메뉴 건너뛰기




Volumn 60, Issue 38, 2012, Pages 9727-9736

Mass spectrometric evidence of malonaldehyde and 4-hydroxynonenal adductions to radical-scavenging soy peptides

Author keywords

4 hydroxynonenal (HNE); malonaldehyde (MDA); mass spectrometry; peptides; radical scavenging activity

Indexed keywords

4-HYDROXY-NONENAL; ANTIOXIDATIVE PEPTIDES; ASPARAGINE RESIDUE; COVALENT MODIFICATIONS; FLUORESCENT PRODUCTS; FOOD SYSTEM; LC-ESI-MS/MS; LYSINE RESIDUES; MALONALDEHYDE; MICHAEL ADDITIONS; MS/MS ANALYSIS; POTENTIAL MECHANISM; POTENTIAL TARGETS; SCHIFF BASE FORMATION; SCHIFF-BASE; SIDE-CHAINS; SOY PROTEIN HYDROLYSATE;

EID: 84866724337     PISSN: 00218561     EISSN: 15205118     Source Type: Journal    
DOI: 10.1021/jf3026277     Document Type: Article
Times cited : (74)

References (41)
  • 1
    • 0034545719 scopus 로고    scopus 로고
    • Quantification and significance of protein oxidation in biological samples
    • Shacter, E. Y. Quantification and significance of protein oxidation in biological samples Drug Metab. Rev. 2000, 32, 307-326
    • (2000) Drug Metab. Rev. , vol.32 , pp. 307-326
    • Shacter, E.Y.1
  • 2
    • 0025814980 scopus 로고
    • Chemistry and biochemistry of 4-hydroxynonenal, malondialdehyde and related aldehydes
    • Esterbauer, H.; Schaur, R. J.; Zollner, H. Chemistry and biochemistry of 4-hydroxynonenal, malondialdehyde and related aldehydes Free Radical Biol. Med. 1991, 11, 81-128
    • (1991) Free Radical Biol. Med. , vol.11 , pp. 81-128
    • Esterbauer, H.1    Schaur, R.J.2    Zollner, H.3
  • 3
    • 0037411282 scopus 로고    scopus 로고
    • 4-Hydroxy-2-nonenal: A product and mediator of oxidative stress
    • Uchida, K. 4-Hydroxy-2-nonenal: a product and mediator of oxidative stress Prog. Lipid Res. 2003, 42, 318-343
    • (2003) Prog. Lipid Res. , vol.42 , pp. 318-343
    • Uchida, K.1
  • 4
    • 23944478990 scopus 로고    scopus 로고
    • A review of recent studies on malondialdehyde as toxic molecule and biological marker of oxidative stress
    • Rio, D. D.; Stewart, A. J.; Pellegrini, N. A review of recent studies on malondialdehyde as toxic molecule and biological marker of oxidative stress Nutr. Metab. Cardiovasc. 2005, 15, 316-328
    • (2005) Nutr. Metab. Cardiovasc. , vol.15 , pp. 316-328
    • Rio, D.D.1    Stewart, A.J.2    Pellegrini, N.3
  • 6
    • 0034492226 scopus 로고    scopus 로고
    • Lipid oxidation in oil-in-water emulsions: Impact of molecular environment on chemical reactions in heterogeneous food systems
    • McClements, D. J.; Decker, E. A. Lipid oxidation in oil-in-water emulsions: impact of molecular environment on chemical reactions in heterogeneous food systems J. Food Sci. 2000, 65, 1270-1282
    • (2000) J. Food Sci. , vol.65 , pp. 1270-1282
    • McClements, D.J.1    Decker, E.A.2
  • 7
    • 77954387450 scopus 로고    scopus 로고
    • Myoglobin and lipid oxidation interactions: Mechanistic bases and control
    • Faustman, C.; Sun, Q.; Mancini, R.; Suman, S. P. Myoglobin and lipid oxidation interactions: mechanistic bases and control Meat Sci. 2010, 86, 86-94
