[1] Iwaniak, A.; Darewicz, M.; Minkiewicz, P. Peptides derived from foods as supportive diet components in the prevention of metabolic syndrome. Compr. Rev. Food Sci. Food Saf. 2018, 17 (1), 63–81.
[2] Iwatani, S.; Yamamoto, N. Functional food products in Japan: A review. Food Sci. Hum. Wellness 2019, 8 (2), 96–101.
[3] Shimizu, M. History and current status of functional food regulations in Japan. In Nutraceutical and Functional Food Regulations in the United States and around the World. Third Edit.; Elsevier: Amsterdam, the Netherlands, 2019; 337-344.
[4] Foltz, M.; Van Der Pijl, P. C.; Duchateau, G. S. M. J. E. Current in vitro testing of bioactive peptides is not valuable. J. Nutr. 2010, 140 (1), 117–118.
[5] Turner, J. R. Intestinal mucosal barrier function in health and disease.Nat. Rev. Immunol. 2009, 9 (11), 799–809.
[6] Fei, Y.J.; Kanai, Y.; Nussberger, S.; Ganapathy, V.; Leibach, F. H.;Romero, M. F.; Singh, S. K.; Boron, W. F.; Hediger, M. A. Expression cloning of a mammalian proton-coupled oligopeptide transporter. Nature 1994, 368 (6471), 563–566.
[7] Fei, Y. J.; Sugawara, M.; Liu, J. C.; Li, H. W.; Ganapathy, V.; Ganapathy, M. E.; Leibach, F. H. cDNA structure, genomic organization, and promoter analysis of the mouse intestinal peptide transporter PEPT1. Biochim. Biophys. Acta - Gene Struct. Expr. 2000, 1492 (1), 145–154.
[8] Liang, R.; Fei, Y. J.; Prasad, P. D.; Ramamoorthy, S.; Han, H.; Yang-Feng, T. L.; Hediger, M. A.; Ganapathy, V.; Leibach, F. H. Human intestinal H+/peptide cotransporter. Cloning, functional expression, and chromosomal localization. J. Biol. Chem. 1995, 270 (12), 6456–6463.
[9] Matsui, T.; Zhu, X. L.; Watanabe, K.; Tanaka, K.; Kusano, Y.; Matsumoto, K. Combined administration of captopril with an antihypertensive Val-Tyr di-peptide to spontaneously hypertensive rats attenuates the blood pressure lowering effect. Life Sci. 2006, 79 (26), 2492–2498.
[10] Matsui, T.; Tamaya, K.; Seki, E.; Osajima, K.; Matsumoto, K.; Kawasaki, T. Absorption of Val-Tyr with in vitro angiotensin I- converting enzyme inhibitory activity into the circulating blood system of mild hypertensive subjects. Biol. Pharm. Bull. 2002, 25 (9), 1228–1230.
[11] Kawasaki, T.; Seki, E.; Osajima, K.; Yoshida, M.; Asada, K.; Matsui, T.; Osajima, Y. Antihypertensive effect of valyl-tyrosine, a short chain peptide derived from sardine muscle hydrolyzate, on mild hypertensive subjects. J. Hum. Hypertens. 2000, 14 (8), 519–523.
[12] Li, S.; Bu, T.; Zheng, J.; Liu, L.; He, G.; Wu, J. Preparation, bioavailability, and mechanism of emerging activities of Ile-Pro-Pro and Val-Pro-Pro. Compr. Rev. Food Sci. Food Saf. 2019, 18 (4), 1097–1110.
[13] Fekete, Á. A.; Ian Givens, D.; Lovegrove, J. A. Casein-derived lactotripeptides reduce systolic and diastolic blood pressure in a meta-analysis of randomised clinical trials. Nutrients 2015, 7 (1),659–681.
[14] Satake, M.; Enjoh, M.; Nakamura, Y.; Takano, T.; Kawamura, Y.; Arai, S.; Shimizu, M. Transepithelial transport of the bioactivetripeptide, Val-Pro-Pro, in human intestinal Caco-2 cell monolayers.Biosci. Biotechnol. Biochem. 2002, 66 (2), 378–384.
[15] Foltz, M.; Meynen, E. E.; Bianco, V.; Van Platerink, C.; Koning, T.M. M. G.; Kloek, J. Angiotensin converting enzyme inhibitory peptides from a lactotripeptide-enriched milk beverage are absorbed intact into the circulation. J. Nutr. 2007, 137 (4), 953–958.
[16] Engle, M. J.; Goetz, G. S.; Alpers, D. H. Caco-2 cells express a combination of colonocyte and enterocyte phenotypes. J. Cell. Physiol. 1998, 174 (3), 362–369.
[17] Sambuy, Y.; De Angelis, I.; Ranaldi, G.; Scarino, M. L.; Stammati, A.; Zucco, F. The Caco-2 cell line as a model of the intestinal barrier: Infuence of cell and culture-related factors on Caco-2 cell functional characteristics. Cell Biol. Toxicol. 2005, 21 (1), 1–26.
[18] Hidalgo, I. J.; Raub, T. J.; Borchardt, R. T. Characterization of the human colon carcinoma cell line (Caco-2) as a model system for intestinal epithelial permeability. Gastroenterology 1989, 96 (3),736–749.
[19] Shen, W.; Matsui, T. Current knowledge of intestinal absorption of bioactive peptides. Food Funct. 2017, 8 (12), 4306–4314.
