Analiza in silico peptydów immunoaktywnych pochodzących z białek żywności - badania z wykorzystaniem bazy BIOPEP

• Autorzy: Marta Dziuba , Dorota Nałęcz , Bartłomiej Dziuba

Warianty tytułu

In Silico Analysis of Immunoactive Peptides Derived from Food Proteins - a Study Based on BIOPEP Database

• Języki publikacji: PL

Abstrakty

Analizie bioinformatycznej poddano 89 peptydów immunoaktywnych dostępnych w bazie BIOPEP. Obecność fragmentów potencjalnie immunoaktywnych stwierdzono w 90 ze 150 sekwencji analizowanych białek. Sekwencje aminokwasowe badanych peptydów analizowano z uwzględnieniem: długości łańcucha, udziału procentowego poszczególnych aminokwasów, pI, molowego współczynnika ekstynkcji, indeksu hydropatii i ładunku wypadkowego. Ponadto określono możliwości ich uwalniania in silico przez enzymy proteolityczne. Na podstawie komputerowej analizy z zastosowaniem programu ProtParam stwierdzono, że immunoaktywne peptydy to głównie fragmenty hydrofilowe, w sekwencji których przeważają takie aminokwasy, jak: Lys, Arg i Pro, obdarzone ładunkiem dodatnim w neutralnym pH. W komputerowej symulacji proteolizy in silico wybranych 11 białek żywności o największej częstości występowania peptydów immunoaktywnych (parametr A > 0,02) wykazano, że tylko trzy enzymy: chymaza (EC 3.4.21.39), elastaza trzustkowa (EC 3.4.21.36) i endopeptydaza glicylowa (EC 3.4.22.25), spośród dostępnych w bazie BIOPEP, wykazywały specyficzność pozwalającą na uwalnianie peptydów immunoaktywnych w układzie jednego enzymu. Produktami hydrolizy analizowanych białek, przy użyciu wybranych enzymów proteolitycznych, były głównie 2 - 3 aminokwasowe fragmenty peptydowe. (abstrakt oryginalny)

EN

89 immunoactive peptides available in the BIOPEP Database were bioinformatically analyzed. It was determined that potentially immunoactive peptide fragments were present in 90 of 150 sequences of the proteins analysed. In the sequences of immunoactive peptides studied, the following was analysed: peptide chain length, percent content of individual amino acids, pI, molar extinction coefficient, hydropathy index, and net charge. Furthermore, it was determined whether it was possible to in silico release those peptides using specific proteolytic enzymes. Based on the results of the computer analysis performed using a ProtParam software, it was confirmed that the immunoactive peptides were, mainly, hydrophilic fragments and in their sequence, the alkaline amino acids prevailed, such as: Arg, Lys, and Pro, with a positive net charge in neutral pH. A computer simulation of in silico proteolysis of 11 selected food proteins showing the highest occurrence frequency of immunoactive peptides (parameter A > 0.02) was performed and based thereon, it was proved that of all the enzymes available in the BIOPEP Database, only three proteolytic enzymes , i.e.: chymase (EC 3.4.21.39), pancreatic elastase (EC 3.4.21.36), and glycyl endopeptidase (EC 3.4.22.25) were able to release immunoactive peptides in one enzyme setup. The 2-3 amino acid peptide fragments were, mainly, produced during the hydrolysis of the analyzed proteins performed using proteolytic enzymes. (original abstract)

Słowa kluczowe

PL

Żywność; Właściwości zdrowotne produktu; Biochemia

EN

Food; Health properties of the product; Biochemistry

• Czasopismo: Żywność: nauka - technologia - jakość
• Rocznik: 21 (2014)
• Numer: nr 5 (96)
• Strony: 144--154