    • (2010) Meat Sci. , vol.86 , pp. 86-94
    • Faustman, C.1    Sun, Q.2    Mancini, R.3    Suman, S.P.4
  • 8
    • 28444440308 scopus 로고    scopus 로고
    • Inhibition of lipid oxidation in cooked beef patties by hydrolyzed potato protein is related to its reducing and radical scavenging ability
    • Wang, L. L.; Xiong, Y. L. Inhibition of lipid oxidation in cooked beef patties by hydrolyzed potato protein is related to its reducing and radical scavenging ability J. Agric. Food Chem. 2005, 53, 9186-9192
    • (2005) J. Agric. Food Chem. , vol.53 , pp. 9186-9192
    • Wang, L.L.1    Xiong, Y.L.2
  • 9
    • 78149393801 scopus 로고    scopus 로고
    • Fractionation, separation, and identification of antioxidative peptides in potato protein hydrolysate that enhance oxidative stability of soybean oil emulsions
    • Cheng, Y.; Chen, J.; Xiong, Y. L. Fractionation, separation, and identification of antioxidative peptides in potato protein hydrolysate that enhance oxidative stability of soybean oil emulsions J. Food Sci. 2010, 75, C760-C765
    • (2010) J. Food Sci. , vol.75
    • Cheng, Y.1    Chen, J.2    Xiong, Y.L.3
  • 10
    • 0031260402 scopus 로고    scopus 로고
    • Protein modification by lipid peroxidation products: Formation of malondialdehyde-derived N -(2-propenol)lysine in proteins
    • Uchida, K.; Sakai, K.; Itakura, K.; Osawa, T.; Toyokuni, S. Protein modification by lipid peroxidation products: formation of malondialdehyde- derived N -(2-propenol)lysine in proteins Arch. Biochem. Biophys. 1997, 346, 45-52
    • (1997) Arch. Biochem. Biophys. , vol.346 , pp. 45-52
    • Uchida, K.1    Sakai, K.2    Itakura, K.3    Osawa, T.4    Toyokuni, S.5
  • 11
    • 0347683483 scopus 로고    scopus 로고
    • Identification of a new cross-link and unique histidine adduct from bovine serum albumin incubated with malondialdehyde
    • Slatter, D. A.; Avery, N. C.; Bailey, A. J. Identification of a new cross-link and unique histidine adduct from bovine serum albumin incubated with malondialdehyde J. Biol. Chem. 2004, 279, 61-69
    • (2004) J. Biol. Chem. , vol.279 , pp. 61-69
    • Slatter, D.A.1    Avery, N.C.2    Bailey, A.J.3
  • 12
    • 84862017251 scopus 로고    scopus 로고
    • Characterization of 4-HNE modified L-FABP reveals alterations in structural and functional dynamics
    • Smathers, R. L.; Fritz, K. S.; Galligan, J. J.; Shearn, C. T.; Reigan, P. Characterization of 4-HNE modified L-FABP reveals alterations in structural and functional dynamics PLoS ONE 2012, 7 (6) e38459
    • (2012) PLoS ONE , vol.7 , Issue.6 , pp. 38459
    • Smathers, R.L.1    Fritz, K.S.2    Galligan, J.J.3    Shearn, C.T.4    Reigan, P.5
  • 13
    • 0030498053 scopus 로고    scopus 로고
    • Lipoxidation products as biomarkers of oxidative damage to proteins during lipid peroxidation reactions
    • Requena, J. R.; Fu, M.; Ahmed, M. U.; Jenkins, A. J.; Lyons, T. J.; Thorpe, S. R. Lipoxidation products as biomarkers of oxidative damage to proteins during lipid peroxidation reactions Nephrol. Dial. Transplant. 1996, 11 (Suppl. 5) 48-53