[20] Zhu, X. L.; Watanabe, K.; Shiraishi, K.; Ueki, T.; Noda, Y.; Matsui, T.; Matsumoto, K. Identification of ACE-inhibitory peptides in salt- free soy sauce that are transportable across Caco-2 cell monolayers. Peptides 2008, 29 (3), 338–344.
[21] Pentzien, A. K.; Meisel, H. Transepithelial transport and stability in blood serum of angiotensin-I-converting enzyme inhibitory dipeptides. Zeitschrift für Naturforsch. - Sect. C J. Biosci. 2008, 63 (5–6), 451–459.
[22] Takeda, J.; Park, H. Y.; Kunitake, Y.; Yoshiura, K.; Matsui, T. Theaflavins, dimeric catechins, inhibit peptide transport across Caco-2 cell monolayers via down-regulation of AMP-activated protein kinase-mediated peptide transporter PEPT1. Food Chem. 2013, 138 (4), 2140–2145.
[23] Fernández-Musoles, R.; Salom, J. B.; Castelló-Ruiz, M.; Contreras,M. del M.; Recio, I.; Manzanares, P. Bioavailability of antihypertensive lactoferricin B-derived peptides: Transepithelial transport and resistance to intestinal and plasma peptidases. Int. Dairy J. 2013, 32 (2), 169–174.
[24] Tanaka, M.; Hong, S. M.; Akiyama, S.; Hu, Q. Q.; Matsui, T. Visualized absorption of anti-atherosclerotic dipeptide, Trp-His, inSprague-Dawley rats by LC-MS and MALDI-MS imaging analyses.Mol. Nutr. Food Res. 2015, 59 (8), 1541–1549.
[25] Osborne, S.; Chen, W.; Addepalli, R.; Colgrave, M.; Singh, T.; Tran, C.; Day, L. In vitro transport and satiety of a beta-lactoglobulin dipeptide and beta-casomorphin-7 and its metabolites. Food Funct. 2014, 5 (11), 2706–2718.
[26] Sontakke, S. B.; Jung, J. H.; Piao, Z.; Chung, H. J. Orally available collagen tripeptide: enzymatic stability, intestinal permeability, and absorption of Gly-Pro-Hyp and Pro-Hyp. J. Agric. Food Chem. 2016, 64 (38), 7127–7133.
[27] Yang, Y. J.; He, H. Y.; Wang, F. Z.; Ju, X. R.; Yuan, J.; Wang, L.F.; Aluko, R. E.; He, R. Transport of angiotensin converting enzyme and renin dual inhibitory peptides LY, RALP and TF across Caco-2 cell monolayers. J. Funct. Foods 2017, 35, 303–314.
[28] Lacroix, I. M. E.; Chen, X. M.; Kitts, D. D.; Li-Chan, E. C. Y. Investigation into the bioavailability of milk protein-derived peptides with dipeptidyl-peptidase IV inhibitory activity using Caco-2 cell monolayers. Food Funct. 2017, 8 (2), 701–709.
[29] Khueychai, S.; Jangpromma, N.; Choowongkomon, K.; Joompang, A.; Daduang, S.; Vesaratchavest, M.; Payoungkiattikun, W.;Tachibana, S.; Klaynongsruang, S. A novel ACE inhibitory peptide derived from alkaline hydrolysis of ostrich (Struthio camelus) egg white ovalbumin. Process Biochem. 2018, 73 (July), 235–245.
[30] Fan, H.; Xu, Q.; Hong, H.; Wu, J. Stability and transport of spent hen-derived ACE-inhibitory peptides IWHHT, IWH, and IW in human intestinal Caco-2 cell monolayers. J. Agric. Food Chem. 2018, 66 (43), 11347–11354.
[31] Foltz, M.; Cerstiaens, A.; van Meensel, A.; Mols, R.; van der Pijl, P. C.; Duchateau, G. S. M. J. E.; Augustijns, P. The angiotensin converting enzyme inhibitory tripeptides Ile-Pro-Pro and Val-Pro- Pro show increasing permeabilities with increasing physiological relevance of absorption models. Peptides 2008, 29 (8), 1312–1320.
[32] Miguel, M.; Dávalos, A.; Manso, M. A.; De La Peña, G.; Lasunción,M. A.; López-Fandiño, R. Transepithelial transport across Caco-2 cell monolayers of antihypertensive egg-derived peptides. PepT1- mediated flux of Tyr-Pro-Ile. Mol. Nutr. Food Res. 2008, 52 (12), 1507–1513.
[33] Kovacs-Nolan, J.; Zhang, H.; Ibuki, M.; Nakamori, T.; Yoshiura, K.; Turner, P. V.; Matsui, T.; Mine, Y. The PepT1-transportable soytripeptide VPY reduces intestinal inflammation. Biochim. Biophys. Acta - Gen. Subj. 2012, 1820 (11), 1753–1763.
[34] Bejjani, S.; Wu, J. Transport of IRW, an ovotransferrin-derived antihypertensive peptide, in human intestinal epithelial Caco-2 cells.J. Agric. Food Chem. 2013, 61 (7), 1487–1492.
[35] Gleeson, J. P.; Brayden, D. J.; Ryan, S. M. Evaluation of PepT1 transport of food-derived antihypertensive peptides, Ile-Pro-Pro and Leu-Lys-Pro using in vitro, ex vivo and in vivo transport models. Eur.J. Pharm. Biopharm. 2017, 115, 276–284.
[36] Lin, Q.; Xu, Q.; Bai, J.; Wu, W.; Hong, H.; Wu, J. Transport of soybean protein-derived antihypertensive peptide LSW across Caco-2 monolayers. J. Funct. Foods 2017, 39 (September), 96–102.
