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Volumn 99, Issue 10, 2010, Pages 4162-4173

Kinetics of aspartic acid isomerization and enantiomerization in model aspartyl tripeptides under forced conditions

Author keywords

Aspartic acid; Aspartyl peptide; Capillary electrophoresis; Deamidation; Enantiomerization; Isoaspartic acid; Isomerization; Kinetics; Peptides; Stability

Indexed keywords

ASPARAGINE; ASPARTIC ACID; ASPARTIC ACID DERIVATIVE; SUCCINIMIDE; TRIPEPTIDE;

EID: 77957372613     PISSN: 00223549     EISSN: 15206017     Source Type: Journal    
DOI: 10.1002/jps.22134     Document Type: Article
Times cited : (19)

References (37)
  • 3
    • 37049082534 scopus 로고
    • Kinetics and mechanism of the reversible isomerization of aspartic-acid residues in tetrapeptides
    • Capasso S, Kirby AJ, Salvadori S, Sica F, Zagari A. 1995. Kinetics and mechanism of the reversible isomerization of aspartic-acid residues in tetrapeptides. J Chem Soc Perkin Trans 2:437-442.
    • (1995) J Chem Soc Perkin Trans , vol.2 , pp. 437-442
    • Capasso, S.1    Kirby, A.J.2    Salvadori, S.3    Sica, F.4    Zagari, A.5
  • 4
    • 0024516367 scopus 로고
    • Succinimide formation from aspartyl and asparaginyl peptides as a model for the spontaneous degradation of proteins
    • Stephenson RC, Clarke S. 1989. Succinimide formation from aspartyl and asparaginyl peptides as a model for the spontaneous degradation of proteins. J Biol Chem 264:6164-6170.
    • (1989) J Biol Chem , vol.264 , pp. 6164-6170
    • Stephenson, R.C.1    Clarke, S.2
  • 5
    • 0023109951 scopus 로고
    • Deamidation, isomerization, and racemization at asparaginyl and aspartyl residues in peptides - Succinimide-linked reactions that contribute to protein-degradation
    • Geiger T, Clarke S. 1987. Deamidation, isomerization, and racemization at asparaginyl and aspartyl residues in peptides - Succinimide-linked reactions that contribute to protein-degradation. J Biol Chem 262:785-794.
    • (1987) J Biol Chem , vol.262 , pp. 785-794
    • Geiger, T.1    Clarke, S.2
  • 6
    • 0028260569 scopus 로고
    • Chemical pathways of peptide degradation. 6. Effect of the primary sequence on the pathways of degradation of aspartyl residues in model hexapeptides
    • Oliyai C, Borchardt RT. 1994. Chemical pathways of peptide degradation. 6. Effect of the primary sequence on the pathways of degradation of aspartyl residues in model hexapeptides. Pharm Res 11:751-758.
    • (1994) Pharm Res , vol.11 , pp. 751-758
    • Oliyai, C.1    Borchardt, R.T.2
  • 7
    • 0025114552 scopus 로고
    • Chemical pathways of peptide degradation. 3. Effect of primary sequence on the pathways of deamidation of asparaginyl residues in hexapeptides
    • Patel K, Borchardt RT. 1990. Chemical pathways of peptide degradation. 3. Effect of primary sequence on the pathways of deamidation of asparaginyl residues in hexapeptides. Pharm Res 7:787-793.
    • (1990) Pharm Res , vol.7 , pp. 787-793
    • Patel, K.1    Borchardt, R.T.2
  • 8
    • 0027463564 scopus 로고
    • Chemical pathways of peptide degradation. 4. Pathways, kinetics, and mechanism of degradation of an aspartyl residue in a model hexapeptide
    • Oliyai C, Borchardt RT. 1993. Chemical pathways of peptide degradation. 4. Pathways, kinetics, and mechanism of degradation of an aspartyl residue in a model hexapeptide. Pharm Res 10:95-102.
