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Volumn 4, Issue 2, 2012, Pages 403-422

Evaluation of the potential of dietary proteins as precursors of dipeptidyl peptidase (DPP)-IV inhibitors by an in silico approach

Author keywords

Bioactive peptide; Dietary protein; Dipeptidyl peptidase (DPP) IV Inhibitor; In silico analysis

Indexed keywords

BOVINAE;

EID: 84860318855     PISSN: 17564646     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jff.2012.01.008     Document Type: Article
Times cited : (197)

References (38)
  • 1
    • 0023875034 scopus 로고
    • A collagen-binding glycoprotein on the surface of mouse fibroblasts is identified as dipeptidyl peptidase IV
    • Bauvois B. A collagen-binding glycoprotein on the surface of mouse fibroblasts is identified as dipeptidyl peptidase IV. Biochemical Journal 1988, 252:723-731.
    • (1988) Biochemical Journal , vol.252 , pp. 723-731
    • Bauvois, B.1
  • 2
    • 0020441144 scopus 로고
    • Rat intestinal brush border membrane dipeptidyl-aminopeptidase IV: kinetic properties and substrate specificities of the purified enzyme
    • Bella A.M., Erickson R.H., Kim Y.S. Rat intestinal brush border membrane dipeptidyl-aminopeptidase IV: kinetic properties and substrate specificities of the purified enzyme. Archives of Biochemistry and Biophysics 1982, 218:156-162.
    • (1982) Archives of Biochemistry and Biophysics , vol.218 , pp. 156-162
    • Bella, A.M.1    Erickson, R.H.2    Kim, Y.S.3
  • 4
    • 70349931376 scopus 로고    scopus 로고
    • Angiotensin-I converting enzyme inhibitory activity of hydrolysates from oat (Avena sativa) proteins by in silico and in vitro analyses
    • Cheung I.W.Y., Nakayama S., Hsu M.N.K., Samaranayaka A.G.P., Li-Chan E.C.Y. Angiotensin-I converting enzyme inhibitory activity of hydrolysates from oat (Avena sativa) proteins by in silico and in vitro analyses. Journal of Agricultural and Food Chemistry 2009, 57:9234-9242.
    • (2009) Journal of Agricultural and Food Chemistry , vol.57 , pp. 9234-9242
    • Cheung, I.W.Y.1    Nakayama, S.2    Hsu, M.N.K.3    Samaranayaka, A.G.P.4    Li-Chan, E.C.Y.5
  • 5
    • 36749005569 scopus 로고    scopus 로고
    • Optimizing angiotensin I-converting enzyme inhibitory activity of Pacific hake (Merluccius productus) fillet hydrolysate using response surface methodology and ultrafiltration
    • Cinq-Mars C.D., Li-Chan E.C.Y. Optimizing angiotensin I-converting enzyme inhibitory activity of Pacific hake (Merluccius productus) fillet hydrolysate using response surface methodology and ultrafiltration. Journal of Agricultural and Food Chemistry 2007, 55:9380-9388.
    • (2007) Journal of Agricultural and Food Chemistry , vol.55 , pp. 9380-9388
    • Cinq-Mars, C.D.1    Li-Chan, E.C.Y.2
  • 7
    • 1342265511 scopus 로고    scopus 로고
    • Hemorphins: substrates and/or inhibitors of dipeptidyl peptidase IV. Hemorphins N-terminus sequence influence on the interaction between hemorphins and DPPIV
    • Cohen M., Fruitier-Arnaudin I., Piot J.M. Hemorphins: substrates and/or inhibitors of dipeptidyl peptidase IV. Hemorphins N-terminus sequence influence on the interaction between hemorphins and DPPIV. Biochimie 2004, 86:31-37.
    • (2004) Biochimie , vol.86 , pp. 31-37
    • Cohen, M.1    Fruitier-Arnaudin, I.2    Piot, J.M.3
  • 10
    • 0037216795 scopus 로고    scopus 로고
    • Computer-aided characteristics of proteins as potential precursors of bioactive peptides
    • Dziuba J., Iwaniak A., Minkiewicz P. Computer-aided characteristics of proteins as potential precursors of bioactive peptides. Polimery 2003, 48:50-53.
