Sequence analysis and molecular docking of antithrombotic peptides from casein hydrolysate by trypsin digestion

Journal of Functional Foods

Volumn 32, Issue , 2017, Pages 313-323

  Tu, Maolin ^a   Feng, Liting ^a   Wang, Zhenyu ^b   Qiao, Meiling ^b   Shahidi, Fereidoon ^c   Lu, Weihong ^a   Du, Ming ^b  

^a HARBIN INSTITUTE OF TECHNOLOGY   (China)

^b DALIAN POLYTECHNIC UNIVERSITY   (China)

^c MEMORIAL UNIVERSITY OF NEWFOUNDLAND   (Canada)

Author keywords

Casein; Hydrolysis; Molecular docking; Screening; Thrombin inhibitory activity

Indexed keywords

EID: 85014991198     PISSN: 17564646     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jff.2017.03.015     Document Type: Article

References (40)

1. Bode, W., Structure and interaction modes of thrombin. Blood Cells, Molecules, and Diseases 36:2 (2006), 122–130.
2. Cappello, M., Bergum, P.W., Vlasuk, G.P., Furmidge, B.A., Pritchard, D.I., Aksoy, S., Isolation and characterization of the tsetse thrombin inhibitor: A potent antithrombotic peptide from the saliva of Glossina morsitans morsitans. American Journal of Tropical Medicine and Hygiene 54:5 (1996), 475–480.
3. Capriotti, A.L., Cavaliere, C., Piovesana, S., Samperi, R., Laganà, A., Recent trends in the analysis of bioactive peptides in milk and dairy products. Analytical and Bioanalytical Chemistry, 2016, 1–9.
4. Cheung, I.W.Y., Nakayama, S., Hsu, M.N.K., Samaranayaka, A.G.P., Li-Chan, E.C.Y., Angiotensim-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 57:19 (2009), 9234–9242.
5. Corral-Rodríguez, M.Á., Bock, P.E., Hernández-Carvajal, E., Gutiérrez-Gallego, R., Fuentes-Prior, P., Structural basis of thrombin-mediated factor V activation: The Glu 666-Glu672 sequence is critical for processing at the heavy chain - B domain junction. Blood 117:26 (2011), 7164–7173.
6. Davie, E.W., Fujikawa, K., Kisiel, W., The coagulation cascade: Initiation, maintenance, and regulation. Biochemistry 30:43 (1991), 10363–10370.
7. Du, M., Zhao, L., Li, C., Zhao, G., Hu, X., Purification and characterization of a novel fungi Se-containing protein from Se-enriched Ganoderma Lucidum mushroom and its Se-dependent radical scavenging activity. European Food Research and Technology 224:5 (2007), 659–665.
8. Dziuba, J., Iwaniak, A., Mine, Y., Shahidi, F., Database of protein and bioactive peptide sequences Nutraceutical proteins and peptides in health and disease, 2006, CRC Press, 543–563.
9. Field, K.L., Kimball, B.A., Mennella, J.A., Beauchamp, G.K., Bachmanov, A.A., Avoidance of hydrolyzed casein by mice. Physiology and Behavior 93:1–2 (2008), 189–199.
10. Furie, B., Furie, B.C., The molecular basis of blood coagulation. Cell 53:4 (1988), 505–518.
11. Jollès, P., Lévy-Toledano, S., Fiat, A.M., Soria, C., Gillessen, D., Thomaidis, A.,.. Caen, J.P., Analogy between fibrinogen and casein. Effect of an undecapeptide isolated from kappa-casein on platelet function. European Journal of Biochemistry/FEBS 158:2 (1986), 379–382.
12. Jung, W.K., Kim, S.K., Isolation and characterisation of an anticoagulant oligopeptide from blue mussel, Mytilus edulis. Food Chemistry 117:4 (2009), 687–692.
13. Kikelj, D., Peptidomimetic thrombin inhibitors. Pathophysiology of Haemostasis and Thrombosis 33:5–6 (2003), 487–491.
14. Ko, J.Y., Kang, N., Lee, J.H., Kim, J.S., Kim, W.S., Park, S.J.,.. Jeon, Y.J., Angiotensin I-converting enzyme inhibitory peptides from an enzymatic hydrolysate of flounder fish (Paralichthys olivaceus) muscle as a potent anti-hypertensive agent. Process Biochemistry 51:4 (2016), 535–541.
15. Koh, C.Y., Kumar, S., Kazimirova, M., Nuttall, P.A., Radhakrishnan, U.P., Kim, S.,.. Kini, R.M., Crystal structure of thrombin in complex with s-variegin: Insights of a novel mechanism of inhibition and design of tunable thrombin inhibitors. PLoS ONE, 6(10), 2011.
16. Kong, Y., Huang, S.L., Shao, Y., Li, S., Wei, J.F., Purification and characterization of a novel antithrombotic peptide from Scolopendra subspinipes mutilans. Journal of Ethnopharmacology 145:1 (2013), 182–186.
17. Korhonen, H., Pihlanto, A., Bioactive peptides: Production and functionality. International Dairy Journal 16:9 (2006), 945–960.
18. Linusson, A., Gottfries, J., Olsson, T., Örnskov, E., Folestad, S., Nordén, B., Wold, S., Statistical molecular design, parallel synthesis, and biological evaluation of a library of thrombin inhibitors. Journal of Medicinal Chemistry 44:21 (2001), 3424–3439.