    • (1993) Pharm Res , vol.10 , pp. 95-102
    • Oliyai, C.1    Borchardt, R.T.2
  • 9
    • 0034829887 scopus 로고    scopus 로고
    • Neighboring side chain effects on asparaginyl and aspartyl degradation: An ab initio study of the relationship between peptide conformation and backbone NH acidity
    • Radkiewicz JL, Zipse H, Clarke S, Houk KN. 2001. Neighboring side chain effects on asparaginyl and aspartyl degradation: An ab initio study of the relationship between peptide conformation and backbone NH acidity. J Am Chem Soc 123:3499-3506.
    • (2001) J Am Chem Soc , vol.123 , pp. 3499-3506
    • Radkiewicz, J.L.1    Zipse, H.2    Clarke, S.3    Houk, K.N.4
  • 10
    • 33750955290 scopus 로고    scopus 로고
    • Formulation considerations for proteins susceptible to asparagine deamidation and aspartate isomerization
    • Wakankar AA, Borchardt RT. 2006. Formulation considerations for proteins susceptible to asparagine deamidation and aspartate isomerization. J Pharm Sci 95:2321-2336.
    • (2006) J Pharm Sci , vol.95 , pp. 2321-2336
    • Wakankar, A.A.1    Borchardt, R.T.2
  • 11
    • 0023794425 scopus 로고
    • Role of peptide conformation in the rate and mechanism of deamidation of asparaginyl residues
    • Lura R, Schirch V. 1988. Role of peptide conformation in the rate and mechanism of deamidation of asparaginyl residues. Biochemistry 27:7671-7677.
    • (1988) Biochemistry , vol.27 , pp. 7671-7677
    • Lura, R.1    Schirch, V.2
  • 12
    • 0032904703 scopus 로고    scopus 로고
    • Secondary structure and protein deamidation
    • Xie M, Schowen RL. 1999. Secondary structure and protein deamidation. J Pharm Sci 88:8-13.
    • (1999) J Pharm Sci , vol.88 , pp. 8-13
    • Xie, M.1    Schowen, R.L.2
  • 13
    • 0037163034 scopus 로고    scopus 로고
    • The influence of protein structure on the products emerging from succinimide hydrolysis
    • Athmer L, Kindrachuk J, Georges F, Napper S. 2002. The influence of protein structure on the products emerging from succinimide hydrolysis. J Biol Chem 277:30502-30507.
    • (2002) J Biol Chem , vol.277 , pp. 30502-30507
    • Athmer, L.1    Kindrachuk, J.2    Georges, F.3    Napper, S.4
  • 14
    • 0026185519 scopus 로고
    • Deamidation via cyclic imide of asparaginyl peptides: Dependence on salts buffers, and organic solvents
    • Capasso S, Mazzarella L, Zagari A. 1991. Deamidation via cyclic imide of asparaginyl peptides: Dependence on salts buffers, and organic solvents. Pept Res 4:234-238.
    • (1991) Pept Res , vol.4 , pp. 234-238
    • Capasso, S.1    Mazzarella, L.2    Zagari, A.3
  • 15
    • 0024068424 scopus 로고
    • Mechanisms of aspartimide formation: The effects of protecting groups, acid, base, temperature and time
    • Tam JP, Riemen MW, Merrifield RB. 1988. Mechanisms of aspartimide formation: The effects of protecting groups, acid, base, temperature and time. Pept Res 1:6-18.
    • (1988) Pept Res , vol.1 , pp. 6-18
    • Tam, J.P.1    Riemen, M.W.2    Merrifield, R.B.3
  • 16
    • 0029831193 scopus 로고    scopus 로고
    • Accelerated racemization of aspartic acid and asparagine residues via succinimide intermediates: An ab initio theoretical exploration of mechanism