    • (2003) Polimery , vol.48 , pp. 50-53
    • Dziuba, J.1    Iwaniak, A.2    Minkiewicz, P.3
  • 12
    • 80051558901 scopus 로고    scopus 로고
    • QSAR-aided in silico approach in evaluation of food proteins as precursors of ACE inhibitory peptides
    • Gu Y., Majumder K., Wu J. QSAR-aided in silico approach in evaluation of food proteins as precursors of ACE inhibitory peptides. Food Research International 2011, 44:2465-2474.
    • (2011) Food Research International , vol.44 , pp. 2465-2474
    • Gu, Y.1    Majumder, K.2    Wu, J.3
  • 13
    • 58249134379 scopus 로고    scopus 로고
    • Optimisation of hydrolysis conditions for the production of the angiotensin-I converting enzyme (ACE) inhibitory peptides from whey protein using response surface methodology
    • Guo Y., Pan D., Tanokura M. Optimisation of hydrolysis conditions for the production of the angiotensin-I converting enzyme (ACE) inhibitory peptides from whey protein using response surface methodology. Food Chemistry 2009, 114:328-333.
    • (2009) Food Chemistry , vol.114 , pp. 328-333
    • Guo, Y.1    Pan, D.2    Tanokura, M.3
  • 14
    • 0022377281 scopus 로고
    • Involvement of plasma membrane dipeptidyl peptidase IV in fibronectin-mediated adhesion of cells on collagen
    • Hanski C., Huhle T., Reutter W. Involvement of plasma membrane dipeptidyl peptidase IV in fibronectin-mediated adhesion of cells on collagen. Biological Chemistry Hoppe-Seyler 1985, 366:1169-1176.
    • (1985) Biological Chemistry Hoppe-Seyler , vol.366 , pp. 1169-1176
    • Hanski, C.1    Huhle, T.2    Reutter, W.3
  • 15
    • 0020491867 scopus 로고
    • Inhibitory action of proline-containing peptides on Xaa-Pro-dipeptidylaminopeptidase
    • Harada M., Fukasawa K.M., Fukasawa K., Nagatsu T. Inhibitory action of proline-containing peptides on Xaa-Pro-dipeptidylaminopeptidase. Biochimica et Biophysica Acta 1982, 705:288-290.
    • (1982) Biochimica et Biophysica Acta , vol.705 , pp. 288-290
    • Harada, M.1    Fukasawa, K.M.2    Fukasawa, K.3    Nagatsu, T.4
  • 16
    • 14044264798 scopus 로고    scopus 로고
    • Glucagon-like peptide 1 and inhibitors of dipeptidyl peptidase IV in the treatment of type 2 diabetes mellitus
    • Holst J.J., Deacon C.F. Glucagon-like peptide 1 and inhibitors of dipeptidyl peptidase IV in the treatment of type 2 diabetes mellitus. Current Opinion in Pharmacology 2004, 4:589-596.
    • (2004) Current Opinion in Pharmacology , vol.4 , pp. 589-596
    • Holst, J.J.1    Deacon, C.F.2
  • 17
    • 33644892053 scopus 로고    scopus 로고
    • Inhibitors of dipeptidyl peptidase IV - Recent advances and structural views
    • Hunziker D., Henning M., Peters J.U. Inhibitors of dipeptidyl peptidase IV - Recent advances and structural views. Current Topics in Medicinal Chemistry 2005, 5:1623-1637.
    • (2005) Current Topics in Medicinal Chemistry , vol.5 , pp. 1623-1637
    • Hunziker, D.1    Henning, M.2    Peters, J.U.3
  • 20
    • 0037787851 scopus 로고    scopus 로고
    • Dipeptidyl-peptidase IV from bench to bedside: an update on structural properties, functions, and clinical aspects of the enzyme DPP IV
    • Lambeir A.-M., Durinx C., Scharpé S., De Meester I. Dipeptidyl-peptidase IV from bench to bedside: an update on structural properties, functions, and clinical aspects of the enzyme DPP IV. Critical Reviews in Clinical Laboratory Sciences 2003, 40:209-294.
    • (2003) Critical Reviews in Clinical Laboratory Sciences , vol.40 , pp. 209-294
