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Volumn 234, Issue , 2017, Pages 431-438

A study to evaluate the potential of an in silico approach for predicting dipeptidyl peptidase-IV inhibitory activity in vitro of protein hydrolysates

Author keywords

Correlation analysis; Dietary protein; Dipeptidyl peptidase IV inhibitor; In silico analysis

Indexed keywords

AMINO ACIDS; CORRELATION METHODS; HYDROLYSIS; PEPTIDES;

EID: 85019070138     PISSN: 03088146     EISSN: 18737072     Source Type: Journal    
DOI: 10.1016/j.foodchem.2017.05.035     Document Type: Article
Times cited : (41)

References (28)
  • 1
    • 0002510086 scopus 로고
    • Enzymatic hydrolysis of crayfish processing by-products
    • Beak, H.H., Cadwallader, K.R., Enzymatic hydrolysis of crayfish processing by-products. Journal of Food Science 60 (1995), 929–935.
    • (1995) Journal of Food Science , vol.60 , pp. 929-935
    • Beak, H.H.1    Cadwallader, K.R.2
  • 6
    • 33644842108 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV inhibitors: A promising new therapeutic approach for the management of type 2 diabetes
    • Deacon, C.F., Holst, J.J., Dipeptidyl peptidase IV inhibitors: A promising new therapeutic approach for the management of type 2 diabetes. The International Journal of Biochemistry & Cell Biology 38 (2006), 831–844.
    • (2006) The International Journal of Biochemistry & Cell Biology , vol.38 , pp. 831-844
    • Deacon, C.F.1    Holst, J.J.2
  • 7
    • 4244116877 scopus 로고    scopus 로고
    • Strightforward statistics for the behavioral sciences
    • Brooks/Cole Pacific Grove, CA
    • Evans, J.D., Strightforward statistics for the behavioral sciences. 1996, Brooks/Cole, Pacific Grove, CA.
    • (1996)
    • Evans, J.D.1
  • 8
    • 84871158996 scopus 로고    scopus 로고
    • Longer term safety of dipeptidyl peptidase-4 inhibitors in patients with type 2 diabetes mellitus: Systematic review and meta-analysis
    • Gooben, K., Gräber, S., Longer term safety of dipeptidyl peptidase-4 inhibitors in patients with type 2 diabetes mellitus: Systematic review and meta-analysis. Diabetes, Obesity & Metabolism 14 (2012), 1061–1072.
    • (2012) Diabetes, Obesity & Metabolism , vol.14 , pp. 1061-1072
    • Gooben, K.1    Gräber, S.2
  • 9
    • 15044354104 scopus 로고    scopus 로고
    • GIP and GLP-1 as incretin hormones: Lessons from single and double incretin receptor knockout mice
    • Hansotia, T., Drucker, D.J., GIP and GLP-1 as incretin hormones: Lessons from single and double incretin receptor knockout mice. Regulatory Peptides 128 (2005), 125–134.
    • (2005) Regulatory Peptides , vol.128 , pp. 125-134
    • Hansotia, T.1    Drucker, D.J.2
  • 10
    • 0031690479 scopus 로고    scopus 로고
    • Inhibition of the activity of dipeptidyl-peptidase IV as a treatment for type 2 diabetes
    • Holst, J.J., Deacon, C.F., Inhibition of the activity of dipeptidyl-peptidase IV as a treatment for type 2 diabetes. Diabetes 47 (1998), 1663–1670.
    • (1998) Diabetes , vol.47 , pp. 1663-1670
    • Holst, J.J.1    Deacon, C.F.2
  • 11
    • 84887132292 scopus 로고    scopus 로고
    • Bioinformatics: current perspectives and future directions for food and nutritional research facilitated by a Food-Wiki database
    • Holton, T.A., Vijayakumar, V., Khaldi, N., Bioinformatics: current perspectives and future directions for food and nutritional research facilitated by a Food-Wiki database. Trends in Food Science & Technology 34 (2013), 5–17.
    • (2013) Trends in Food Science & Technology , vol.34 , pp. 5-17