    • (1996) Nephrol. Dial. Transplant. , vol.11 , Issue.SUPPL. 5 , pp. 48-53
    • Requena, J.R.1    Fu, M.2    Ahmed, M.U.3    Jenkins, A.J.4    Lyons, T.J.5    Thorpe, S.R.6
  • 14
    • 0031772147 scopus 로고    scopus 로고
    • U-101033E (2,4-diaminopyrrolopyrimidine), a potent inhibitor of membrane lipid peroxidation as assessed by the production of 4-hydroxynonenal, malondialdehyde, and 4-hydroxynonenal-protein adducts
    • Rohn, T. T.; Nelson, L. K.; Waeg, G.; Quinn, M. T. U-101033E (2,4-diaminopyrrolopyrimidine), a potent inhibitor of membrane lipid peroxidation as assessed by the production of 4-hydroxynonenal, malondialdehyde, and 4-hydroxynonenal-protein adducts Biochem. Pharmacol. 1998, 56, 1371-1379
    • (1998) Biochem. Pharmacol. , vol.56 , pp. 1371-1379
    • Rohn, T.T.1    Nelson, L.K.2    Waeg, G.3    Quinn, M.T.4
  • 15
    • 67249118991 scopus 로고    scopus 로고
    • Structural modification of soy protein by the lipid peroxidation product malondialdehyde
    • Wu, W.; Zhang, C.; Hua, Y. Structural modification of soy protein by the lipid peroxidation product malondialdehyde J. Sci. Food Agric. 2009, 89, 1416-1423
    • (2009) J. Sci. Food Agric. , vol.89 , pp. 1416-1423
    • Wu, W.1    Zhang, C.2    Hua, Y.3
  • 16
    • 0026606054 scopus 로고
    • Modification of histidine residues in proteins by reaction with 4-hydroxynonenal
    • Uchida, K.; Stadtman, E. R. Modification of histidine residues in proteins by reaction with 4-hydroxynonenal Proc. Natl. Acad. Sci. U.S.A. 1992, 89, 4544-4548
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 4544-4548
    • Uchida, K.1    Stadtman, E.R.2
  • 17
    • 0041846956 scopus 로고    scopus 로고
    • Ms2Assign, automated assignment and nomenclature of tandem mass spectra of chemically crosslinked peptides
    • Schilling, B.; Row, R. H.; Gibson, B. W.; Guo, X.; Young, M. M. Ms2Assign, automated assignment and nomenclature of tandem mass spectra of chemically crosslinked peptides J. Am. Soc. Mass Spectrom. 2003, 14, 834-850
    • (2003) J. Am. Soc. Mass Spectrom. , vol.14 , pp. 834-850
    • Schilling, B.1    Row, R.H.2    Gibson, B.W.3    Guo, X.4    Young, M.M.5
  • 18
    • 70349215199 scopus 로고    scopus 로고
    • Structural and emulsifying properties of soy protein isolate subjected to acid and alkaline pH-shifting processes
    • Jiang, J.; Chen, J.; Xiong, Y. L. Structural and emulsifying properties of soy protein isolate subjected to acid and alkaline pH-shifting processes J. Agric. Food Chem. 2009, 57, 7576-7583
    • (2009) J. Agric. Food Chem. , vol.57 , pp. 7576-7583
    • Jiang, J.1    Chen, J.2    Xiong, Y.L.3
  • 20
    • 69349093534 scopus 로고    scopus 로고
    • Fractionation and evaluation of radical scavenging peptides from in vitro digests of buckwheat protein
    • Ma, Y.; Xiong, Y. L.; Zhai, J.; Zhu, H.; Dziubla, T. Fractionation and evaluation of radical scavenging peptides from in vitro digests of buckwheat protein Food Chem. 2010, 118, 582-588
    • (2010) Food Chem. , vol.118 , pp. 582-588
