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Volumn 141, Issue 1, 2013, Pages 644-653

Inhibition of dipeptidyl peptidase IV and xanthine oxidase by amino acids and dipeptides

Author keywords

Amino acids; AutoDock Vina; Dipeptides; Dipeptidyl peptidase IV inhibitors; Intestinal stability; Milk; Predictive modelling; Xanthine oxidase inhibitors

Indexed keywords

AMINO ACIDS; BINDING SITES;

EID: 84884602268     PISSN: 03088146     EISSN: 18737072     Source Type: Journal    
DOI: 10.1016/j.foodchem.2013.02.115     Document Type: Article
Times cited : (137)

References (32)
  • 1
    • 0015160590 scopus 로고
    • Intestinal transport of dipeptides in man: Relative importance of hydrolysis and intact absorption
    • Adibi, S. A., & Morse, E. L. (1971). Intestinal transport of dipeptides in man: Relative importance of hydrolysis and intact absorption. Journal of Clinical Investigation, 50(11), 2266-2275.
    • (1971) Journal of Clinical Investigation , vol.50 , Issue.11 , pp. 2266-2275
    • Adibi, S.A.1    Morse, E.L.2
  • 2
    • 29144522905 scopus 로고    scopus 로고
    • Rigidity and flexibility of dipeptidyl peptidase IV: Crystal structures of and docking experiments with DPIV
    • DOI 10.1016/j.jmb.2005.11.014, PII S0022283605014002
    • Engel, M., Hoffmann, T., Manhart, S., Heiser, U., Chambre, S., Huber, R., et al. (2006). Rigidity and flexibility of dipeptidyl peptidase IV: Crystal structures of and docking experiments with DPP IV. Journal of Molecular Biology, 355(4), 768-783. (Pubitemid 41817635)
    • (2006) Journal of Molecular Biology , vol.355 , Issue.4 , pp. 768-783
    • Engel, M.1    Hoffmann, T.2    Manhart, S.3    Heiser, U.4    Chambre, S.5    Huber, R.6    Demuth, H.-U.7    Bode, W.8
  • 4
    • 84884636179 scopus 로고    scopus 로고
    • Swiss institute of bioinformatics, bioinformatics eessource portal
    • ExPaSy. Swiss institute of bioinformatics, bioinformatics eessource portal. (2011). 〈http://web.expasy.org/peptide-cutter/〉.
    • (2011)
  • 5
    • 0742296736 scopus 로고    scopus 로고
    • Milk protein hydrolysates and bioactive peptides
    • P. F. Fox & P. L. H. McSweeney (Eds.). 3rd ed. NewYork: Kluwer Academic/Plenum Publishers
    • FitzGerald, R. J., & Meisel, H. (2003). Milk protein hydrolysates and bioactive peptides. In P. F. Fox & P. L. H. McSweeney (Eds.). Advanced dairy chemistry: Volume 1: Proteins, Part B (vol. 1, 3rd ed., pp. 675-698). NewYork: Kluwer Academic/Plenum Publishers.
    • (2003) Advanced Dairy Chemistry: Volume 1: Proteins, Part B , vol.1 , pp. 675-698
    • Fitzgerald, R.J.1    Meisel, H.2
  • 6
    • 69749111280 scopus 로고    scopus 로고
    • Modeling of the relationship between dipeptide structure and dipeptide stability, permeability, and ACE inhibitory activity
    • Foltz, M., Van Buren, L., Klaffke, W., & Duchateau, G. S. M. J. E. (2009). Modeling of the relationship between dipeptide structure and dipeptide stability, permeability, and ACE inhibitory activity. Journal of Food Science, 74(7), H243-H251.
    • (2009) Journal of Food Science , vol.74 , Issue.7
    • Foltz, M.1    Van Buren, L.2    Klaffke, W.3    Duchateau, G.S.M.J.E.4
  • 7
    • 84866312460 scopus 로고    scopus 로고
    • Identification of novel human dipeptidyl peptidase-IV inhibitors of natural prigin (part I): Virtual screening and activity assays
    • Guasch, L., Ojeda, M. J., González-Abuín, N., Sala, E., Cereto-Massagué, A., Mulero, M., et al. (2012). Identification of novel human dipeptidyl peptidase-IV inhibitors of natural prigin (part I): Virtual screening and activity assays. PLoS ONE, 7(9), e44971.
