In silico methods to identify meat-derived prolyl endopeptidase inhibitors

Food Chemistry

Volumn 175, Issue , 2015, Pages 337-343

  Lafarga, Tomas ^a   O'Connor, Paula ^a   Hayes, Maria ^a  

^a TEAGASC   (Ireland)

Author keywords

Bioactive peptides; In silico; Meat by products; Meat proteins; Mental health; Prolyl endopeptidase

Indexed keywords

HEALTH; HEALTH RISKS; MEATS; NEURODEGENERATIVE DISEASES; NEUROLOGY;

BIOACTIVE PEPTIDES; IN-SILICO; MEAT BY-PRODUCTS; MEAT PROTEINS; MENTAL HEALTH; PROLYL ENDOPEPTIDASE;

PEPTIDES;

ANTIINFECTIVE AGENT; ANTIOXIDANT; COLLAGEN; DIPEPTIDYL CARBOXYPEPTIDASE; DIPEPTIDYL PEPTIDASE IV; HEMOGLOBIN; MYOSIN; PROLYL ENDOPEPTIDASE INHIBITOR; SERUM ALBUMIN; PROLYL ENDOPEPTIDASE; SERINE PROTEINASE; SERINE PROTEINASE INHIBITOR;

AMINO ACID SEQUENCE; ARTICLE; BIOAVAILABILITY; BLOOD BRAIN BARRIER; COMPUTER MODEL; CONTROLLED STUDY; IC50; IN VITRO STUDY; MEAT; MEAT INDUSTRY; MOLECULAR WEIGHT; NONHUMAN; PEPTIDE SYNTHESIS; PROTEIN ANALYSIS; REVERSED PHASE HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; ANALYSIS; ANIMAL; CHEMISTRY; HUMAN; MOLECULAR GENETICS;

AMINO ACID SEQUENCE; ANIMALS; HUMANS; MEAT; MOLECULAR SEQUENCE DATA; SERINE ENDOPEPTIDASES; SERINE PROTEINASE INHIBITORS;

EID: 84916608548     PISSN: 03088146     EISSN: 18737072     Source Type: Journal    
DOI: 10.1016/j.foodchem.2014.11.150     Document Type: Article

References (38)