    • Ma, Y.1    Xiong, Y.L.2    Zhai, J.3    Zhu, H.4    Dziubla, T.5
  • 21
    • 0031760413 scopus 로고    scopus 로고
    • Screening of dietary carotenoids and carotenoid-rich fruit extracts for antioxidant activities applying the 2,2′-azobis(3-ethylenebenzothiazoline- 6-sulfonic) acid radical cation decolorization assay
    • Pellegrini, N.; Re, R.; Yang, M.; Rice-Evans, C. A. Screening of dietary carotenoids and carotenoid-rich fruit extracts for antioxidant activities applying the 2,2′-azobis(3-ethylenebenzothiazoline-6-sulfonic) acid radical cation decolorization assay Methods Enzymol. 1999, 299, 379-389
    • (1999) Methods Enzymol. , vol.299 , pp. 379-389
    • Pellegrini, N.1    Re, R.2    Yang, M.3    Rice-Evans, C.A.4
  • 22
    • 0035816496 scopus 로고    scopus 로고
    • Comparison of analytical techniques to quantify malondialdehyde in milk powders
    • Fenaille, F.; Mottier, P.; Turesky, R. J.; Ali, S.; Guy, P. A. Comparison of analytical techniques to quantify malondialdehyde in milk powders J. Chromatogr., A 2001, 921, 237-245
    • (2001) J. Chromatogr., A , vol.921 , pp. 237-245
    • Fenaille, F.1    Mottier, P.2    Turesky, R.J.3    Ali, S.4    Guy, P.A.5
  • 23
    • 0031051893 scopus 로고    scopus 로고
    • Quantification of malondialdehyde and 4-hydroxynonenal adducts to lysine residues in native and oxidized human low-density lipoprotein
    • Requena, J. R.; Fu, M. X.; Ahmed, M. U.; Jenkins, A. J.; Lyons, T. J.; Baynes, J. W.; Thorpe, S. R. Quantification of malondialdehyde and 4-hydroxynonenal adducts to lysine residues in native and oxidized human low-density lipoprotein Biochem. J. 1997, 322, 317-325
    • (1997) Biochem. J. , vol.322 , pp. 317-325
    • Requena, J.R.1    Fu, M.X.2    Ahmed, M.U.3    Jenkins, A.J.4    Lyons, T.J.5    Baynes, J.W.6    Thorpe, S.R.7
  • 25
    • 80055045358 scopus 로고    scopus 로고
    • Effect of peptide size on antioxidant properties of African yam bean seed (Sphenostylis stenocarpa) protein hydrolysate fractions
    • Ajibola, C. F.; Fashakin, J. B.; Fagbemi, T. N.; Aluko, R. E. Effect of peptide size on antioxidant properties of African yam bean seed (Sphenostylis stenocarpa) protein hydrolysate fractions Int. J. Mol. Sci. 2011, 12, 6685-6702
    • (2011) Int. J. Mol. Sci. , vol.12 , pp. 6685-6702
    • Ajibola, C.F.1    Fashakin, J.B.2    Fagbemi, T.N.3    Aluko, R.E.4
  • 26
    • 0038058742 scopus 로고    scopus 로고
    • Bioactive proteins and peptides from food sources. Applications of bioprocesses used in isolation and recovery
    • Kitts, D. D.; Weiler, K. Bioactive proteins and peptides from food sources. Applications of bioprocesses used in isolation and recovery Curr. Pharm. Des. 2003, 9, 1309-1323
    • (2003) Curr. Pharm. Des. , vol.9 , pp. 1309-1323
    • Kitts, D.D.1    Weiler, K.2
  • 27
    • 77955666361 scopus 로고    scopus 로고
    • Chromatographic separation and tandem MS identification of active peptides in potato protein hydrolysate that inhibit autoxidation of soybean oil-in-water emulsions