    • Holton, T.A.1    Vijayakumar, V.2    Khaldi, N.3
  • 12
    • 84959370147 scopus 로고    scopus 로고
    • In silico, in vitro and in vivo analyses of dipeptidyl peptidase IV inhibitory activity and the antidiabetic effect of sodium caseinate hydrolysate
    • Hsieh, C.H., Wang, T.Y., Hung, C.C., Jao, C.L., Hsieh, Y.L., Wu, S.X., Hsu, K.C., In silico, in vitro and in vivo analyses of dipeptidyl peptidase IV inhibitory activity and the antidiabetic effect of sodium caseinate hydrolysate. Food & Function 7 (2016), 1122–1128.
    • (2016) Food & Function , vol.7 , pp. 1122-1128
    • Hsieh, C.H.1    Wang, T.Y.2    Hung, C.C.3    Jao, C.L.4    Hsieh, Y.L.5    Wu, S.X.6    Hsu, K.C.7
  • 13
    • 84926315093 scopus 로고    scopus 로고
    • Porcine skin gelatin hydrolysate as a dipeptidyl peptidase IV inhibitor improves glycemic control in streptozotocin-induced diabetic rats
    • Huang, S.L., Hung, C.C., Jao, C.L., Tung, Y.S., Hsu, K.C., Porcine skin gelatin hydrolysate as a dipeptidyl peptidase IV inhibitor improves glycemic control in streptozotocin-induced diabetic rats. Journal of Functional Foods 11 (2014), 235–242.
    • (2014) Journal of Functional Foods , vol.11 , pp. 235-242
    • Huang, S.L.1    Hung, C.C.2    Jao, C.L.3    Tung, Y.S.4    Hsu, K.C.5
  • 14
    • 84942524542 scopus 로고    scopus 로고
    • Screening and identification of DPP-IV inhibitory peptides from deer skin hydrolysates by an integrated approach of LC-MS/MS and in silico analysis
    • Jin, Y., Yan, J., Yu, Y., Qi, Y., Screening and identification of DPP-IV inhibitory peptides from deer skin hydrolysates by an integrated approach of LC-MS/MS and in silico analysis. Journal of Functional Foods 18 (2015), 344–357.
    • (2015) Journal of Functional Foods , vol.18 , pp. 344-357
    • Jin, Y.1    Yan, J.2    Yu, Y.3    Qi, Y.4
  • 15
    • 0018836136 scopus 로고
    • Rapid chromatographic purification of dipeptidyl peptidase IV in human submaxillary gland
    • Kojima, K., Ham, T., Kato, T., Rapid chromatographic purification of dipeptidyl peptidase IV in human submaxillary gland. Journal of Chromatography A 189 (1980), 233–240.
    • (1980) Journal of Chromatography A , vol.189 , pp. 233-240
    • Kojima, K.1    Ham, T.2    Kato, T.3
  • 16
    • 84905197278 scopus 로고    scopus 로고
    • Identification of novel dipeptidyl peptidase-IV and angiotensin-I-converting enzyme inhibitory peptides from meat proteins using in silico analysis
    • Lafarga, T., O'Connor, P., Hayes, M., Identification of novel dipeptidyl peptidase-IV and angiotensin-I-converting enzyme inhibitory peptides from meat proteins using in silico analysis. Peptides 59 (2014), 53–62.
    • (2014) Peptides , vol.59 , pp. 53-62
    • Lafarga, T.1    O'Connor, P.2    Hayes, M.3
  • 17
    • 84861332110 scopus 로고    scopus 로고
    • Dipeptidyl peptidase-IV inhibitory activity of dairy protein hydrolysates
    • Lacroix, I.M.E., Li-Chan, E.C.Y., Dipeptidyl peptidase-IV inhibitory activity of dairy protein hydrolysates. International Dairy Journal 25 (2012), 97–102.
    • (2012) International Dairy Journal , vol.25 , pp. 97-102
    • Lacroix, I.M.E.1    Li-Chan, E.C.Y.2
  • 18
    • 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., 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 (2012), 403–422.
    • (2012) Journal of Functional Foods , vol.4 , pp. 403-422
    • Lacroix, I.M.E.1    Li-Chan, E.C.Y.2
  • 19
    • 0035798196 scopus 로고    scopus 로고