    • (2012) PLoS ONE , vol.7 , Issue.9
    • Guasch, L.1    Ojeda, M.J.2    González-Abuín, N.3    Sala, E.4    Cereto-Massagué, A.5    Mulero, M.6
  • 8
    • 84860295841 scopus 로고    scopus 로고
    • Production of dipeptidyl peptidase IV inhibitory peptides from defatted rice bran
    • Hatanaka, T., Inoue, Y., Arima, J., Kumagai, Y., Usuki, H., Kawakami, K., et al. (2012). Production of dipeptidyl peptidase IV inhibitory peptides from defatted rice bran. Food Chemistry, 134(2), 797-802.
    • (2012) Food Chemistry , vol.134 , Issue.2 , pp. 797-802
    • Hatanaka, T.1    Inoue, Y.2    Arima, J.3    Kumagai, Y.4    Usuki, H.5    Kawakami, K.6
  • 9
    • 13144253218 scopus 로고    scopus 로고
    • Uric acid: A new look at an old risk marker for cardiovascular disease, metabolic syndrome, and type 2 diabetes mellitus: The urate redox shuttle
    • Hayden, M. R., & Tyagi, S. C. (2001). Uric acid: A new look at an old risk marker for cardiovascular disease, metabolic syndrome, and type 2 diabetes mellitus: The urate redox shuttle. Nutrition and Metabolism, 1(10), 1-10.
    • (2001) Nutrition and Metabolism , vol.1 , Issue.10 , pp. 1-10
    • Hayden, M.R.1    Tyagi, S.C.2
  • 10
    • 3242809886 scopus 로고    scopus 로고
    • The crystal structure of human dipeptidyl peptidase IV (DPPIV) complex with diprotin A
    • Hiramatsu, H., Yamamoto, A., Kyono, K., Higashiyama, Y., Fukushima, C., Shima, H., et al. (2005). The crystal structure of human dipeptidyl peptidase IV (DPPIV) complex with diprotin A. Biological Chemistry, 385(6), 561-564.
    • (2005) Biological Chemistry , vol.385 , Issue.6 , pp. 561-564
    • Hiramatsu, H.1    Yamamoto, A.2    Kyono, K.3    Higashiyama, Y.4    Fukushima, C.5    Shima, H.6
  • 11
    • 84859788742 scopus 로고    scopus 로고
    • Dipeptidyl-peptidase IV inhibitory activity of peptides derived from tuna cooking juice hydrolysates
    • Huang, S.-L., Jao, C.-L., Ho, K.-P., & Hsu, K.-C. (2012). Dipeptidyl-peptidase IV inhibitory activity of peptides derived from tuna cooking juice hydrolysates. Peptides, 35(1), 114-121.
    • (2012) Peptides , vol.35 , Issue.1 , pp. 114-121
    • Huang, S.-L.1    Jao, C.-L.2    Ho, K.-P.3    Hsu, K.-C.4
  • 12
    • 79953713734 scopus 로고    scopus 로고
    • Selective inhibition of dipeptidyl peptidase 4 by targeting a substrate-specific secondary binding site
    • Kühn-Wache, K., Bär, J. W., Hoffmann, T., Wolf, R., Rahfeld, J.-U., & Demuth, H.-U. (2011). Selective inhibition of dipeptidyl peptidase 4 by targeting a substrate-specific secondary binding site. Biological Chemistry, 392(3), 223-231.
    • (2011) Biological Chemistry , vol.392 , Issue.3 , pp. 223-231
    • Kühn-Wache, K.1    Bär, J.W.2    Hoffmann, T.3    Wolf, R.4    Rahfeld, J.-U.5    Demuth, H.-U.6
  • 13
    • 84861332110 scopus 로고    scopus 로고
    • Dipeptidyl peptidase-IV inhibitory activity of dairy protein hydrolysates
    • Lacroix, I. M. E., & Li-Chan, E. C. Y. (2012a). Dipeptidyl peptidase-IV inhibitory activity of dairy protein hydrolysates. International Dairy Journal, 25(2), 97-102.
    • (2012) International Dairy Journal , vol.25 , Issue.2 , pp. 97-102
    • Lacroix, I.M.E.1    Li-Chan, E.C.Y.2
  • 14
    • 84860318855 scopus 로고    scopus 로고
    • Evaluation of the potential of dietary proteins as precursors of dipeptidyl peptidase (DPP)-IV inhibitors by an in silico approach
