The Relative Separation of Lunasin Peptide from Soya Protein and Checking Its Characteristics with Computational Tools (Based on Bioinformatics Findings)

Authors

  • Fatemeh safakhah Masters student in microbial biotechnology /Department of Biotechnology, Faculty of Biological Sciences/Alzahra University,Tehran,Iran
  • Mahboobeh Zarrabi Assistant Professor of Biophysics/ Department of Biotechnology, Faculty of Biological Sciences/Alzahra University,Tehran,Iran
  • Fakhri Sadat Hosseini Assistant Professor of Biotechnology/ Department of Biotechnology, Faculty of Biological Sciences/Alzahra University,Tehran,Iran

DOI:

https://doi.org/10.63053/ijhes.59

Abstract

Bioactive peptides are small peptides that can exhibit various properties including anticancer properties. Lunasin peptide is a 43-amino acid peptide isolated from soy protein that has anticancer properties. In this study, soy protein was enzymatically hydrolyzed and has some properties similar to lunasin in in- silico .  item It was checked The present study used commercial soybeans and soybean meal. In this research, the trypsin enzyme has acted on the substrate and the water quality has been measured. Protein extracted water was analyzed using methods such as electrophoresis and Bradford test to measure the quantity of protein.

In the second phase of the research, the properties of Lunasin were investigated using computational tools

The quality of water quality for commercial soybeans and soybean meal was 4.13 and 3.83, respectively. It was also determined by electrophoresis analysis that the peptides similar to lunasin were derived from soybean by trypsin enzyme. Bioinformatics results showed that acid Amines That At sustainability Role have, able change are. Results sign gave That this Peptide has Capabilities Anti cancerous Is That Maximum Score 87 % receive done Is .

References

Abel, S. D. A., & Baird, S. K. (2018). Honey is cytotoxic towards prostate cancer cells but interacts with the MTT reagent: Considerations for the choice of cell viability assay. Food Chemistry, 241, 70–78.

Aleksis, R., Jaudzems, K., Muceniece, R., & Liepinsh, E. (2016). Lunasin is a redox sensitive intrinsically disordered peptide with two transiently populated α-helical regions. Peptides, 85, 56–62.

Andersen, C. A. F., Palmer, A. G., Brunak, S., & Rost, B. (2002). Continuum secondary structure captures protein flexibility. Structure, 10(2), 175–184.

Ashaolu, T. J., Yantiam, N., & Yupanqui, C. T. (2017). Immunomodulatory effects of pepsin-educed soy protein hydrolysate in rats and murine cells. Functional Foods in Health and Disease, 7(11), 889-900.

Chiangjong, W., Chutipongtanate, S., & Hongeng, S. (2020). Anticancer peptide: Physicochemical property, functional aspect and trend in clinical application. International Journal of Oncology, 57(3), 678–696.

Dai, Y., Cai, X., Shi, W., Bi, X., Su, X., Pan, M., … Qian, H. (2017). Pro-apoptotic cationic host defense peptides rich in lysine or arginine to reverse drug resistance by disrupting tumor cell membrane. Amino Acids, 49(9), 1601–1610.

Daliri, E. B.-M., Oh, D. H., & Lee, B. H. (2017). Bioactive peptides. Foods, 6(5), 32.

de Souza, S. M. A., Fernandes, T. V. A., Kalume, D. E., Lima, L. M. T., Pascutti, P. G., & de Souza, T. L. F. (2020). Physicochemical and structural properties of lunasin revealed by spectroscopic, chromatographic and molecular dynamics approaches. Biochimica et Biophysica Acta (BBA)-Proteins and Proteomics, 1868(8), 140440.

Esteve, C., Marina, M. L., & García, M. C. (2015). Novel strategy for the revalorization of olive (Olea europaea) residues based on the extraction of bioactive peptides. Food Chemistry, 167, 272-280.

Fernández-Tomé, S., Sanchón, J., Recio, I., & Hernández-Ledesma, B. (2018). Transepithelial transport of lunasin and derived peptides: Inhibitory effects on the gastrointestinal cancer cells viability. Journal of Food Composition and Analysis, 68, 101–110.

Garnier, J., Osguthorpe, D. J., & Robson, B. (1978). Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins. Journal of Molecular Biology, 120(1), 97–120.

Gonzalez de Mejia, E., Castañeda-Reyes, E. D., Mojica, L., Dia, V., Wang, H., Wang, T., & Johnson, L. A. (2021). Potential health benefits associated with lunasin concentration in dietary supplements and lunasin-enriched soy extract. Nutrients, 13(5), 1618.

Hernandez-Ledesma, B., Hsieh, C.-C., & Ben, O. (2009). Lunasin, a novel seed peptide for cancer prevention. Peptides, 30(2), 426–430.

Hoskin, D. W., & Ramamoorthy, A. (2008). Studies on anticancer activities of antimicrobial peptides. Biochimica et Biophysica Acta (BBA)-Biomembranes, 1778(2), 357–375.

Huang, Y., Wang, X., Wang, H., Liu, Y., & Chen, Y. (2011). Studies on mechanism of action of anticancer peptides by modulation of hydrophobicity within a defined structural framework. Molecular Cancer Therapeutics, 10(3), 416–426.

Jahangirian, H., Kalantari, K., Izadiyan, Z., Rafiee-Moghaddam, R., Shameli, K., & Webster, T. J. (2019). A review of small molecules and drug delivery applications using gold and iron nanoparticles. International Journal of Nanomedicine, 14, 1633.