    • Cheng, Y.; Chen, J.; Xiong, Y. L. Chromatographic separation and tandem MS identification of active peptides in potato protein hydrolysate that inhibit autoxidation of soybean oil-in-water emulsions J. Agric. Food Chem. 2010, 58, 8825-8832
    • (2010) J. Agric. Food Chem. , vol.58 , pp. 8825-8832
    • Cheng, Y.1    Chen, J.2    Xiong, Y.L.3
  • 29
    • 33748747614 scopus 로고    scopus 로고
    • A new frontier in soy bioactive peptides that may prevent age-related chronic diseases
    • Wang, W. Y.; De Mejia, E. G. A new frontier in soy bioactive peptides that may prevent age-related chronic diseases Comp. Rev. Food Sci. Food Saf. 2005, 4, 63-78
    • (2005) Comp. Rev. Food Sci. Food Saf. , vol.4 , pp. 63-78
    • Wang, W.Y.1    De Mejia, E.G.2
  • 30
    • 79958164223 scopus 로고    scopus 로고
    • Free aromatic amino acids in egg yolk show antioxidant properties
    • Nimalaratne, C.; Lopes-Lutz, D.; Schieber, A.; Wu, J. Free aromatic amino acids in egg yolk show antioxidant properties Food Chem. 2011, 129, 155-161
    • (2011) Food Chem. , vol.129 , pp. 155-161
    • Nimalaratne, C.1    Lopes-Lutz, D.2    Schieber, A.3    Wu, J.4
  • 31
    • 77951270043 scopus 로고    scopus 로고
    • Amino acid composition and antioxidant properties of pea seed (Pisum sativum L.) enzymatic protein hydrolysate fractions
    • Pownall, T. L.; Udenigwe, C. C.; Aluko, R. E. Amino acid composition and antioxidant properties of pea seed (Pisum sativum L.) enzymatic protein hydrolysate fractions J. Agric. Food Chem. 2010, 58, 4712-4718
    • (2010) J. Agric. Food Chem. , vol.58 , pp. 4712-4718
    • Pownall, T.L.1    Udenigwe, C.C.2    Aluko, R.E.3
  • 32
    • 69549107612 scopus 로고    scopus 로고
    • Fast and accurate determination of absolute individual molecular weight distributions from mixtures of polymers via size exclusion chromatography- electrospray ionization mass spectrometry
    • Gruendling, T.; Guilhaus, M.; Barner-Kowollik, C. Fast and accurate determination of absolute individual molecular weight distributions from mixtures of polymers via size exclusion chromatography-electrospray ionization mass spectrometry Macromolecules 2009, 42, 6366-6374
    • (2009) Macromolecules , vol.42 , pp. 6366-6374
    • Gruendling, T.1    Guilhaus, M.2    Barner-Kowollik, C.3
  • 33
    • 31844452260 scopus 로고    scopus 로고
    • Mass spectroscopic characterization of protein modification by malondialdehyde
    • Ishii, T.; Kumazawa, S.; Sakurai, T.; Nakayama, T.; Uchida, K. Mass spectroscopic characterization of protein modification by malondialdehyde Chem. Res. Toxicol. 2006, 19, 122-129
    • (2006) Chem. Res. Toxicol. , vol.19 , pp. 122-129
    • Ishii, T.1    Kumazawa, S.2    Sakurai, T.3    Nakayama, T.4    Uchida, K.5
  • 34
    • 77958151524 scopus 로고    scopus 로고
    • The malondialdehyde-derived fluorophore DHP-lysine is a potent sensitizer of UVA-induced photooxidative stress in human skin cells
    • Lamore, S. D.; Azimian, S.; Horn, D.; Anglin, B. L.; Uchida, K.; Cabello, C. M.; Wondrak, G. T. The malondialdehyde-derived fluorophore DHP-lysine is a potent sensitizer of UVA-induced photooxidative stress in human skin cells J. Photochem. Photobiol. B 2010, 101, 251-264