[37] Xu, Q.; Fan, H.; Yu, W.; Hong, H.; Wu, J. Transport study of egg- derived antihypertensive peptides (LKP and IQW) using Caco-2 and HT29 coculture monolayers. J. Agric. Food Chem. 2017, 65 (34), 7406–7414.
[38] Sowmya, K.; Mala, D.; Bhat, M. I.; Kumar, N.; Bajaj, R. K.; Kapila, S.; Kapila, R. Bio-accessible milk casein derived tripeptide (LLY) mediates overlapping anti-inflammatory and anti-oxidative effectsunder cellular (Caco-2) and in vivo milieu. J. Nutr. Biochem. 2018,62, 167–180.
[39] He, Y. Y.; Li, T. T.; Chen, J. X.; She, X. X.; Ren, D. F.; Lu, J.Transport of ACE inhibitory peptides Ile-Gln-Pro and Val-Glu-Pro derived from Spirulina platensis across Caco-2 monolayers. J. Food Sci. 2018, 83 (10), 2586–2592.
[40] Li, Y.; Wang, B.; Li, B. The in vitro bioavailability of anti-platelet peptides in collagen hydrolysate from silver carp (Hypophthalmichthys molitrix) skin. J. Food Biochem. 2020, 44 (6), e13226.
[41] Shimizu, M.; Tsunogai, M.; Arai, S. Transepithelial transport of oligopeptides in the human intestinal cell, Caco-2. Peptides 1997, 18 (5), 681–687.
[42] Fu, Y.; Young, J. F.; Rasmussen, M. K.; Dalsgaard, T. K.; Lametsch, R.; Aluko, R. E.; Therkildsen, M. Angiotensin I-converting enzyme- inhibitory peptides from bovine collagen: Insights into inhibitory mechanism and transepithelial transport. Food Res. Int. 2016, 89, 373–381.
[43] Li, Y.; Zhao, J.; Liu, X.; Xia, X.; Wang, Y.; Zhou, J. Transport of a novel angiotensin-I-converting enzyme inhibitory peptide Ala-His-Leu-Leu across human intestinal epithelial Caco-2 cells. J. Med. Food 2017, 20 (3), 243–250.
[44] Xing, L.; Liu, R.; Tang, C.; Pereira, J.; Zhou, G.; Zhang, W. The antioxidant activity and transcellular pathway of Asp-Leu-Glu-Glu in a Caco‑2 cell monolayer. Int. J. Food Sci. Technol. 2018, 53 (10), 2405–2414.
[45] Sangsawad, P.; Choowongkomon, K.; Kitts, D. D.; Chen, X. M.; Li- Chan, E. C. Y.; Yongsawatdigul, J. Transepithelial transport and structural changes of chicken angiotensin I-converting enzyme (ACE) inhibitory peptides through Caco-2 cell monolayers. J. Funct. Foods 2018, 45 (April), 401–408.
[46] Aiello, G.; Ferruzza, S.; Ranaldi, G.; Sambuy, Y.; Arnoldi, A.; Vistoli, G.; Lammi, C. Behavior of three hypocholesterolemic peptides from soy protein in an intestinal model based on differentiated Caco-2 cell. J. Funct. Foods 2018, 45 (March), 363– 370.
[47] Ritian, J.; Teng, X.; Liao, M.; Zhang, L.; Wei, Z.; Meng, R.; Liu, N. Release of dipeptidyl peptidase IV inhibitory peptides from salmon (Salmo salar) skin collagen based on digestion–intestinal absorption in vitro. Int. J. Food Sci. Technol. 2021, 56 (7), 3507–3518.
[48] Quirós, A.; Dávalos, A.; Lasunción, M. A.; Ramos, M.; Recio, I. Bioavailability of the antihypertensive peptide LHLPLP: Transepithelial flux of HLPLP. Int. Dairy J. 2008, 18 (3), 279–286.
[49] Lei, L.; Sun, H.; Liu, D.; Liu, L.; Li, S. Transport of Val-Leu-Pro- Val-Pro in human intestinal epithelial (Caco-2) cell monolayers. J. Agric. Food Chem. 2008, 56 (10), 3582–3586.
[50] Sienkiewicz-Szłapka, E.; Jarmołowska, B.; Krawczuk, S.; Kostyra, E.; Kostyra, H.; Bielikowicz, K. Transport of bovine milk-derived opioid peptides across a Caco-2 monolayer. Int. Dairy J. 2009, 19 (4), 252–257.
[51] Ding, L.; Zhang, Y.; Jiang, Y.; Wang, L.; Liu, B.; Liu, J. Transport of egg white ACE-inhibitory peptide, Gln-Ile-Gly-Leu-Phe, in human intestinal Caco-2 cell monolayers with cytoprotective effect.J. Agric. Food Chem. 2014, 62 (14), 3177–3182.
[52] Ding, L.; Wang, L.; Zhang, Y.; Liu, J. Transport of antihypertensive peptide RVPSL, ovotransferrin 328 – 332, in human intestinal Caco- 2 cell monolayers. J. Agric. Food Chem. 2015, 63 (37), 8143–8150.
[53] Maggioni, M.; Stuknytė, M.; De Luca, P.; Cattaneo, S.; Fiorilli, A.; De Noni, I.; Ferraretto, A. Transport of wheat gluten exorphins A5and C5 through an in vitro model of intestinal epithelium. Food Res. Int. 2016, 88 (Part B), 319–326.
