The use of UniProtKB/BIOPEP for the analysis of oat globulin physicochemical parameters and bioactivity
The physico-chemical properties of oat proteins (globulins) were determined and an analysis was done whether products of in silico proteolysis contain mono- and multi-functional peptides with various biological activity. The MW(s), calculated by the ProtParam program, for precursors of 12S and 11S globulins and proteins without signal peptides were in the range of 50.78–61.86 kDa. The pH at which the solubility of the proteins under analysis was the lowest ranged from 7.29 to 9.44. A simulation of proteolysis with three enzymes (pepsin, trypsin, and chymotrypsin A) in the optimum conditions of the enzyme action can produce 6–8 bi-functional, 5–10 mono-functional biopeptides from oat globulins (12S, 11S globulins), and one tri-functional biopeptide (VY). The mono-functional biopeptides exhibited the activity of DPPIV inhibitors or ACE inhibitors, and the multi-functional biopeptides can exhibit the activity of inhibitors of both enzymes (DPPIV and ACE). Sensory peptides accounted for 43% of all the released mono- and multi-functional biopeptides.
Bhat Z. F., Kumar Sunil, Bhat Hina Fayaz (2015): Bioactive peptides from egg: a review. Nutrition & Food Science, 45, 190-212
https://doi.org/10.1108/NFS-10-2014-0088
Cheng Yu, Chen Jie, Xiong Youling L. (2010): Chromatographic Separation and Tandem MS Identification of Active Peptides in Potato Protein Hydrolysate That Inhibit Autoxidation of Soybean Oil-in-Water Emulsions. Journal of Agricultural and Food Chemistry, 58, 8825-8832
https://doi.org/10.1021/jf101556n
Fala L., Writer M. (2015): Trulicity (dulaglutide): a new GLP-1 receptor agonist once-weekly subcutaneous injection approved for the treatment of patients with type 2 diabetes. American Health and Drug Benefits, 8: 131–134.
Gasteiger E., Hoogland C., Gattiker A., Duvaud S., Wilkins M.R., Appel R.D., Bairoch A. (2005): Protein identification and analysis tools on the ExPASy Server. In: Walker J.M. (ed.): The Proteomics Protocols Handbook. UK, Humana Press: 571–607.
Jain Eric, Bairoch Amos, Duvaud Severine, Phan Isabelle, Redaschi Nicole, Suzek Baris E, Martin Maria J, McGarvey Peter, Gasteiger Elisabeth (2009): Infrastructure for the life sciences: design and implementation of the UniProt website. BMC Bioinformatics, 10, 136-
https://doi.org/10.1186/1471-2105-10-136
Klose Christina, Arendt Elke K. (2012): Proteins in Oats; their Synthesis and Changes during Germination: A Review. Critical Reviews in Food Science and Nutrition, 52, 629-639
https://doi.org/10.1080/10408398.2010.504902
Lafarga Tomas, O’Connor Paula, Hayes Maria (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
https://doi.org/10.1016/j.peptides.2014.07.005
Lan Vu Thi Tuyet, Ito Keisuke, Ohno Masumi, Motoyama Takayasu, Ito Sohei, Kawarasaki Yasuaki (2015): Analyzing a dipeptide library to identify human dipeptidyl peptidase IV inhibitor. Food Chemistry, 175, 66-73
https://doi.org/10.1016/j.foodchem.2014.11.131
Li Huan, Aluko Rotimi E. (2010): Identification and Inhibitory Properties of Multifunctional Peptides from Pea Protein Hydrolysate. Journal of Agricultural and Food Chemistry, 58, 11471-11476
https://doi.org/10.1021/jf102538g
Magrane M., Consortium U. (2011): UniProt Knowledgebase: a hub of integrated protein data. Database, 2011, bar009-bar009
https://doi.org/10.1093/database/bar009
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: 965–980.
Minkiewicz P., Dziuba J., Michalska J. (2011): Bovine Meat Proteins as Potential Precursors of Biologically Active Peptides - a Computational Study based on the BIOPEP Database. Food Science and Technology International, 17, 39-45
https://doi.org/10.1177/1082013210368461
Morato P.N., Lollo P.C.B., Moura C.S., Batista T.M., Carneiro E.M., Amaya-Farfan J. (2013): A dipeptide and an amino acid present in whey protein hydrolysate increase translocation of GLUT-4 to the plasma membrane in Wistar rats. Food Chemistry, 139, 853-859
https://doi.org/10.1016/j.foodchem.2012.12.062
MORIFUJI Masashi, KOGA Jinichiro, KAWANAKA Kentaro, HIGUCHI Mitsuru (2009): Branched-Chain Amino Acid-Containing Dipeptides, Identified from Whey Protein Hydrolysates, Stimulate Glucose Uptake Rate in L6 Myotubes and Isolated Skeletal Muscles. Journal of Nutritional Science and Vitaminology, 55, 81-86
https://doi.org/10.3177/jnsv.55.81
Möller Niels Peter, Scholz-Ahrens Katharina Elisabeth, Roos Nils, Schrezenmeir Jürgen (2008): Bioactive peptides and proteins from foods: indication for health effects. European Journal of Nutrition, 47, 171-182
https://doi.org/10.1007/s00394-008-0710-2
Nogata Yoichi, Nagamine Takashi, Yanaka Mikiko, Ohta Hideaki (2009): Angiotensin I Converting Enzyme Inhibitory Peptides Produced by Autolysis Reactions from Wheat Bran. Journal of Agricultural and Food Chemistry, 57, 6618-6622
https://doi.org/10.1021/jf900857w
Nongonierma Alice B., Mooney Catherine, Shields Denis C., FitzGerald Richard J. (2013): Inhibition of dipeptidyl peptidase IV and xanthine oxidase by amino acids and dipeptides. Food Chemistry, 141, 644-653
https://doi.org/10.1016/j.foodchem.2013.02.115
Pundir Sangya, Magrane Michele, Martin Maria J., O'Donovan Claire (2015): Searching and Navigating UniProt Databases. Current Protocols in Bioinformatics, 50, 1.27.1-1.27.10
https://doi.org/10.1002/0471250953.bi0127s50
Saito Yoshiyuki, Wanezaki (Nakamura) Keiko, Kawato Akitsugu, Imayasu Satoshi (2014): Structure and Activity of Angiotensin I Converting Enzyme Inhibitory Peptides from Sake and Sake Lees. Bioscience, Biotechnology, and Biochemistry, 58, 1767-1771
https://doi.org/10.1271/bbb.58.1767
Shamloo M., Eck P., Beta T. (2015): Angiotensin converting enzyme inhibitory peptides derived from cereals. Journal of Human Nutrition and Food Sciences, 3: 1057.
Szerszunowicz I., Nałęcz D., Dziuba M. (2017): Selected bioinformatic tools and MS (MALDI-TOF, PMF) techniques used in the strategy for the identification of oat proteins after 2-DE. In: Gasparis S. (ed.): Oat-Methods and Protocols. Methods in Molecular Biology. USA, Springer International Publishing: 253–270.
Vilmane L., Zute S., Straumite E., Galoburda R. (2015): Protein, amino acid and gluten content in oat (Avena sativa L.) grown in Latvia. Proceedings of the Latvian Academy of Sciences. Section B, 69: 170–177.
Zhang H., Wang J., Liu Y., Sun B. (2015): Peptides derived from oats improve insulin sensitivity and lower blood glucose in streptozotoci-induced diabetic mice. Journal of Biomedical Sciences, 4: 1–7.