    • Lambeir, A.-M.1    Durinx, C.2    Scharpé, S.3    De Meester, I.4
  • 21
    • 0038531163 scopus 로고    scopus 로고
    • Different modes of dipeptidyl peptidase IV (CD26) inhibition by oligopeptides derived from the N-terminus of HIV-1 Tat indicate at least two inhibitor binding sites
    • Lorey S., Stöckel-Maschek A., Faust J., Brandt W., Stiebitz B., Gorrell M.D., et al. Different modes of dipeptidyl peptidase IV (CD26) inhibition by oligopeptides derived from the N-terminus of HIV-1 Tat indicate at least two inhibitor binding sites. European Journal of Biochemistry 2003, 270:2147-2156.
    • (2003) European Journal of Biochemistry , vol.270 , pp. 2147-2156
    • Lorey, S.1    Stöckel-Maschek, A.2    Faust, J.3    Brandt, W.4    Stiebitz, B.5    Gorrell, M.D.6
  • 22
    • 0030073021 scopus 로고    scopus 로고
    • Prolylendopeptidase inhibitory activity of a glial fibrillary acidic protein fragment and other proline-rich peptides
    • Maruyama S., Ohmori T., Nakagami T. Prolylendopeptidase inhibitory activity of a glial fibrillary acidic protein fragment and other proline-rich peptides. Bioscience Biotechnology and Biochemistry 1996, 60:358-359.
    • (1996) Bioscience Biotechnology and Biochemistry , vol.60 , pp. 358-359
    • Maruyama, S.1    Ohmori, T.2    Nakagami, T.3
  • 23
    • 33645501006 scopus 로고    scopus 로고
    • New insights in biologically active proteins and peptides derived from hen egg
    • Mine Y., Kovacs-Nolan J. New insights in biologically active proteins and peptides derived from hen egg. World's Poultry Science Journal 2006, 62:87-96.
    • (2006) World's Poultry Science Journal , vol.62 , pp. 87-96
    • Mine, Y.1    Kovacs-Nolan, J.2
  • 24
    • 79952353155 scopus 로고    scopus 로고
    • Bovine meat proteins as potential precursors of biologically active peptides - a computational study based on the BIOPEP database
    • 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 Science and Technology International 2011, 17:39-45.
    • (2011) Food Science and Technology International , vol.17 , pp. 39-45
    • Minkiewicz, P.1    Dziuba, J.2    Michalska, J.3
  • 25
    • 59649100770 scopus 로고    scopus 로고
    • Comparison of ACE inhibitory and DPPH radical scavenging activities of fish muscle hydrolysates
    • Nakajima K., Yoshie-Stark Y., Ogushi M. Comparison of ACE inhibitory and DPPH radical scavenging activities of fish muscle hydrolysates. Food Chemistry 2009, 114:844-851.
    • (2009) Food Chemistry , vol.114 , pp. 844-851
    • Nakajima, K.1    Yoshie-Stark, Y.2    Ogushi, M.3
  • 26
    • 34548484135 scopus 로고    scopus 로고
    • Fractionation and identification of ACE-inhibitory peptides from α-lactalbumin and β-casein produced by thermolysin-catalysed hydrolysis
    • Otte J., Shalaby S.M.A., Zakora M., Nielsen M.S. Fractionation and identification of ACE-inhibitory peptides from α-lactalbumin and β-casein produced by thermolysin-catalysed hydrolysis. International Dairy Journal 2007, 17:1460-1472.
    • (2007) International Dairy Journal , vol.17 , pp. 1460-1472
    • Otte, J.1    Shalaby, S.M.A.2    Zakora, M.3    Nielsen, M.S.4
  • 27
    • 0024436374 scopus 로고
    • Evidence for the role of dipeptidyl peptidase IV in fibronectin-mediated interactions of hepatocytes with extracellular matrix
    • Piazza G.A., Callanan H.M., Mowery J., Hixson D.C. Evidence for the role of dipeptidyl peptidase IV in fibronectin-mediated interactions of hepatocytes with extracellular matrix. Biochemical Journal 1989, 262:327-334.
