A multidisciplinary investigation on the bioavailability and activity of peptides from lupin protein

Journal of Functional Foods

Volumn 24, Issue , 2016, Pages 297-306

  Lammi, Carmen ^a   Aiello, Gilda ^a   Vistoli, Giulio ^a   Zanoni, Chiara ^b   Arnoldi, Anna ^a   Sambuy, Yula ^c   Ferruzza, Simonetta ^c   Ranaldi, Giulia ^c  

^a UNIVERSITY OF MILAN   (Italy)

^b OSPEDALE NIGUARDA CA GRANDA   (Italy)

^c CREA   (Italy)

Author keywords

Bioactive peptides; Caco 2 cells; HMGCoA reductase; Intestinal absorption; Lupinus albus; Plant protein

Indexed keywords

EID: 84973151746     PISSN: 17564646     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jff.2016.04.017     Document Type: Article

References (40)

1. Amigo-Benavent M., Clemente A., Caira S., Stiuso P., Ferranti P., del Castillo M.D. Use of phytochemomics to evaluate the bioavailability and bioactivity of antioxidant peptides of soybean β-conglycinin. Electrophoresis 2014, 35(11):1582-1589.
2. Arnoldi A., Boschin G., Zanoni C., Lammi C. The health benefits of sweet lupin seed flours and isolated proteins. Journal of Functional Foods 2015, 18:550-563.
3. Augustyns K., Van der Veken P., Senten K., Haemers A. The therapeutic potential of inhibitors of dipeptidyl peptidase IV (DPP IV) and related proline-specific dipeptidyl aminopeptidases. Current Medicinal Chemistry 2005, 12(8):971-998.
4. Baker N.A., Sept D., Joseph S., Holst M.J., McCammon J.A. Electrostatics of nanosystems: Application to microtubules and the ribosome. Proceedings of the National Academy of Sciences of the United States of America 2001, 98(18):10037-10041.
5. Bähr M., Fechner A., Kiehntopf M., Jahreis G. Consuming a mixed diet enriched with lupin protein beneficially affects plasma lipids in hypercholesterolemic subjects: A randomized controlled trial. Clinical Nutrition: Official Journal of the European Society of Parenteral and Enteral Nutrition 2015, 34(1):7-14.
6. Boschin G., Scigliuolo G.M., Resta D., Arnoldi A. ACE-inhibitory activity of enzymatic protein hydrolysates from lupin and other legumes. Food Chemistry 2014, 145:34-40.
7. Boschin G., Scigliuolo G.M., Resta D., Arnoldi A. Optimization of the enzymatic hydrolysis of lupin (Lupinus) proteins for producing ACE-inhibitory peptides. Journal of Agricultural and Food Chemistry 2014, 62(8):1846-1851.
8. Cam A., de Mejia E.G. Role of dietary proteins and peptides in cardiovascular disease. Molecular Nutrition and Food Research 2012, 56(1):53-66.
9. Capraro J., Clemente A., Rubio L.A., Magni C., Scarafoni A., Duranti M. Assessment of the lupin seed glucose-lowering protein intestinal absorption by using in vitro and ex vivo models. Food Chemistry 2011, 125(4):1279-1283.
10. Chen H.M., Muramoto K., Yamauchi F. Structural-analysis of antioxidative peptides from soybean beta-conglycinin. Journal of Agricultural and Food Chemistry 1995, 43(3):574-578.
11. da Silva Júnior W.S., de Godoy-Matos A.F., Kraemer-Aguiar L.G. Dipeptidyl peptidase 4: A new link between diabetes mellitus and atherosclerosis?. BioMed Research International 2015, 2015:816164.
12. Duranti M., Consonni A., Magni C., Sessa F., Scarafoni A. The major proteins of lupin seed: Characterisation and molecular properties for use as functional and nutraceutical ingredients. Trends in Food Science & Technology 2008, 19(12):624-633.
13. Ferruzza S., Rossi C., Scarino M.L., Sambuy Y. A protocol for differentiation of human intestinal Caco-2 cells in asymmetric serum-containing medium. Toxicology in Vitro: An International Journal Published in Association with BIBRA 2012, 26(8):1252-1255.
14. Ferruzza S., Scarino M.L., Gambling L., Natella F., Sambuy Y. Biphasic effect of iron on human intestinal Caco-2 cells: Early effect on tight junction permeability with delayed onset of oxidative cytotoxic damage. Cellular and Molecular Biology 2003, 49(1):89-99.
15. Foltz M., Meynen E.E., Bianco V., van Platerink C., Koning T.M., Kloek J. Angiotensin converting enzyme inhibitory peptides from a lactotripeptide-enriched milk beverage are absorbed intact into the circulation. The Journal of Nutrition 2007, 137(4):953-958.
16. Hashimoto K., Shimizu M. Epithelial properties of human intestinal Caco-2 cells cultured in a serum-free medium. Cytotechnology 1993, 13(3):175-184.
17. Heyman M., Crain-Denoyelle A.M., Nath S.K., Desjeux J.F. Quantification of protein transcytosis in the human colon carcinoma cell line CaCo-2. Journal of Cellular Physiology 1990, 143(2):391-395.
18. Hidalgo I.J., Raub T.J., Borchardt R.T. Characterization of the human colon carcinoma cell line (Caco-2) as a model system for intestinal epithelial permeability. Gastroenterology 1989, 96(3):736-749.
19. Korb O., Stützle T., Exner T.E. Empirical scoring functions for advanced protein-ligand docking with PLANTS. Journal of Chemical Information and Modeling 2009, 49(1):84-96.