    • Lacroix, I. M. E., & Li-Chan, E. C. Y. (2012b). Evaluation of the potential of dietary proteins as precursors of dipeptidyl peptidase (DPP)-IV inhibitors by an in silico approach. Journal of Functional Foods, 4(2), 403-422.
    • (2012) Journal of Functional Foods , vol.4 , Issue.2 , pp. 403-422
    • Lacroix, I.M.E.1    Li-Chan, E.C.Y.2
  • 17
    • 84865324339 scopus 로고    scopus 로고
    • Tryptophan-containing milk proteinderived dipeptides inhibit xanthine oxidase
    • Nongonierma, A. B., & FitzGerald, R. J. (2012). Tryptophan-containing milk proteinderived dipeptides inhibit xanthine oxidase. Peptides, 37(2), 263-272.
    • (2012) Peptides , vol.37 , Issue.2 , pp. 263-272
    • Nongonierma, A.B.1    Fitzgerald, R.J.2
  • 18
    • 84871549211 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV inhibitory and antioxidative properties of milk-derived dipeptides and hydrolysates
    • Nongonierma, A. B., & FitzGerald, R. J. (2013). Dipeptidyl peptidase IV inhibitory and antioxidative properties of milk-derived dipeptides and hydrolysates. Peptides, 39, 157-163.
    • (2013) Peptides , vol.39 , pp. 157-163
    • Nongonierma, A.B.1    Fitzgerald, R.J.2
  • 19
    • 84859791745 scopus 로고    scopus 로고
    • Predictive modelling of angiotensin converting enzyme inhibitory dipeptides
    • Norris, R., Casey, F., FitzGerald, R. J., Shields, D., & Mooney, C. (2012). Predictive modelling of angiotensin converting enzyme inhibitory dipeptides. Food Chemistry, 133(4), 1349-1354.
    • (2012) Food Chemistry , vol.133 , Issue.4 , pp. 1349-1354
    • Norris, R.1    Casey, F.2    Fitzgerald, R.J.3    Shields, D.4    Mooney, C.5
  • 21
    • 46749134762 scopus 로고    scopus 로고
    • Mechanism of inhibition of xanthine oxidoreductase by allopurinol: Crystal structure of reduced bovine milk xanthine oxidoreductase bound with oxipurinol
    • DOI 10.1080/15257770802146577, PII 794699692
    • Okamoto, K., Eger, B. T., Nishino, T., Pai, E. F., & Nishino, T. (2008). Mechanism of inhibition of xanthine oxidoreductase by Allopurinol: Crystal structure of reduced bovine milk xanthine oxidoreductase bound with oxipurinol. Nucleosides, Nucleotides & Nucleic Acids, 27(6-7), 888-893. (Pubitemid 351948548)
    • (2008) Nucleosides, Nucleotides and Nucleic Acids , vol.27 , Issue.6-7 , pp. 888-893
    • Okamoto, K.1    Eger, B.T.2    Nishino, T.3    Pai, E.F.4    Nishino, T.5
  • 22
    • 33748319573 scopus 로고    scopus 로고
    • Antioxidative peptides derived from milk proteins
    • DOI 10.1016/j.idairyj.2006.06.005, PII S0958694606001488
    • Pihlanto, A. (2006). Antioxidative peptides derived from milk proteins. International Dairy Journal, 16(11), 1306-1314. (Pubitemid 44331582)
    • (2006) International Dairy Journal , vol.16 , Issue.11 , pp. 1306-1314
    • Pihlanto, A.1
  • 23
    • 84878364395 scopus 로고    scopus 로고
    • Antioxidative peptides: Enzymatic production, in vitro and in vivo antioxidant activity and potential applications of milk-derived antioxidative peptides
    • [published online]
    • Power, O., Jakeman, P., & FitzGerald, R. (2012). Antioxidative peptides: Enzymatic production, in vitro and in vivo antioxidant activity and potential applications of milk-derived antioxidative peptides. Amino Acids, 1-24 [published online].
    • (2012) Amino Acids , pp. 1-24
    • Power, O.1    Jakeman, P.2    Fitzgerald, R.3
  • 24
    • 34250643512 scopus 로고    scopus 로고
    • Docking and virtual screening of ACE inhibitory dipeptides
    • DOI 10.1007/s00217-006-0450-6
    • Pripp, A. (2007). Docking and virtual screening of ACE inhibitory dipeptides. European Food Research and Technology, 225(3), 589-592. (Pubitemid 46945678)