[54] Ding, L.; Wang, L.; Zhang, T.; Yu, Z.; Liu, J. Hydrolysis and transepithelial transport of two corn gluten derived bioactive peptides in human Caco-2 cell monolayers. Food Res. Int. 2018, 106, 475–480.
[55] Sun, H.; Liu, D.; Li, S.; Qin, Z. Transepithelial transport characteristics of the antihypertensive peptide, Lys-Val-Leu-Pro- Val-Pro, in human intestinal Caco-2 cell monolayers. Biosci. Biotechnol. Biochem. 2009, 73 (2), 293–298.
[56] Gallego, M.; Grootaert, C.; Mora, L.; Aristoy, M. C.; Van Camp, J.; Toldrá, F. Transepithelial transport of dry-cured ham peptides with ACE inhibitory activity through a Caco-2 cell monolayer. J. Funct. Foods 2016, 21, 388–395.
[57] Ding, L.; Wang, L.; Yu, Z.; Zhang, T.; Liu, J. Digestion and absorption of an egg white ACE-inhibitory peptide in human intestinal Caco-2 cell monolayers. Int. J. Food Sci. Nutr. 2016, 67 (2), 111–116.
[58] Guo, Y.; Gan, J.; Zhu, Q.; Zeng, X.; Sun, Y.; Wu, Z.; Pan, D.Transepithelial transport of milk-derived angiotensin I-convertingenzyme inhibitory peptide with the RLSFNP sequence. J. Sci. Food Agric. 2018, 98 (3), 976–983.
[59] Zhang, C.; Liu, H.; Chen, S.; Luo, Y. Evaluating the effects of IADHFL on inhibiting DPP-IV activity and expression in Caco-2 cells and contributing to the amount of insulin released from INS-1 cells in vitro. Food Funct. 2018, 9 (4), 2240–2250.
[60] Tianrui, Z.; Bingtong, L.; Ling, Y.; Liping, S.; Yongliang, Z. ACE inhibitory activity in vitro and antihypertensive effect in vivo of LSGYGP and its transepithelial transport by Caco-2 cell monolayer.J. Funct. Foods 2019, 61 (January), 103488.
[61] Zhang, T.; Su, M.; Jiang, X.; Xue, Y.; Zhang, J.; Zeng, X.; Wu, Z.; Guo, Y.; Pan, D. Transepithelial transport route and liposome encapsulation of milk-derived ACE-inhibitory peptide Arg-Leu- Ser-Phe-Asn-Pro. J. Agric. Food Chem. 2019, 67 (19), 5544–5551.
[62] Sowmya, K.; Bhat, M. I.; Bajaj, R.; Kapila, S.; Kapila, R. Antioxidative and anti-inflammatory potential with trans-epithelial transport of a buffalo casein-derived hexapeptide (YFYPQL). Food Biosci. 2019, 28 (January), 151–163.
[63] Zhang, H.; Duan, Y.; Feng, Y.; Wang, J. Transepithelial transport characteristics of the cholesterol-lowing soybean peptide, WGAPSL, in Caco-2 cell monolayers. Molecules 2019, 24 (15), 2843.
[64] Lin, K.; Ma, Z.; Ramachandran, M.; De Souza, C.; Han, X.; Zhang,L. ACE inhibitory peptide KYIPIQ derived from yak milk casein induces nitric oxide production in HUVECs and diffuses via a transcellular mechanism in Caco-2 monolayers. Process Biochem. 2020, 99 (August), 103–111.
[65] Hong, H.; Zheng, Y.; Song, S.; Zhang, Y.; Zhang, C.; Liu, J.; Luo,Y. Identification and characterization of DPP-IV inhibitory peptides from silver carp swim bladder hydrolysates. Food Biosci. 2020, 38 (August), 100748.
[66] Dang, Y.; Pei, J.; Hua, Y.; Zhou, T.; Gao, X.; Wang, Y. Transport, in vivo antihypertensive effect, and pharmacokinetics of an angiotensin-converting enzyme (ACE) inhibitory peptide LVLPGE.J. Agric. Food Chem. 2021, 69 (7), 2149–2156.
[67] Vermeirssen, V.; Deplancke, B.; Tappenden, K. A.; Van Camp, J.; Gaskins, H. R.; Verstraete, W. Intestinal transport of the lactokinin Ala-Leu-Pro-Met-His-Ile-Arg through a Caco-2 Bbe monolayer. J. Pept. Sci. 2002, 8 (3), 95–100.
[68] Cakir-Kiefer, C.; Miclo, L.; Balandras, F.; Dary, A.; Soligot, C.; Roux, Y. Le. Transport across Caco-2 cell monolayer and sensitivity to hydrolysis of two anxiolytic peptides from αs1-casein, α- casozepine, and αs1-casein-(f91 – 97): Effect of bile salts. J. Agric. Food Chem. 2011, 59 (22), 11956–11965.
[69] Vij, R.; Reddi, S.; Kapila, S.; Kapila, R. Transepithelial transport of milk derived bioactive peptide VLPVPQK. Food Chem. 2016, 190, 681–688.
[70] Jin, R.; Shang, J.; Teng, X.; Zhang, L.; Liao, M.; Kang, J.; Meng, R.; Wang, D.; Ren, H.; Liu, N. Characterization of DPP-IV inhibitory peptides using an in vitro cell culture model of the intestine. J. Agric. Food Chem. 2021, 69 (9), 2711–2718.