19. Liu, F., Baggerman, G., D'Hertog, W., Verleyen, P., Schoofs, L., Wets, G., In silico identification of new secretory peptide genes in drosophila melanogaster. Molecular & Cellular Proteomics 5:3 (2006), 510–522.
20. Luchtman-Jones, L., Broze, G.J., The current status of coagulation. Annals of Medicine 27 (2009), 47–52.
21. Mannucci, E., Rotella, C.M., Future perspectives on glucagon-like peptide-1, diabetes and cardiovascular risk. Nutrition, Metabolism and Cardiovascular Diseases 18:9 (2008), 639–645.
22. Minkiewicz, P., Dziuba, J., Food peptidomics‏. Food Technology and Biotechnology 46:1 (2008), 1–10.
23. Minkiewicz, P., Dziuba, J., Iwaniak, A., Dziuba, M., Darewicz, M., BIOPEP database and other programs for processing bioactive peptide sequences. Journal of AOAC International 91:4 (2008), 965–980.
24. 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 17:1 (2011), 39–45.
25. Mohanty, D.P., Mohapatra, S., Misra, S., Sahu, P.S., Milk derived bioactive peptides and their impact on human health - A review. Saudi Journal of Biological Sciences 23:5 (2016), 577–583.
26. Neumann, T., Junker, H.-D., Keil, O., Burkert, K., Ottleben, H., Gamer, J.,.. Metz, G., Discovery of thrombin inhibitor fragments from chemical microarray screening. Letters in Drug Design & Discovery 2:8 (2005), 590–594.
27. Nilsson, M., Hämäläinen, M., Ivarsson, M., Gottfries, J., Xue, Y., Hansson, S.,.. Fex, T., Compounds binding to the S2–S3 pockets of thrombin. Journal of Medicinal Chemistry 52:9 (2009), 2708–2715.
28. Rawendra, R.D., Chang, C.I., Chen, H.H., Huang, T.C., Hsu, J.L., A novel angiotensin converting enzyme inhibitory peptide derived from proteolytic digest of Chinese soft-shelled turtle egg white proteins. Journal of Proteomics 94 (2013), 359–369.
29. Rojas-Ronquillo, R., Cruz-Guerrero, A., Flores-Nájera, A., Rodríguez-Serrano, G., Gómez-Ruiz, L., Reyes-Grajeda, J.P.,.. García-Garibay, M., Antithrombotic and angiotensin-converting enzyme inhibitory properties of peptides released from bovine casein by Lactobacillus casei Shirota. International Dairy Journal 26:2 (2012), 147–154.
30. Sabbione, A.C., Nardo, A.E., Añón, M.C., Scilingo, A., Amaranth peptides with antithrombotic activity released by simulated gastrointestinal digestion. Journal of Functional Foods 20 (2016), 204–214.
31. Shahidi, F., Zhong, Y., Bioactive peptides. Journal of AOAC International 91 (2008), 914–931.
32. Taufer, M., Crowley, M., Price, D.J., Chien, a.a., Brooks, C.L., Study of a highly accurate and fast protein-ligand docking method based on molecular dynamics. Concurrency and Computation: Practice and Experience 17 (2005), 1627–1641.
33. Udenigwe, C.C., Bioinformatics approaches, prospects and challenges of food bioactive peptide research. Trends in Food Science and Technology 36:2 (2014), 137–143.
34. UniProt Consortium, Reorganizing the protein space at the Universal Protein Resource (UniProt). Nucleic Acids Research 40 (2011), D1–D75.
35. van de Locht, a., Stubbs, M.T., Bode, W., Friedrich, T., Bollschweiler, C., Höffken, W., Huber, R., The ornithodorin-thrombin crystal structure, a key to the TAP enigma?. The EMBO Journal 15:22 (1996), 6011–6017.
36. Vercruysse, L., Smagghe, G., van der Bent, A., van Amerongen, A., Ongenaert, M., Van Camp, J., Critical evaluation of the use of bioinformatics as a theoretical tool to find high-potential sources of ACE inhibitory peptides. Peptides 30:3 (2009), 575–582.
37. Wu, G., Robertson, D.H., Brooks, C.L., Vieth, M., Detailed analysis of grid-based molecular docking: A case study of CDOCKER - A CHARMm-based MD docking algorithm. Journal of Computational Chemistry 24:13 (2003), 1549–1562.
38. Xu, H.J., Hao, Y.B., Qi, J.X., Fan, G.S., Wang, K.J., Study on antioxidant activity and antihypertensive activity of enzymatic hydrolysis products of walnut protein. Innovational Edition of Farm Products Processing 10 (2009), 38–42.
39. Yang, W.G., Wang, Z., Xu, S.Y., A new method for determination of antithrombotic activity of egg white protein hydrolysate by microplate reader. Chinese Chemical Letters 18:4 (2007), 449–451.
40. Zhang, S.B., In vitro antithrombotic activities of peanut protein hydrolysates. Food Chemistry 202 (2016), 1–8.