20. Koska J., Sands M., Burciu C., Reaven P. Cardiovascular effects of dipeptidyl peptidase-4 inhibitors in patients with type 2 diabetes. Diabetes and Vascular Disease Research 2015, 12(3):154-163.
21. Lafarga T., O'Connor P., Hayes M. In silico methods to identify meat-derived prolyl endopeptidase inhibitors. Food Chemistry 2015, 175:337-343.
22. Lammi C., Zanoni C., Arnoldi A., Vistoli G. Two peptides from soy beta-conglycinin induce a hypocholesterolemic effect in HepG2 cells by a statin-like mechanism: Comparative in vitro and in silico modeling studies. Journal of Agricultural and Food Chemistry 2015, 63(36):7945-7951.
23. Lammi C., Zanoni C., Scigliuolo G.M., D'Amato A., Arnoldi A. Lupin peptides lower low-density lipoprotein (LDL) cholesterol through an up-regulation of the LDL receptor/sterol regulatory element binding protein 2 (SREBP2) pathway at HepG2 cell line. Journal of Agricultural and Food Chemistry 2014, 62(29):7151-7159.
24. Levashov P.A., Sutherland D.S., Besenbacher F., Shipovskov S. A robust method of determination of high concentrations of peptides and proteins. Analytical Biochemistry 2009, 395:111-112.
25. Miguel M., Dávalos A., Manso M.A., de la Peña G., Lasunción M.A., López-Fandiño R. Transepithelial transport across Caco-2 cell monolayers of antihypertensive egg-derived peptides. PepT1-mediated flux of Tyr-Pro-Ile. Molecular Nutrition and Food Research 2008, 52(12):1507-1513.
26. Miner-Williams W.M., Stevens B.R., Moughan P.J. Are intact peptides absorbed from the healthy gut in the adult human?. Nutrition Research Reviews 2014, 27(2):308-329.
27. Minkiewicz P., Dziuba J., Darewicz M., Bucholska J., Mogut D. Evaluation of in silico prediction possibility of epitope sequences using experimental data concerning allergenic food proteins summarised in BIOPEP database. Polish Journal of Food and Nutrition Sciences 2012, 62(3):151-157.
28. Natoli M., Leoni B.D., D'Agnano I., D'Onofrio M., Brandi R., Arisi I., Zucco F., Felsani A. Cell growing density affects the structural and functional properties of Caco-2 differentiated monolayer. Journal of Cellular Physiology 2011, 226(6):1531-1543.
29. Pak V.V., Koo M., Kim M.J., Yun L., Kwon D.Y. Binding effect and design of a competitive inhibitory peptide for HMG-CoA reductase through modeling of an active peptide backbone. Bioorganic and Medicinal Chemistry 2008, 16(3):1309-1318.
30. Regazzo D., Mollé D., Gabai G., Tomé D., Dupont D., Leonil J., Boutrou R. The (193-209) 17-residues peptide of bovine β-casein is transported through Caco-2 monolayer. Molecular Nutrition and Food Research 2010, 54(10):1428-1435.
31. Saito K., Jin D.H., Ogawa T., Muramoto K., Hatakeyama E., Yasuhara T., Nokihara K. Antioxidative properties of tripeptide libraries prepared by the combinatorial chemistry. Journal of Agricultural and Food Chemistry 2003, 51(12):3668-3674.
32. Sambuy Y., De Angelis I., Ranaldi G., Scarino M.L., Stammati A., Zucco F. The Caco-2 cell line as a model of the intestinal barrier: Influence of cell and culture-related factors on Caco-2 cell functional characteristics. Cell Biology and Toxicology 2005, 21(1):1-26.
33. Shi J., Blundell T.L., Mizuguchi K. FUGUE: Sequence-structure homology recognition using environment-specific substitution tables and structure-dependent gap penalties. Journal of Molecular Biology 2001, 310(1):243-257.
34. Sirtori C.R., Triolo M., Bosisio R., Bondioli A., Calabresi L., De Vergori V., Gomaraschi M., Mombelli G., Pazzucconi F., Zacherl C., Arnoldi A. Hypocholesterolaemic effects of lupin protein and pea protein/fibre combinations in moderately hypercholesterolaemic individuals. The British Journal of Nutrition 2012, 107(8):1176-1183.
35. Sirtori E., Resta D., Brambilla F., Zacherl C., Arnoldi A. The effects of various processing conditions on a protein isolate from Lupinus angustifolius. Food Chemistry 2010, 120(2):496-504.
36. Tanzadehpanah H., Asoodeh A., Chamani J. An antioxidant peptide derived from Ostrich (Struthio camelus) egg white protein hydrolysates. Food Research International 2012, 49(1):105-111.
37. Thwaites D.T., Brown C.D., Hirst B.H., Simmons N.L. Transepithelial glycylsarcosine transport in intestinal Caco-2 cells mediated by expression of H(+)-coupled carriers at both apical and basal membranes. The Journal of Biological Chemistry 1993, 268(11):7640-7642.
38. Vistoli G., Pedretti A., Mazzolari A., Testa B. In silico prediction of human carboxylesterase-1 (hCES1) metabolism combining docking analyses and MD simulations. Bioorganic and Medicinal Chemistry 2010, 18(1):320-329.
39. Yea C.S., Ebrahimpour A., Hamid A.A., Bakar J., Muhammad K., Saari N. Winged bean [Psophorcarpus tetragonolobus (L.) DC] seeds as an underutilised plant source of bifunctional proteolysate and biopeptides. Food & Function 2014, 5(5):1007-1016.
40. Zhu X.L., Watanabe K., Shiraishi K., Ueki T., Noda Y., Matsui T., Matsumoto K. Identification of ACE-inhibitory peptides in salt-free soy sauce that are transportable across caco-2 cell monolayers. Peptides 2008, 29(3):338-344.