Jeong, H. J., Jeong, J. B., Hsieh, C. C., Hernández-Ledesma, B., & de Lumen, B. O. (2010). Lunasin is prevalent in barley and is bioavailable and bioactive in in vivo and in vitro studies. Nutrition and Cancer, 62(8), 1113–1119.

Kawaguchi, K., Han, Q., Li, S., Tan, Y., Igarashi, K., Kiyuna, T., … Nelson, S. D. (2018). Targeting methionine with oral recombinant methioninase (o-rMETase) arrests a patient-derived orthotopic xenograft (PDOX) model of BRAF-V600E mutant melanoma: implications for chronic clinical cancer therapy and prevention. Cell Cycle, 17(3), 356–361.

Kruger, N. J. (2009). The Bradford method for protein quantitation. The Protein Protocols Handbook, 17–24.

Kong, X., Guo, M., Hua, Y., Cao, D., & Zhang, C. (2008). Enzymatic preparation of immunomodulating hydrolysates from soy proteins. Bioresource technology, 99(18), 8873-8879.

Kyte, J. (2006). Structure in protein chemistry. Garland Science.

Lafarga, T., Álvarez, C., Bobo, G., & Aguiló-Aguayo, I. (2018). Characterization of functional properties of proteins from Ganxet beans (Phaseolus vulgaris L. var. Ganxet) isolated using an ultrasound-assisted methodology. Lwt, 98, 106–112.

Maddocks, O. D. K., Athineos, D., Cheung, E. C., Lee, P., Zhang, T., van den Broek, N. J. F., … Kruiswijk, F. (2017). Modulating the therapeutic response of tumours to dietary serine and glycine starvation. Nature, 544(7650), 372–376.

Pimentel, F. B., Alves, R. C., Harnedy, P. A., FitzGerald, R. J., & Oliveira, M. B. P. P. (2019). Macroalgal-derived protein hydrolysates and bioactive peptides: Enzymatic release and potential health enhancing properties. Trends in Food Science & Technology, 93, 106–124.

Rodrigues, E. G., Dobroff, A. S., Taborda, C. P., & Travassos, L. R. (2009). Antifungal and antitumor models of bioactive protective peptides. Anais Da Academia Brasileira de Ciências, 81, 503–520.

Roy, S., & Teron, R. (2019). BioDADPep: a bioinformatics database for anti diabetic peptides. Bioinformation, 15(11), 780.

Ruth, T. K., Rumble, J. N., Lamm, A. J., & Ellis, J. D. (2020). How Consumers Process Complex Information Related to Food Biotechnology: The Case of Citrus Greening. Journal of Food Products Marketing, 26(2), 103–122.

Rutherfurd, S. M. (2010). Methodology for determining degree of hydrolysis of proteins in hydrolysates: a review. Journal of AOAC International, 93(5), 1515–1522.Sánchez, A., & Vázquez, A. (2017). Bioactive peptides: A review. Food Quality and Safety, 1(1), 29-46.

Sharma, P., Kaur, H., Kehinde, B. A., Chhikara, N., Sharma, D., & Panghal, A. (2021). Food-derived anticancer peptides: a review. International Journal of Peptide Research and Therapeutics, 27(1), 55–70.

Shoombuatong, W., Schaduangrat, N., & Nantasenamat, C. (2018). Unraveling the bioactivity of anticancer peptides as deduced from machine learning. EXCLI Journal, 17, 734.

Singh, A., Kaushik, R., Mishra, A., Shanker, A., & Jayaram, B. (2016). ProTSAV: a protein tertiary structure analysis and validation server. Biochimica et Biophysica Acta (BBA)-Proteins and Proteomics, 1864(1), 11–19.

Suarez-Jimenez, G.-M., Burgos-Hernandez, A., & Ezquerra-Brauer, J.-M. (2012). Bioactive peptides and depsipeptides with anticancer potential: Sources from marine animals. Marine Drugs, 10(5), 963–986.

Tyagi, A., Tuknait, A., Anand, P., Gupta, S., Sharma, M., Mathur, D., … Raghava, G. P. S. (2015). CancerPPD: a database of anticancer peptides and proteins. Nucleic Acids Research, 43(D1), D837–D843.

Variyar, P. S., Limaye, A., & Sharma, A. (2004). Radiation-induced enhancement of antioxidant contents of soybean (Glycine max Merrill). Journal of Agricultural and Food Chemistry, 52(11), 3385–3388.

Vijayakumar, S., & Ptv, L. (2015). ACPP: a web server for prediction and design of anti-cancer peptides. International Journal of Peptide Research and Therapeutics, 21(1), 99–106.

Vuister, G. W., Fogh, R. H., Hendrickx, P., Doreleijers, J. F., & Gutmanas, A. (2014). An overview of tools for the validation of protein NMR structures. Journal of Biomolecular NMR, 58(4), 259–285.

Vuyyuri, S. B., Shidal, C., & Davis, K. R. (2018). Development of the plant-derived peptide lunasin as an anticancer agent. Current Opinion in Pharmacology, 41, 27–33.

Yang, Q.-Z., Wang, C., Lang, L., Zhou, Y., Wang, H., & Shang, D.-J. (2013). Design of potent, non-toxic anticancer peptides based on the structure of the antimicrobial peptide, temporin-1CEa. Archives of Pharmacal Research, 36(11), 1302–1310.

Published

2024-01-01

How to Cite

safakhah, F., Zarrabi, M., & Hosseini, F. S. (2024). The Relative Separation of Lunasin Peptide from Soya Protein and Checking Its Characteristics with Computational Tools (Based on Bioinformatics Findings). International Journal of New Findings in Health and Educational Sciences (IJHES), 2(1), 28–44. https://doi.org/10.63053/ijhes.59

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