    • Kinetic study of the processing by dipeptidyl-peptidase IV/CD26 of neuropeptides involved in pancreatic insulin secretion
    • Lambeir, A.M., 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 Letters 507 (2001), 327–330.
    • (2001) FEBS Letters , vol.507 , pp. 327-330
    • Lambeir, A.M.1    Durinx, C.2    Proost, P.3    Van Damme, J.4    Scharpe, S.5    De Meester, I.6
  • 22
    • 84903131059 scopus 로고    scopus 로고
    • An in silico model to predict the potential of dietary proteins as sources of dipeptidyl peptidase IV (DPP-IV) inhibitory peptides
    • Nongonierma, A.B., FitzGerald, R.J., An in silico model to predict the potential of dietary proteins as sources of dipeptidyl peptidase IV (DPP-IV) inhibitory peptides. Food Chemistry 165 (2014), 489–498.
    • (2014) Food Chemistry , vol.165 , pp. 489-498
    • Nongonierma, A.B.1    FitzGerald, R.J.2
  • 23
    • 84901310564 scopus 로고    scopus 로고
    • In silico approaches to predict the potential of milk protein-derived peptides as dipeptidyl peptidase IV (DPP-IV) inhibitors
    • Nongonierma, A.B., Mooney, C., Shields, D.C., FitzGerald, R.J., In silico approaches to predict the potential of milk protein-derived peptides as dipeptidyl peptidase IV (DPP-IV) inhibitors. Peptides 57 (2014), 43–51.
    • (2014) Peptides , vol.57 , pp. 43-51
    • Nongonierma, A.B.1    Mooney, C.2    Shields, D.C.3    FitzGerald, R.J.4
  • 24
    • 84893917196 scopus 로고    scopus 로고
    • Food protein hydrolysates as a source of dipeptidyl peptidase IV inhibitory peptides for the management of type 2 diabetes
    • Power, O., Nongonierma, A.B., Jakeman, P., FitzGerald, R.J., Food protein hydrolysates as a source of dipeptidyl peptidase IV inhibitory peptides for the management of type 2 diabetes. Proceedings of the Nutrition Society 73 (2014), 34–46.
    • (2014) Proceedings of the Nutrition Society , vol.73 , pp. 34-46
    • Power, O.1    Nongonierma, A.B.2    Jakeman, P.3    FitzGerald, R.J.4
  • 26
    • 84887112623 scopus 로고    scopus 로고
    • In silico analysis of the large and small subunits of cereal RuBisCO as precursors of cryptic bioactive peptides
    • Udenigwe, C.C., Gong, M., Wu, S., In silico analysis of the large and small subunits of cereal RuBisCO as precursors of cryptic bioactive peptides. Process Biochemistry 48 (2013), 1794–1799.
    • (2013) Process Biochemistry , vol.48 , pp. 1794-1799
    • Udenigwe, C.C.1    Gong, M.2    Wu, S.3
  • 27
    • 84875393233 scopus 로고    scopus 로고
    • Is the structural diversity of tripeptides sufficient for developing functional food additives with satisfactory multiple bioactivities?
    • Wang, J.H., Liu, Y.L., Ning, J.H., Yu, J., Li, X.H., Wang, F.X., Is the structural diversity of tripeptides sufficient for developing functional food additives with satisfactory multiple bioactivities?. Journal of Molecular Structure 1040 (2013), 164–170.
    • (2013) Journal of Molecular Structure , vol.1040 , pp. 164-170
    • Wang, J.H.1    Liu, Y.L.2    Ning, J.H.3    Yu, J.4    Li, X.H.5    Wang, F.X.6
  • 28
    • 84879468389 scopus 로고    scopus 로고
    • What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach
    • Zhou, P., Yang, C., Ren, Y., Wang, C., Tian, F., What are the ideal properties for functional food peptides with antihypertensive effect? A computational peptidology approach. Food Chemistry 141 (2013), 2967–2973.
    • (2013) Food Chemistry , vol.141 , pp. 2967-2973
    • Zhou, P.1    Yang, C.2    Ren, Y.3    Wang, C.4    Tian, F.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.