[71] Shimizu, K.; Sato, M.; Zhang, Y.; Kouguchi, T.; Takahata, Y.; Morimatsu, F.; Shimizu, M. The bioavailable octapeptide Gly-Ala- Hyp-Gly-Leu-Hyp-Gly-Pro stimulates nitric oxide synthesis in vascular endothelial cells. J. Agric. Food Chem. 2010, 58 (11), 6960–6965.
[72] Fernández-Tomé, S.; Sanchón, J.; Recio, I.; Hernández-Ledesma, B. Transepithelial transport of lunasin and derived peptides: Inhibitoryeffects on the gastrointestinal cancer cells viability. J. Food Compos. Anal. 2018, 68, 101–110.
[73] Sun, L.; Wu, B.; Yan, M.; Hou, H.; Zhuang, Y. Antihypertensive effect in vivo of QAGLSPVR and its transepithelial transport through the Caco-2 cell monolayer. Mar. Drugs 2019, 17 (5), 288.
[74] Xu, F.; Mejia, E. G. de; Chen, H.; Rebecca, K.; Pan, M.; He, R.; Yao, Y.; Wang, L.; Ju, X. Assessment of the DPP-IV inhibitory activity of a novel octapeptide derived from rapeseed using Caco-2 cell monolayers and molecular docking analysis. J. Food Biochem. 2020, 44 (10), e13406.
[75] Lammi, C.; Aiello, G.; Bollati, C.; Li, J.; Bartolomei, M.; Ranaldi, G.; Ferruzza, S.; Fassi, E. M. A.; Grazioso, G.; Sambuy, Y.; Arnoldi,A. Trans‐epithelial transport, metabolism and biological activity assessment of the multi‐target lupin peptide LILPKHSDAD (P5) and its metabolite LPKHSDAD (P5‐met). Nutrients 2021, 13 (3),863.
[76] Xu, F.; Zhang, J.; Wang, Z.; Yao, Y.; Atungulu, G. G.; Ju, X.; Wang,L. Absorption and metabolism of peptide WDHHAPQLR derived from rapeseed protein and inhibition of HUVEC apoptosis under oxidative stress. J. Agric. Food Chem. 2018, 66 (20), 5178–5189.
[77] Xu, F.; Wang, L.; Ju, X.; Zhang, J.; Yin, S.; Shi, J.; He, R.; Yuan, Q.Transepithelial transport of YWDHNNPQIR and its metabolic fate with cytoprotection against oxidative stress in human intestinal Caco-2 cells. J. Agric. Food Chem. 2017, 65 (10), 2056–2065.
[78] Xu, Z.; Chen, H.; Fan, F.; Shi, P.; Cheng, S.; Tu, M.; Ei-Seedi, H. R.; Du, M.; Du, M. Pharmacokinetics and transport of an osteogenic dodecapeptide. J. Agric. Food Chem. 2020, 68 (37), 9961–9967.
[79] Regazzo, D.; Mollé, D.; Gabai, G.; Tomé, D.; Dupont, D.; Leonil, J.; Boutrou, R. The (193 – 209) 17-residues peptide of bovine β-caseinis transported through Caco-2 monolayer. Mol. Nutr. Food Res.2010, 54 (10), 1428–1435.
[80] Nakashima, E. M. N.; Kudo, A.; Iwaihara, Y.; Tanaka, M.; Matsumoto, K.; Matsui, T. Application of 13C stable isotope labeling liquid chromatography-multiple reaction monitoring-tandem mass spectrometry method for determining intact absorption of bioactive dipeptides in rats. Anal. Biochem. 2011, 414 (1), 109–116.
[81] Nakashima, E. M. N.; Qing, H. Q.; Tanaka, M.; Matsui, T. Improved detection of di-peptides by liquid chromatography-tandem mass spectrometry with 2,4,6-trinitrobenzene sulfonate conversion. Biosci. Biotechnol. Biochem. 2013, 77 (10), 2094–2099.
[82] Hashimoto, C.; Iwaihara, Y.; Chen, S. J.; Tanaka, M.; Watanabe, T.; Matsui, T. Highly-sensitive detection of free advanced glycation end-products by liquid chromatography-electrospray ionization- tandem mass spectrometry with 2,4,6-trinitrobenzene sulfonate derivatization. Anal. Chem. 2013, 85 (9), 4289–4295.
[83] Nakao, R.; Hirasaka, K.; Goto, J.; Ishidoh, K.; Yamada, C.; Ohno,A.; Okumura, Y.; Nonaka, I.; Yasutomo, K.; Baldwin, K. M.; Kominami, E.; Higashibata, A.; Nagano, K.; Tanaka, K.; Yasui, N.; Mills, E. M.; Takeda, S.; Nikawa, T. Ubiquitin ligase Cbl-b is a negative regulator for insulin-like growth factor 1 signaling during muscle atrophy caused by unloading. Mol. Cell. Biol. 2009, 29 (17), 4798–4811.
[84] Kawai, N.; Hirasaka, K.; Maeda, T.; Haruna, M.; Shiota, C.; Ochi,A.; Abe, T.; Kohno, S.; Ohno, A.; Teshima-Kondo, S.; Mori, H.; Tanaka, E.; Nikawa, T. Prevention of skeletal muscle atrophy in vitro using anti-ubiquitination oligopeptide carried by atelocollagen. Biochim. Biophys. Acta - Mol. Cell Res. 2015, 1853 (5), 873–880.