    • Radkiewicz JL, Zipse H, Clarke S, Houk KN. 1996. Accelerated racemization of aspartic acid and asparagine residues via succinimide intermediates: An ab initio theoretical exploration of mechanism. J Am Chem Soc 118:9148-9155.
    • (1996) J Am Chem Soc , vol.118 , pp. 9148-9155
    • Radkiewicz, J.L.1    Zipse, H.2    Clarke, S.3    Houk, K.N.4
  • 18
    • 0036483747 scopus 로고    scopus 로고
    • Racemization of aspartic acid in human proteins
    • Ritz-Timme S, Collins MJ. 2002. Racemization of aspartic acid in human proteins. Ageing Res Rev 1:43-59.
    • (2002) Ageing Res Rev , vol.1 , pp. 43-59
    • Ritz-Timme, S.1    Collins, M.J.2
  • 19
    • 0021118564 scopus 로고
    • In vivo racemization in mammalian proteins
    • Bada JL. 1984. In vivo racemization in mammalian proteins. Methods Enzymol 106:98-115.
    • (1984) Methods Enzymol , vol.106 , pp. 98-115
    • Bada, J.L.1
  • 22
    • 0028177534 scopus 로고
    • Racemization of Asp23 residue affects the aggregation properties of Alzheimer amyloid beta protein analogues
    • Tomiyama T, Asano S, Furiya Y, Shirasawa T, Endo N, Mori H. 1994. Racemization of Asp23 residue affects the aggregation properties of Alzheimer amyloid beta protein analogues. J Biol Chem 269:10205-10208.
    • (1994) J Biol Chem , vol.269 , pp. 10205-10208
    • Tomiyama, T.1    Asano, S.2    Furiya, Y.3    Shirasawa, T.4    Endo, N.5    Mori, H.6
  • 24
    • 0029746662 scopus 로고    scopus 로고
    • Kinetic study of racemization of aspartyl residues in model peptides of alpha-A-crystalline
    • Fujii N, Momose Y, Harada K. 1996. Kinetic study of racemization of aspartyl residues in model peptides of alpha-A-crystalline. Int J Pept Protein Res 48:118-122.
    • (1996) Int J Pept Protein Res , vol.48 , pp. 118-122
    • Fujii, N.1    Momose, Y.2    Harada, K.3
  • 26
    • 0036298751 scopus 로고    scopus 로고
    • The presence of D-beta-aspartic acid-containing peptides in elastic fibers of sun-damaged skin: A potent marker for ultraviolet-induced skin aging
    • Fujii N, Tajima S, Tanaka N, Fujimoto N, Takata T, Shimo-Oka T. 2002. The presence of D-beta-aspartic acid-containing peptides in elastic fibers of sun-damaged skin: A potent marker for ultraviolet-induced skin aging. Biochem Biophys Res Commun 294:1047-1051.
    • (2002) Biochem Biophys Res Commun , vol.294 , pp. 1047-1051
    • Fujii, N.1    Tajima, S.2    Tanaka, N.3    Fujimoto, N.4    Takata, T.5    Shimo-Oka, T.6
  • 27
    • 8644223952 scopus 로고    scopus 로고
    • Kinetic study of racemization of aspartyl residues in synthetic elastin peptides
    • Kuge K, Fujii N, Miura Y, Tajima S, Saito T. 2004. Kinetic study of racemization of aspartyl residues in synthetic elastin peptides. Amino Acids 27:193-197.
    • (2004) Amino Acids , vol.27 , pp. 193-197
    • Kuge, K.1    Fujii, N.2    Miura, Y.3    Tajima, S.4    Saito, T.5
  • 28
    • 0034141218 scopus 로고    scopus 로고
    • Collagen fragments in urine derived from bone resorption are highly racemized and isomerized: A biological clock of protein aging with clinical potential
    • Cloos PA, Fledelius C. 2000. Collagen fragments in urine derived from bone resorption are highly racemized and isomerized: A biological clock of protein aging with clinical potential. Biochem J 345:473-480.
    • (2000) Biochem J , vol.345 , pp. 473-480