    • (2007) European Food Research and Technology , vol.225 , Issue.3-4 , pp. 589-592
    • Pripp, A.H.1
  • 25
    • 84856993484 scopus 로고    scopus 로고
    • R Development Core Team: A language and environment for statistical computing [computer program]
    • R Development Core Team: A language and environment for statistical computing [computer program] (2004). Vienna, Austria: R Foundation for Statistical Computing. Available at http://www.R-project.org.in.
    • (2004) Vienna, Austria: R Foundation for Statistical Computing
  • 26
    • 84857763136 scopus 로고    scopus 로고
    • Flavonoid glycosides isolated from unique legume plant extracts as novel inhibitors of xanthine oxidase
    • Spanou, C., Veskoukis, A. S., Kerasioti, T., Kontou, M., Angelis, A., Aligiannis, N., et al. (2012). Flavonoid glycosides isolated from unique legume plant extracts as novel inhibitors of xanthine oxidase. PLoS ONE, 7(3), e32214.
    • (2012) PLoS ONE , vol.7 , Issue.3
    • Spanou, C.1    Veskoukis, A.S.2    Kerasioti, T.3    Kontou, M.4    Angelis, A.5    Aligiannis, N.6
  • 27
    • 84864419151 scopus 로고    scopus 로고
    • PepSite: Prediction of peptide-binding sites from protein surfaces
    • Trabuco, L. G., Lise, S., Petsalaki, E., & Russell, R. B. (2012). PepSite: Prediction of peptide-binding sites from protein surfaces. Nucleic Acids Research, 40(W1), W423-W427.
    • (2012) Nucleic Acids Research , vol.40 , Issue.W1
    • Trabuco, L.G.1    Lise, S.2    Petsalaki, E.3    Russell, R.B.4
  • 28
    • 76149120388 scopus 로고    scopus 로고
    • AutoDock Vina: Improving the speed and accuracy of docking with a new scoring function, efficient optimisation and multithreading
    • Trott, O., & Olsen, A. J. (2010). AutoDock Vina: Improving the speed and accuracy of docking with a new scoring function, efficient optimisation and multithreading. Journal of Computational Chemistry, 31, 455-461.
    • (2010) Journal of Computational Chemistry , vol.31 , pp. 455-461
    • Trott, O.1    Olsen, A.J.2
  • 29
    • 82655173852 scopus 로고    scopus 로고
    • Isolation and identification of casein-derived dipeptidyl-peptidase 4 (DPP-4)-inhibitory peptide LPQNIPPL from gouda-type cheese and its effect on plasma glucose in rats
    • Uenishi, H., Kabuki, T., Seto, Y., Serizawa, A., & Nakajima, H. (2012). Isolation and identification of casein-derived dipeptidyl-peptidase 4 (DPP-4)-inhibitory peptide LPQNIPPL from gouda-type cheese and its effect on plasma glucose in rats. International Dairy Journal, 22(1), 24-30.
    • (2012) International Dairy Journal , vol.22 , Issue.1 , pp. 24-30
    • Uenishi, H.1    Kabuki, T.2    Seto, Y.3    Serizawa, A.4    Nakajima, H.5
  • 31
    • 84866883091 scopus 로고    scopus 로고
    • In vitro inhibition of dipeptidyl peptidase IV by peptides derived from the hydrolysis of amaranth (Amaranthus hypochondriacus L.) proteins
    • Velarde-Salcedo, A. J., Barrera-Pacheco, A., Lara-González, S., Montero-Morán, G. M., Díaz-Gois, A., González de Mejia, E., et al. (2013). In vitro inhibition of dipeptidyl peptidase IV by peptides derived from the hydrolysis of amaranth (Amaranthus hypochondriacus L.) proteins. Food Chemistry, 136(2), 758-764.
    • (2013) Food Chemistry , vol.136 , Issue.2 , pp. 758-764
    • Velarde-Salcedo, A.J.1    Barrera-Pacheco, A.2    Lara-González, S.3    Montero-Morán, G.M.4    Díaz-Gois, A.5    González De Mejia, E.6


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