[85] Ochi, A.; Abe, T.; Nakao, R.; Yamamoto, Y.; Kitahata, K.; Takagi, M.; Hirasaka, K.; Ohno, A.; Teshima-Kondo, S.; Taesik, G.; Choi, I.; Kawamura, T.; Nemoto, H.; Mukai, R.; Terao, J.; Nikawa, T. N- myristoylated ubiquitin ligase Cbl-b inhibitor prevents onglucocorticoid-induced atrophy in mouse skeletal muscle. Arch. Biochem. Biophys. 2015, 570, 23–31.
[86] Thomason, D. B.; Biggs, R. B.; Booth, F. W. Protein metabolism and beta-myosin heavy-chain mRNA in unweighted soleus muscle. Am. J. Physiol. Integr. Comp. Physiol. 1989, 257 (2), R300–R305.
[87] Tischler, M. E.; Rosenberg, S.; Satarug, S.; Henriksen, E. J.; Kirby,C. R.; Tome, M.; Chase, P. Different mechanisms of increased proteolysis in atrophy induced by denervation or unweighting of rat soleus muscle. Metabolism 1990, 39 (7), 756–763.
[88] Nikawa, T.; Ishidoh, K.; Hirasaka, K.; Ishihara, I.; Ikemoto, M.; Kano, M.; Kominami, E.; Nonaka, I.; Ogawa, T.; Adams, G. R.; Baldwin, K. M.; Yasui, N.; Kishi, K.; Takeda, S. Skeletal muscle gene expression in space-flown rats. FASEB J. 2004, 18 (3), 522–524.
[89] Matsui, T.; Tanaka, M. Antihypertensive peptides and their underlying mechanisms. In Bioactive Proteins and Peptides as Functional Foods and Nutraceuticals; Wiley-Blackwell: Oxford, UK, 2010; 43–54.
[90] Shangguan, D.; Zhao, Y.; Han, H.; Zhao, R.; Liu, G. Derivatization and fluorescence detection of amino acids and peptides with 9-fluorenylmethyl chloroformate on the surface of a solid adsorbent.Anal. Chem. 2001, 73 (9), 2054–2057.
[91] Deantonis, K. M.; Brown, P. R.; Cohen, S. A. High-performance liquid chromatographic analysis of synthetic peptides using derivatization with 6-aminoquinolyl-N-hydroxysuccinimidyl carbamate. Anal. Biochem. 1994, 223 (2), 191–197.
[92] Zhu, R.; Kok, W. T. Postcolumn derivatization of peptides with fluorescamine in capillary electrophoresis. J. Chromatogr. A 1998, 814 (1–2), 213–221.
[93] Kang, X.; Xiao, J.; Huang, X.; Gu, Z. Optimization of dansyl derivatization and chromatographic conditions in the determination of neuroactive amino acids of biological samples. Clin. Chim. Acta 2006, 366 (1–2), 352–356.
[94] Matsui, T.; Tamaya, K.; Kawasaki, T.; Osajima, Y. Determination of angiotensin metabolites in human plasma by fluorimetric high- performance liquid chromatography using a heart-cut column- switching technique. J. Chromatogr. B Biomed. Sci. Appl. 1999, 729 (1–2), 89–95.
[95] Matsui, T.; Imamura, M.; Oka, H.; Osajima, K.; Kimoto, K. I.; Kawasaki, T.; Matsumoto, K. Tissue distribution of antihypertensivedipeptide, Val-Tyr, after its single oral administration to spontaneously hypertensive rats. J. Pept. Sci. 2004, 10 (9), 535–545.
[96] Wilm, M. Principles of electrospray ionization. Mol. Cell.Proteomics 2011, 10 (7), M111.009407.
[97] Iribarne, J. V.; Dziedzic, P. J.; Thomson, B. A. Atmospheric pressure ion evaporation-mass spectrometry. Int. J. Mass Spectrom. Ion Phys. 1983, 50 (3), 331–347.
[98] Iribarne, J. V.; Thomson, B. A. On the evaporation of small ions from charged droplets. J. Chem. Phys. 1976, 64 (6), 2287–2294.
[99] Cech, N. B.; Enke, C. G. Relating electrospray ionization response to nonpolar character of small peptides. Anal. Chem. 2000, 72 (13), 2717–2723.
[100] Shimbo, K.; Oonuki, T.; Yahashi, A.; Hirayama, K.; Miyano, H. Precolumn derivatization reagents for high-speed analysis of amines and amino acids in biological fluid using liquid chromatography/electrospray ionization tandem mass spectrometry. Rapid Commun. Mass Spectrom. 2009, 23 (10), 1483–1492.
[101] Pashkova, A.; Moskovets, E.; Karger, B. L. Coumarin tags for improved analysis of peptides by MALDI-TOF MS and MS/MS. 1.Enhancement in MALDI MS signal intensities. Anal. Chem. 2004,76 (15), 4550–4557.
[102] Cech, N. B.; Krone, J. R.; Enke, C. G. Predicting electrospray response from chromatographic retention time. Anal. Chem. 2001, 73 (2), 208–213.
[103] Liigand, P.; Kaupmees, K.; Kruve, A. Influence of the amino acid composition on the ionization efficiencies of small peptides. J. Mass Spectrom. 2019, 54 (6), 481–487.
[104] Rebane, R.; Oldekop, M. L.; Herodes, K. Comparison of amino acid derivatization reagents for LC-ESI-MS analysis. Introducing a novel phosphazene-based derivatization reagent. J. Chromatogr. B Anal. Technol. Biomed. Life Sci. 2012, 904, 99–106.
