T, Hosono O, Dang NH, Morimoto C. Role of CD26/dipeptidyl peptidase IV in human T cell activation and function. Front Biosci. 13: 2299-2310 (2008) https://doi.org/10.2741/2844
- Pal S, Ellis V. The acute effects of four protein meals on insulin, glucose, appetite and energy intake in lean men. Br. J. Nutr. 104: 1241-1248 (2010) https://doi.org/10.1017/S0007114510001911
- Petersen BL, Ward LS, Bastian ED, Jenkins AL, Campbell J, Vuksan V. A whey protein supplement decreases post-prandial glycemia. Nutr. J. 8: 47 (2009) https://doi.org/10.1186/1475-2891-8-47
- Portha B, Tourrel-Cuzin C, Movassat J. Activation of the GLP-1 receptor signaling pathway: a relevant strategy to repair a deficient beta-cell mass. Exp. Diabetes Res. Article ID 376509 doi:10.1155/2011/376509 (2011)
- Pripp AH, Ardo Y. Modelling relationship between angiotensin-(I)-converting enzyme inhibition and the bitter taste of peptides. Food Chem. 102: 880-888 (2007) https://doi.org/10.1016/j.foodchem.2006.06.026
- Russell-Jones D, Gough S. Recent advances in incretin-based therapies. Clin. Endocrinol. 77: 489-499 (2012)
- Shaw JE, Sicree RA, Zimmet PZ. Global estimates of the prevalence of diabetes for 2010 and 2030. Diabetes Res. Clin. Pract. 87: 4-14 (2010) https://doi.org/10.1016/j.diabres.2009.10.007
- Thoma R, Loffler B, Stihle M, Huber W, Ruf A, Hennig M. Structure basis of proline-specific exopeptidase activity as observed in human dipeptidyl peptidase-IV. Structure, 11: 947-959 (2003)
- Toft-Nielsen MB, Damholt MB, Madsbad S, Hilsted LM, Hughes TE, Michelsen BK, Holst JJ. Determinants of the impaired secretion of glucagon-like peptide-1 in Type 2 diabetic patients. J. Clin. Endocrinol. Metab. 86: 3717-3723 (2001) https://doi.org/10.1210/jcem.86.8.7750
- Udenigwe CC, Fogliano V. Food matrix interaction and bioavailability of bioactive peptides: Two faces of the same coin? J. Func. Foods 35: 9-12 (2017) https://doi.org/10.1016/j.jff.2017.05.029
- Wada Y, Lonnerdal B. Effects of different industrial heating processes of milk on site-specific protein modifications and their relation to in vitro and in vivo digestibility. J. Agric. Food Chem. 62: 4175-4185 (2014). https://doi.org/10.1021/jf501617s
- Walzem RL, Dillard CJ, German JB. Whey components: Millennia of evolution create functionalities for mammalian nutrition: What we know and what we may be overlooking. Crit. Rev. Food Sci. Nutr. 42: 353-375 (2002) https://doi.org/10.1080/10408690290825574
- Wang JH, Liu YL, Ning JH, Yu NJ, Li XH, Wang FX. Is the structural diversity of tripeptides sufficient for developing functional food additives with satisfactory multiple bioactivities? J. Mol. Struc. 1040: 164-170 (2013) https://doi.org/10.1016/j.molstruc.2013.03.004
- Yang J, Chi Y, Burkhardt BR, Guan Y, Wolf BA. Leucine metabolism in regulation of insulin secretion from pancreatic beta cells. Nutr Rev. 68: 270-279 (2010) https://doi.org/10.1111/j.1753-4887.2010.00282.x
-
Zeng Z, Luo J, Zuo F, Zhang Y, Ma H, Chen S. Screening for potential novel probiotic Lactobacillus strains based on high dipeptidyl peptidase IV and
${\alpha}$ -glucosidase inhibitory activity. J. Func. Food 20: 486-495 (2016) https://doi.org/10.1016/j.jff.2015.11.030