    • (2010) J. Photochem. Photobiol. B , vol.101 , pp. 251-264
    • Lamore, S.D.1    Azimian, S.2    Horn, D.3    Anglin, B.L.4    Uchida, K.5    Cabello, C.M.6    Wondrak, G.T.7
  • 35
    • 0028897831 scopus 로고
    • Structural definition of early lysine and histidine adduction chemistry of 4-hydroxynonenal
    • Nadkarni, D. V.; Sayre, L. M. Structural definition of early lysine and histidine adduction chemistry of 4-hydroxynonenal Chem. Res. Toxicol. 1995, 8, 284-291
    • (1995) Chem. Res. Toxicol. , vol.8 , pp. 284-291
    • Nadkarni, D.V.1    Sayre, L.M.2
  • 36
    • 23844448026 scopus 로고    scopus 로고
    • 4-Oxo-2-nonenal is both more neurotoxic and more protein reactive than 4-hydroxy-2-nonenal
    • Lin, D.; Lee, H. G.; Liu, Q.; Perry, G.; Smith, M. A.; Sayre, L. M. 4-Oxo-2-nonenal is both more neurotoxic and more protein reactive than 4-hydroxy-2-nonenal Chem. Res. Toxicol. 2005, 18, 1219-1231
    • (2005) Chem. Res. Toxicol. , vol.18 , pp. 1219-1231
    • Lin, D.1    Lee, H.G.2    Liu, Q.3    Perry, G.4    Smith, M.A.5    Sayre, L.M.6
  • 37
    • 33845390864 scopus 로고    scopus 로고
    • Protein adducts generated from products of lipid oxidation: Focus on HNE and ONE
    • Sayre, L. M.; Lin, D.; Yuan, Q.; Zhu, X.; Tang, X. Protein adducts generated from products of lipid oxidation: focus on HNE and ONE Drug Metab. Rev. 2006, 38, 651-675
    • (2006) Drug Metab. Rev. , vol.38 , pp. 651-675
    • Sayre, L.M.1    Lin, D.2    Yuan, Q.3    Zhu, X.4    Tang, X.5
  • 39
    • 3242768438 scopus 로고    scopus 로고
    • Modification of cytochrome c by 4-hydroxy-2-nonenal: Evidence for histidine, lysine, and arginine-aldehyde adducts
    • Isom, A. L.; Barnes, S.; Wilson, L.; Kirk, M.; Coward, L.; Darley-Usmar, V. Modification of cytochrome c by 4-hydroxy-2-nonenal: evidence for histidine, lysine, and arginine-aldehyde adducts J. Am. Soc. Mass Spectrom. 2004, 15, 1136-1147
    • (2004) J. Am. Soc. Mass Spectrom. , vol.15 , pp. 1136-1147
    • Isom, A.L.1    Barnes, S.2    Wilson, L.3    Kirk, M.4    Coward, L.5    Darley-Usmar, V.6
  • 40
    • 58149163597 scopus 로고    scopus 로고
    • Synaptosomal toxicity and nucleophillic targets of 4-hydroxy-2-nonenal
    • LoPachin, R. M.; Geohagen, B. C.; Gavin, T. Synaptosomal toxicity and nucleophillic targets of 4-hydroxy-2-nonenal Toxicol. Sci. 2009, 107, 171-181
    • (2009) Toxicol. Sci. , vol.107 , pp. 171-181
    • Lopachin, R.M.1    Geohagen, B.C.2    Gavin, T.3
  • 41
    • 0036852609 scopus 로고    scopus 로고
    • Covalent modification of amino acid nucleophiles by the lipid peroxidation products 4-hydroxy-2-nonenal and 4-oxo-2-nonenal
    • Doorn, J. A.; Petersen, D. R. Covalent modification of amino acid nucleophiles by the lipid peroxidation products 4-hydroxy-2-nonenal and 4-oxo-2-nonenal Chem. Res. Toxicol. 2000, 15, 1445-1450
    • (2000) Chem. Res. Toxicol. , vol.15 , pp. 1445-1450
    • Doorn, J.A.1    Petersen, D.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.