    • (1989) Biochemical Journal , vol.262 , pp. 327-334
    • Piazza, G.A.1    Callanan, H.M.2    Mowery, J.3    Hixson, D.C.4
  • 28
    • 0025976294 scopus 로고
    • Are diprotin A (Ile-Pro-Ile) and diprotin B (Val-Pro-Leu) inhibitors or substrates of dipeptidyl peptidase IV?
    • Rahfeld J., Schierborn M., Hartrodt B., Neubert K., Heins J. Are diprotin A (Ile-Pro-Ile) and diprotin B (Val-Pro-Leu) inhibitors or substrates of dipeptidyl peptidase IV?. Biochimica et Biophysica Acta 1991, 1076:314-316.
    • (1991) Biochimica et Biophysica Acta , vol.1076 , pp. 314-316
    • Rahfeld, J.1    Schierborn, M.2    Hartrodt, B.3    Neubert, K.4    Heins, J.5
  • 29
    • 33947672273 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV inhibitors: the next generation of new promising therapies for the management of type 2 diabetes
    • Sebokova E., Christ A.D., Boehringer M., Mizrahi J. Dipeptidyl peptidase IV inhibitors: the next generation of new promising therapies for the management of type 2 diabetes. Current Topics in Medicinal Chemistry 2007, 7:547-555.
    • (2007) Current Topics in Medicinal Chemistry , vol.7 , pp. 547-555
    • Sebokova, E.1    Christ, A.D.2    Boehringer, M.3    Mizrahi, J.4
  • 32
    • 0042131827 scopus 로고    scopus 로고
    • Structural basis of proline-specific exopeptidase activity as observed in human dipeptidyl peptidase-IV
    • Thoma R., Löffler B., Stihle M., Huber W., Ruf A., Hennig M. Structural basis of proline-specific exopeptidase activity as observed in human dipeptidyl peptidase-IV. Structure 2003, 11:947-959.
    • (2003) Structure , vol.11 , pp. 947-959
    • Thoma, R.1    Löffler, B.2    Stihle, M.3    Huber, W.4    Ruf, A.5    Hennig, M.6
  • 33
    • 79952799368 scopus 로고    scopus 로고
    • Whey proteins as source of dipeptidyl dipeptidase IV (dipeptidyl peptidase-4) inhibitors
    • Tulipano G., Sibilia V., Caroli A.M., Cocchi D. Whey proteins as source of dipeptidyl dipeptidase IV (dipeptidyl peptidase-4) inhibitors. Peptides 2011, 32:835-838.
    • (2011) Peptides , vol.32 , pp. 835-838
    • Tulipano, G.1    Sibilia, V.2    Caroli, A.M.3    Cocchi, D.4
  • 34
    • 80052897910 scopus 로고    scopus 로고
    • Novel dipeptidyl peptidase-4-inhibiting peptide derived from β-lactoglobulin
    • Uchida M., Ohshiba Y., Mogami O. Novel dipeptidyl peptidase-4-inhibiting peptide derived from β-lactoglobulin. Journal of Pharmacological Sciences 2011, 117:63-66.
    • (2011) Journal of Pharmacological Sciences , vol.117 , pp. 63-66
    • Uchida, M.1    Ohshiba, Y.2    Mogami, O.3
  • 36
    • 2342466734 scopus 로고    scopus 로고
    • Global prevalence of diabetes estimates from the year 2000 and projections for 2030
    • Wild S., Roglic G., Green A., Sicree R., King H. Global prevalence of diabetes estimates from the year 2000 and projections for 2030. Diabetes Care 2004, 27:1047-1053.
    • (2004) Diabetes Care , vol.27 , pp. 1047-1053
    • Wild, S.1    Roglic, G.2    Green, A.3    Sicree, R.4    King, H.5
  • 37
    • 0026858424 scopus 로고
    • Catalytic properties of X-prolyl dipeptidyl aminopeptidase from Lactococcus lactis subsp. cremoris nTR
    • Yan T.-R., Ho S.-C., Hou C.-L. Catalytic properties of X-prolyl dipeptidyl aminopeptidase from Lactococcus lactis subsp. cremoris nTR. Bioscience Biotechnology and Biochemistry 1992, 56:704-707.
    • (1992) Bioscience Biotechnology and Biochemistry , vol.56 , pp. 704-707
    • Yan, T.-R.1    Ho, S.-C.2    Hou, C.-L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.