Twórcy

autor

Marta Dziuba

• Uniwersytet Warmińsko-Mazurski w Olsztynie

autor

Dorota Nałęcz

• Uniwersytet Warmińsko-Mazurski w Olsztynie

autor

Bartłomiej Dziuba

• Uniwersytet Warmińsko-Mazurski w Olsztynie

Bibliografia

• [1] BIOPEP. [online]. Dostęp w Internecie: [01.2009, 12.2011, 01.2013.]: http://www.edu.pl/biochemia/index.php/pl/biochemia
• [2] Carrasco-Castilla J., Hernandez-Alvarez A.J., Jimenez-Martinez C., Gutierrez-Lopez G.F., Davila-Ortiz G.: Use of proteomics and peptidomics methods in food bioactive peptide science and engineering. Food Eng. Rev., 2012, 4 (4), 224-243.
• [3] Chanput W., Nakai S., Theerakulkait C.: Introduction of new computer softwares for classification and prediction purposes of bioactive peptides: case study in antioxidative tripeptides. Int. J. Food Prop., 2010, 13, 947-959.
• [4] Chen C., Chi Y.J.: Antioxidant, ACE inhibitory activities and functional properties of egg white protein hydrolysate. J. Food Biochem., 2012, 36, 383-394.
• [5] Choi J., Sabikhi L., Hassan A., Anand S.: Bioactive peptides in dairy products. Int. J. Dairy Technol., 2012, 65 1-12.
• [6] Dziuba J., Iwaniak A., Darewicz M., Niklewicz M.: Computer simulation of animal proteins proteolysis in aspect of obtaining bioactive peptides. Pol. J. Nat. Sci., 2002, 10, 209-222.
• [7] Dziuba M., Darewicz M.: Food proteins as precursors of bioactive peptides - Classification into families. Food Sci. Technol. Int., 2007, 13, 393-404.
• [8] Dziuba M., Dziuba B.: In silico analysis of bioactive peptides. In: Bioactive proteins and peptides as functional foods and nutraceuticals. Mine Y, Li-Chan ECY, Jiang B (eds). Blackwell Publishing Ltd.and Institute of Food Technologists, London, Boca Raton, FL, 2010, pp. 325-340.
• [9] Dziuba M., Minkiewicz P., Dąbek M.: Peptides, products of specific proteolysis as a molecular marker of allergenic proteins - in silico studies. Acta Sci. Pol., Technol. Aliment., 2013 12 (1), 101-112.
• [10] Epand R.M., Vogel H.J.: Diversity of antimicrobial peptides and their mechanisms of action. BBABiomembranes, 1999, 1462, 11-28.
• [11] Fiat A.M., Jolles P.: Caseins of various origins and biologically-active casein peptides and oligosaccharides: structural and physiological aspects. Mol. Cell. Biochem., 1989, 87, 5-30.
• [12] Gasteiger E., Hoogland C., Gattiker A., Duvaud S., Wilkins M.R., Appel R.D., Bairoch A.: Protein identification and analysis tools on the ExPASy server. In: The Proteomics Protocols Handbook.Walker JM (ed). Humana Press Inc., Totowa, New York 2005, pp. 571-607.
• [13] Gautier S.F., Pouliot Y., Saint-Sauveur D.: Immunomodulatory peptides obtained by the enzymatic hydrolysis of whey proteins. Int. Dairy J., 2006, 16, 1315-1323.
• [14] Gill H.S., Doull F., Rutherford K.J., Cross M.L.: Immunoregulatory peptides in bovine milk. Br. J. Nutr., 2000, 84, 111-117.
• [15] Gobetti M., Stepaniak L., De Angelis M., Corsetti A., Di Cagno R.: Latent bioactive peptides in milk proteins: Proteolytic activation and significance in dairy processing. CRC Cr. Rev. Food Sci., 2002,42, 223-239.
• [16] Guruprasad K., Reddy B.V.B., Pandit M.W.: Correlation between stability of a protein and its dipeptide composition - a novel-approach for predicting in vivo stability of a protein from its primary sequence.Protein Eng., 1990, 4, 155-161.
• [17] Jenssen H., Hancock R.E.: Therapeutic potential of HDPs as immunomodulatory agents. In: Antimicrobial Peptides. Methods and Protocols. Giuliani A, Rinaldi A (eds). Humana Press Inc., Monserrato2010, pp. 329-347.
• [18] Kannan A., Hettiarachchy N.S., Lay J.O., Liyanage R.: Human cancer cell proliferation inhibition by a pentapeptide isolated and characterized from rice bran. Peptides, 2010, 31, 1629-1634.
• [19] Korhonen H., Pihlanto A.: Bioactive peptides: Production and functionality. Int. Dairy J., 2006, 16, 945-960.
• [20] Korhonen H., Pihlanto A.: Food-derived bioactive peptides - Opportunities for designing future foods. Curr. Pharm. Design, 2003, 9, 1297-1308.
• [21] Kyte J., Doolittle R.F.: A simple method for displaying the hydropathic character of a protein. J. Mol. Biol., 1982, 157 (1), 105-132.
• [22] Lahov E., Regelson W.: Antibacterial and immunostimulating casein-derived substances from milk: Casecidin, isracidin peptides. Food Chem. Toxicol., 1996, 34, 131-145.
• [23] Migliore-Samour D., Floch F., Jolles P.: Biologically-active casein peptides implicated in immunomodulation. J. Dairy Res., 1989, 56, 357-362.
• [24] Moller N.P., Scholz-Ahrens K.E., Roos N., Schrezenmeir J.: Bioactive peptides and proteins from foods: indication for health effects. Eur. J. Nutr., 2008, 47, 171-182.
• [25] ProtParam. [online]. EXPASY. Dostęp w Internecie [01.2012.]: http://web.expasy.org/protparam/
• [26] Schober Y., Yoo S.H., Paik H.D., Spengler B., Roempp A., Jayaprakasha H.M., Yoon Y.C.: Characterization of bioactive peptides derived by enzymatic hydrolysis of whey protein concentrate.Milchwissenschaft, 2012, 67, 55-57.
• [27] Srinivasan M., Dunker A.K.: Proline rich motifs as drug targets in immune mediated disorders. Int. J. Pept., 2012, 634769:1-634769:14.
• [28] Steinstraesser L., Kraneburg U., Jacobson F., Al-Benna S.: Host defense peptides and their antimicrobial - immunomodulatory duality. Immunobiology, 2011, 216, 322-333.
• [29] Takahashi M., Moriguchi S., Ikeno M., Kono S., Ohata K., Usui H., Kurahashi K., Sasaki R., Yoshikawa M.: Studies on the ileum-contracting mechanisms and identification as a complement C3a receptoragonist of oryzatensin, a bioactive peptide derived from rice albumin. Peptides, 1996, 17, 5-12.
• [30] Udenigwe C.C., Aluko R.E.: Food protein-derived bioactive peptides: production, processing, and potential health benefits. J. Food Sci., 2012, 77 (1), 11-24.
• [31] Zhang L., Falla T.J.: Host defense peptides for use as potential therapeutics. Curr. Opin. Invest. Dr., 2009, 10, 164-171.

Identyfikatory

DOI

10.15193/ZNTJ/2014/96/144-154