[105] Leng, J.; Wang, H.; Zhang, L.; Zhang, J.; Wang, H.; Guo, Y. A highly sensitive isotope-coded derivatization method and its application for the mass spectrometric analysis of analytes containing the carboxyl group. Anal. Chim. Acta 2013, 758, 114– 121.
[106] Mirzaei, H.; Regnier, F. Enhancing electrospray ionization efficiency of peptides by derivatization. Anal. Chem. 2006, 78 (12), 4175–4183.
[107] Hermans, J.; Ongay, S.; Markov, V.; Bischoff, R. Physicochemical parameters affecting the electrospray ionization efficiency of amino acids after acylation. Anal. Chem. 2017, 89 (17), 9159–9166.
[108] Connolly, M. L. Analytical molecular surface calculation. J. Appl.Crystallogr. 1983, 16 (5), 548–558.
[109] Raji, M. A.; Fryčák, P.; Temiyasathit, C.; Kim, S. B.; Mavromaras, G.; Ahn, J. M.; Schug, K. A. Using multivariate statistical methods to model the electrospray ionization response of GXG tripeptides based on multiple physicochemical parameters. Rapid Commun. Mass Spectrom. 2009, 23 (14), 2221–2232.
[110] Randall, S. M.; Koryakina, I.; Williams, G. J.; Muddiman, D. C. Evaluating nonpolar surface area and liquid chromatography/mass spectrometry response: An application for site occupancy measurements for enzyme intermediates in polyketide biosynthesis. Rapid Commun. Mass Spectrom. 2014, 28 (23), 2511–2522.
[111] Toyo’oka, T. Derivatization-based high-throughput bioanalysis by LC-MS. Anal. Sci. 2017, 33 (5), 555–564.
[112] Liigand, J.; Kruve, A.; Leito, I.; Girod, M.; Antoine, R. Effect of mobile phase on electrospray ionization efficiency. J. Am. Soc. Mass Spectrom. 2014, 25 (11), 1853–1861.
[113] Roth, K. D. W.; Huang, Z. H.; Sadagopan, N.; Watson, J. T. Charge derivatization of peptides for analysis by mass spectrometry. Mass Spectrom. Rev. 1998, 17 (4), 255–274.
[114] Li, X.; Franke, A. A. Improved LC-MS method for the determination of fatty acids in red blood cells by LC-Orbitrap MS. Anal. Chem. 2011, 83 (8), 3192–3198.
[115] Kretschmer, A.; Giera, M.; Wijtmans, M.; De Vries, L.; Lingeman, H.; Irth, H.; Niessen, W. M. A. Derivatization of carboxylic acids with 4-APEBA for detection by positive-ion LC-ESI-MS(/MS) applied for the analysis of prostanoids and NSAID in urine. J. Chromatogr. B Anal. Technol. Biomed. Life Sci. 2011, 879 (17–18), 1393–1401.
[116] Julka, S.; Regnier, F. E. Recent advancements in differential proteomics based on stable isotope coding. Briefings Funct. Genomics Proteomics 2005, 4 (2), 158–177.
[117] Hong, S. M.; Tanaka, M.; Koyanagi, R.; Shen, W.; Matsui, T. Structural design of oligopeptides for intestinal transport model. J. Agric. Food Chem. 2016, 64 (10), 2072–2079.
[118] Boersema, P. J.; Raijmakers, R.; Lemeer, S.; Mohammed, S.; Heck,A. J. R. Multiplex peptide stable isotope dimethyl labeling for quantitative proteomics. Nat. Protoc. 2009, 4 (4), 484–494.
[119] Mochizuki, T.; Taniguchi, S.; Tsutsui, H.; Min, J. Z.; Inoue, K.; Todoroki, K.; Toyo’oka, T. Relative quantification of enantiomers of chiral amines by high-throughput LC-ESI-MS/MS using isotopic variants of light and heavy L-pyroglutamic acids as the derivatization reagents. Anal. Chim. Acta 2013, 773, 76–82.
[120] Piovesana, S.; Montone, C. M.; Cavaliere, C.; Crescenzi, C.; La Barbera, G.; Laganà, A.; Capriotti, A. L. Sensitive untargeted identification of short hydrophilic peptides by high performance liquid chromatography on porous graphitic carbon coupled to high resolution mass spectrometry. J. Chromatogr. A 2019, 1590, 73–79.
[121] Greguš, M.; Kostas, J. C.; Ray, S.; Abbatiello, S. E.; Ivanov, A. R. Improved sensitivity of ultralow flow LC-MS-based proteomic profiling of limited samples using monolithic capillary columns and FAIMS technology. Anal. Chem. 2020, 92 (21), 14702–14712.
[122] Lortie, M.; Bark, S.; Blantz, R.; Hook, V. Detecting low-abundance vasoactive peptides in plasma: progress toward absolute quantitationusing nano liquid chromatography-mass spectrometry. Anal. Biochem. 2009, 394 (2), 164–170.
[123] Glass, D. J. Skeletal muscle hypertrophy and atrophy signaling pathways. Int. J. Biochem. Cell Biol. 2005, 37 (10), 1974–1984.
[124] Ikemoto, M.; Nikawa, T.; Takeda, S.; Watanabe, C.; Kitano, T.; Baldwin, K. M.; Izumi, R.; Nonaka, I.; Towatari, T.; Teshima, S.; Rokutan, K.; Kishi, K. Space shuttle flight (STS 90) enhancesdegradation of rat myosin heavy chain in association with activation of ubiquitin-proteasome pathway. FASEB J. 2001, 15 (7), 1279–1281.