1. Asano, M., Nio, N., & Ariyoshi, Y. (1992). Inhibition of prolyl endopeptidase by synthetic beta-casein peptides and their derivatives with a C-terminal prolinol or prolinal. Bioscience, Biotechnology, and Biochemistry, 56(6), 976-977.
2. Ashmarin, I. P., Karazeeva, E. P., Lyapina, L. A., & Samonina, G. E. (1998). The simplest proline-containing peptides PG, GP, PGP, and GPGG: Regulatory activity and possible sources of biosynthesis. Biochemistry (Moscow), 63(2), 119-124.
3. Boye, J. I., & Maltais, A. (2011). Pulses A novel protein source. Agro Food Industry Hi-Tech, 22(1), 24-26.
4. Cheng, L., Lumb, M., Polgár, L., & Mudge, A. W. (2005). How can the mood stabilizer VPA limit both mania and depression? Molecular and Cellular Neuroscience, 29(2), 155-161.
5. Cheung, H. S., Wang, F. L., Ondetti, M. A., Sabo, E. F., & Cushman, D. W. (1980). Binding of peptide substrates and inhibitors of angiotensin-converting enzyme. Importance of the COOH-terminal dipeptide sequence. Journal of Biological Chemistry, 255(2), 401-407.
6. Diaz, A. A., Tomba, E., Lennarson, R., Richard, R., Bagajewicz, M. J., & Harrison, R. G. (2010). Prediction of protein solubility in Escherichia coli using logistic regression. Biotechnology and Bioengineering, 105(2), 374-383.
7. Diemunsch, P., & Grelot, L. (2000). Potential of substance P antagonists as antiemetics. Drugs, 60 (3), 533-546.
8. European Food Safety Authority (EFSA) (2011). Scientific Opinion on the substantiation of a health claim related to isoleucyl-prolyl-proline (IPP) and valyl-prolyl-proline (VPP) and maintenance of normal blood pressure pursuant to Article 13(5) of Regulation (EC) No 1924/2006. EFSA Journal, 9(9), 2380-2398.
9. Fülöp, V., Böcskei, Z., & Polgár, L. (1998). Prolyl oligopeptidase: An unusual β-propeller domain regulates proteolysis. Cell, 94(2), 161-170.
10. Fülöp, V., Szeltner, Z., Renner, V., & Polgár, L. (2001). Structures of prolyl oligopeptidase substrate/inhibitor complexes: Use of inhibitor binding for titration of the catalytic histidine residue. Journal of Biological Chemistry, 276(2), 1262-1266.
11. García-Horsman, J. A., Männistö, P. T., & Venäläinen, J. I. (2007). On the role of prolyl oligopeptidase in health and disease. Neuropeptides, 41(1), 1-24.
12. Gasteiger, E., Gattiker, A., Hoogland, C., Ivanyi, I., Appel, R. D., & Bairoch, A. (2003). ExPASy: The proteomics server for in-depth protein knowledge and analysis. Nucleic Acids Research, 31(13), 3784-3788.
13. Graaf, C., Frewer, L., & Trijp, H. (2007). Sensory influences on food choice and food intake. Woodhead Publishing Ltd. (pp. 30-66). .
14. Gupta, S., Kapoor, P., Chaudhary, K., Gautam, A., Kumar, R., & Raghava, G. P. S. (2013). In silico approach for predicting toxicity of peptides and proteins. PLoS ONE, 8(9).
15. Häckel, M., Hinz, H. J., & Hedwig, G. R. (1999). Partial molar volumes of proteins: Amino acid side-chain contributions derived from the partial molar volumes of some tripeptides over the temperature range 10-90°C. Biophysical Chemistry, 82(1), 35-50.
16. Lafarga, T., & Hayes, M. (2014). Bioactive peptides from meat muscle and byproducts: Generation, functionality and application as functional ingredients. Meat Science, 98(2), 227-239.
17. Lafarga, T., O'Connor, P., & Hayes, M. (2014). Identification of novel dipeptidyl peptidase-IV and angiotensin-I-converting enzyme inhibitory peptides from meat proteins using in silico analysis. Peptides, 59, 53-62.
18. Lawandi, J., Gerber-Lemaire, S., Juillerat-Jeanneret, L., & Moitessier, N. (2010). Inhibitors of prolyl oligopeptidases for the therapy of human diseases: Defining diseases and inhibitors. Journal of Medicinal Chemistry, 53(9), 3423-3438.
19. López-Barrios, L., Gutiérrez-Uribe, J. A., & Serna-Saldívar, S. O. (2014). Bioactive peptides and hydrolysates from pulses and their potential use as functional ingredients. Journal of Food Science, 79(3), R273-R283.
20. Maruyama, S., Miyoshi, S., Osa, T., & Tanaka, H. (1992). Prolyl endopeptidase inhibitory activity of peptides in the repeated sequence of various proline-rich proteins. Journal of Fermentation and Bioengineering, 74(3), 145-148.
21. Maruyama, S., Ohmori, T., & Nakagami, T. (1996). Prolylendopeptidase inhibitory activity of a glial fibrillary acidic protein fragment and other proline-rich peptides. Bioscience, Biotechnology and Biochemistry, 60(2), 358-359.
22. Meethal, S. V., Smith, M. A., Bowen, R. L., & Atwood, C. S. (2005). The gonadotropin connection in Alzheimer's disease. Endocrine, 26(3), 317-325.
23. Minkiewicz, P., Dziuba, J., Iwaniak, A., Dziuba, M., & Darewicz, M. (2008). BIOPEP database and other programs for processing bioactive peptide sequences. Journal of AOAC International, 91(4), 965-980.
24. Mooney, C., Haslam, N. J., Pollastri, G., & Shields, D. C. (2012). Towards the improved discovery and design of functional peptides: Common features of diverse classes permit generalized prediction of bioactivity. PLoS ONE, 7(10), e45012.
25. Morain, P., Lestage, P., De Nanteuil, G., Jochemsen, R., Robin, J.-L., Guez, D., et al. (2002). S 17092: A prolyl endopeptidase inhibitor as a potential therapeutic drug for memory impairment. preclinical and clinical studies. CNS Drug Reviews, 8(1), 31-52.
26. Nongonierma, A. B., Mooney, C., Shields, D. C., & Fitzgerald, R. J. (2014). In silico approaches to predict the potential of milk protein-derived peptides as dipeptidyl peptidase IV (DPP-IV) inhibitors. Peptides, 57, 43-51.
27. Ohmori, T., Nakagami, T., Tanaka, H., & Maruyama, S. (1994). Isolation of prolylendopeptidase-inhibiting peptides from bovine brain. Biochemical and Biophysical Research Communications, 202 (2), 809-815.
28. Pardridge, W. M. (2012). Drug transport across the blood-brain barrier. Journal of Cerebral Blood Flow & Metabolism, 32(1), 1959-1972.
29. Pripp, A. H. (2006). Quantitative structure-activity relationship of prolyl oligopeptidase inhibitory peptides derived from b -casein using simple amino acid descriptors. Journal of Agricultural and Food Chemistry, 54(1), 224-228.
30. Rosenblum, J. S., & Kozarich, J. W. (2003). Prolyl peptidases: A serine protease subfamily with high potential for drug discovery. Current Opinion in Chemical Biology, 7(4), 496-504.
31. Sørensen, R., Kildal, E., Stepaniak, L., Pripp, A. H., & Sørhaug, T. (2004). Screening for peptides from fish and cheese inhibitory to prolyl endopeptidase. Nahrung-Food, 48(1), 53-56.
32. The UniProt Consortium (2012). Reorganizing the protein space at the Universal Protein Resource (UniProt). Nucleic Acids Research, 40(D1), D71-D75.
33. Wang, W., & Gonzalez De Mejia, E. (2005). A new frontier in soy bioactive peptides that may prevent age-related chronic diseases. Comprehensive Reviews in Food Science and Food Safety, 4(4), 63-78.
34. Weksler, B., Romero, I. A., & Couraud, P. O. (2013). The hCMEC/D3 cell line as a model of the human blood brain barrier. Fluids and Barriers of the CNS, 10(16), 1-10.
35. Wilson, J., Hayes, M., & Carney, B. (2011). Angiotensin-I-converting enzyme and prolyl endopeptidase inhibitory peptides from natural sources with a focus on marine processing by-products. Food Chemistry, 129 (2), 235-244.
36. WHO (2013), Mental Health: Action Plan 2013-2020. Geneva, Switzerland. 〈http://www.who.int/iris/handle/10665/89966〉 Accessed 23.10.2014, [2013, Page 7].
37. WHO (2004), Prevention of mental disorders: effective interventions and policy options. Geneva, Switzerland. 〈http://www.who.int/iris/handle/10665/43027〉 Accessed 23.10.2014, [2013, Page 13].
38. Zubrzycka, M., & Janecka, A. (2000). Substance P: Transmitter of nociception (minireview). Endocrine Regulations, 34(4), 195-201.