[125] Hanh, V. T.; Shen, W.; Tanaka, M.; Siltari, A.; Korpela, R.; Matsui,T. Effect of aging on the absorption of small peptides in spontaneously hypertensive rats. J. Agric. Food Chem. 2017, 65 (29), 5935–5943.
[126] Jappar, D.; Wu, S. P.; Hu, Y.; Smith, D. E. Significance and regional dependency of peptide transporter (PEPT) 1 in the intestinal permeability of glycylsarcosine: In situ single-pass perfusion studies in wild-type and Pept1 knockout mice. Drug Metab. Dispos. 2010, 38 (10), 1740–1746.
[127] Madara, J. L.; Barenberg, D.; Carlson, S. Effects of cytochalasin D on occluding junctions of intestinal absorptive cells: Further evidence that the cytoskeleton may influence paracellular permeability and junctional charge selectivity. J. Cell Biol. 1986, 102 (6), 2125–2136.
[128] Hong, S. M.; Tanaka, M.; Yoshii, S.; Mine, Y.; Matsui, T. Enhanced visualization of small peptides absorbed in rat small intestine by phytic-acid-aided matrix-assisted laser desorption/ionization- imaging mass spectrometry. Anal. Chem. 2013, 85 (21), 10033–10039.
[129] Aito-Inoue, M.; Lackeyram, D.; Fan, M. Z.; Sato, K.; Mine, Y. Transport of a tripeptide, Gly-Pro-Hyp, across the porcine intestinal brush-border membrane. J. Pept. Sci. 2007, 13 (7), 468–474.
[130] Dörfel, M. J.; Huber, O. Modulation of tight junction structure and function by kinases and phosphatases targeting occludin. J. Biomed. Biotechnol. 2012, 2012, 807356.
[131] Estaki, M. Interplay between intestinal alkaline phosphatase, diet, gut microbes and immunity. World J. Gastroenterol. 2014, 20 (42), 15650.
[132] Brodin, B.; Nielsen, C. U.; Steffansen, B.; Frøkjær, S. Transport of peptidomimetic drugs by the intestinal di/tri-peptide transporter, PepT1. Pharmacol. Toxicol. 2002, 90 (6), 285–296.
[133] Newstead, S.; Drew, D.; Cameron, A. D.; Postis, V. L. G.; Xia, X.;Fowler, P. W.; Ingram, J. C.; Carpenter, E. P.; Sansom, M. S. P.; McPherson, M. J.; Baldwin, S. A.; Iwata, S. Crystal structure of a prokaryotic homologue of the mammalian oligopeptide-proton symporters, PepT1 and PepT2. EMBO J. 2011, 30 (2), 417–426.
[134] Chothe, P.; Singh, N.; Ganapathy, V. Evidence for two different broad-specificity oligopeptide transporters in intestinal cell line Caco-2 and colonic cell line CCD841. Am. J. Physiol. - Cell Physiol. 2011, 300 (6), 1260–1269.
[135] Xu, Q.; Hong, H.; Wu, J.; Yan, X. Bioavailability of bioactive peptides derived from food proteins across the intestinal epithelial membrane: A review. Trends Food Sci. Technol. 2019, 86 (February), 399–411.
[136] Sánchez-Rivera, L.; Ares, I.; Miralles, B.; Gómez-Ruiz, J. Á.; Recio, I.; Martínez-Larrañaga, M. R.; Anadón, A.; Martínez, M. A. Bioavailability and kinetics of the antihypertensive casein-derivedpeptide HLPLP in rats. J. Agric. Food Chem. 2014, 62 (49), 11869–11875.
[137] Picariello, G.; Ferranti, P.; Addeo, F. Use of brush border membrane vesicles to simulate the human intestinal digestion. Food Res. Int. 2016, 88 (Part B), 327–335.
[138] Abe, T.; Kohno, S.; Yama, T.; Ochi, A.; Suto, T.; Hirasaka, K.; Ohno, A.; Teshima-Kondo, S.; Okumura, Y.; Oarada, M.; Choi, I.; Mukai, R.; Terao, J.; Nikawa, T. Soy glycinin contains a functional inhibitory sequence against muscle-atrophy-associated ubiquitin ligase Cbl-b. Int. J. Endocrinol. 2013, 2013, 907565.
[139] Ohno, A.; Ochi, A.; Maita, N.; Ueji, T.; Bando, A.; Nakao, R.; Hirasaka, K.; Abe, T.; Teshima-Kondo, S.; Nemoto, H.; Okumura, Y.; Higashibata, A.; Yano, S.; Tochio, H.; Nikawa, T. Structural analysis of the TKB domain of ubiquitin ligase Cbl-b complexed with its small inhibitory peptide, Cblin. Arch. Biochem. Biophys. 2016, 594, 1–7.
[140] Ten Have, G. A. M.; Van Der Pijl, P. C.; Kies, A. K.; Deutz, N. E.P. Enhanced lacto-tri-peptide bio-availability by co-ingestion of macronutrients. PLoS One 2015, 10 (6), e0130638.
[141] Pye, C. R.; Hewitt, W. M.; Schwochert, J.; Haddad, T. D.; Townsend,C. E.; Etienne, L.; Lao, Y.; Limberakis, C.; Furukawa, A.; Mathiowetz, A. M.; Price, D. A.; Liras, S.; Lokey, R. S. Nonclassical size dependence of permeation defines bounds for passive adsorption of large drug molecules. J. Med. Chem. 2017, 60 (5), 1665–1672.