    • Cloos, P.A.1    Fledelius, C.2
  • 29
    • 0032831446 scopus 로고    scopus 로고
    • Kinetics and mechanism of degradation of klerval, a pseudo-tetrapeptide
    • Won CM, Molnar TE, Windisch VL, McKean RE. 1999. Kinetics and mechanism of degradation of klerval, a pseudo-tetrapeptide. Int J Pharm 190:1-11.
    • (1999) Int J Pharm , vol.190 , pp. 1-11
    • Won, C.M.1    Molnar, T.E.2    Windisch, V.L.3    McKean, R.E.4
  • 30
    • 0242489004 scopus 로고    scopus 로고
    • Analysis of aspartyl peptide degradation products by high-performance liquid chromatography and high-performance liquid chromatography-mass spectrometry
    • De Boni S, Oberthür C, Hamburger M, Scriba GKE. 2004. Analysis of aspartyl peptide degradation products by high-performance liquid chromatography and high-performance liquid chromatography-mass spectrometry. J Chromatogr A 1022:95-102.
    • (2004) J Chromatogr A , vol.1022 , pp. 95-102
    • De Boni, S.1    Oberthür, C.2    Hamburger, M.3    Scriba, G.K.E.4
  • 31
    • 33845207781 scopus 로고    scopus 로고
    • Capillary electrophoresis analysis of hydrolysis, isomerization and enantiomerization of aspartyl model tripeptides in acidic and alkaline solution
    • De Boni S, Scriba GKE. 2007. Capillary electrophoresis analysis of hydrolysis, isomerization and enantiomerization of aspartyl model tripeptides in acidic and alkaline solution. J Pharm Biomed Anal 43:49-56.
    • (2007) J Pharm Biomed Anal , vol.43 , pp. 49-56
    • De Boni, S.1    Scriba, G.K.E.2
  • 32
    • 35349028965 scopus 로고    scopus 로고
    • The role of the cyclic imide in alternate degradation pathways for asparagine-containing peptides and proteins
    • DeHart MP, Anderson BD. 2007. The role of the cyclic imide in alternate degradation pathways for asparagine-containing peptides and proteins. J Pharm Sci 96:2667-2685.
    • (2007) J Pharm Sci , vol.96 , pp. 2667-2685
    • DeHart, M.P.1    Anderson, B.D.2
  • 33
    • 0018623326 scopus 로고
    • Formation of aminosuccinyl peptides during acidolytic deprotection followed by their transformation to piperazine-2,5-dione derivatives in neutral media
    • Schön I, Kisfaludy L. 1979. Formation of aminosuccinyl peptides during acidolytic deprotection followed by their transformation to piperazine-2,5-dione derivatives in neutral media. Int J Pept Protein Res 14:485-494.
    • (1979) Int J Pept Protein Res , vol.14 , pp. 485-494
    • Schön, I.1    Kisfaludy, L.2
  • 34
    • 0030196598 scopus 로고    scopus 로고
    • A relative weighting method for estimating parameters and variances in multiple data sets
    • Bell BM, Burke JV, Schumitzky A. 1996. A relative weighting method for estimating parameters and variances in multiple data sets. Comput Stat Data Anal 22:119-135.
    • (1996) Comput Stat Data Anal , vol.22 , pp. 119-135
    • Bell, B.M.1    Burke, J.V.2    Schumitzky, A.3
  • 35
    • 0033613646 scopus 로고    scopus 로고
    • Predicting protein decomposition: The case of aspartic-acid racemization kinetics
    • Collins MJ, Waite ER, van Duin ACT. 1999. Predicting protein decomposition: The case of aspartic-acid racemization kinetics. Philos Trans R Soc B 354:51-64.
    • (1999) Philos Trans R Soc B , vol.354 , pp. 51-64
    • Collins, M.J.1    Waite, E.R.2    Van Duin, A.C.T.3
  • 36
    • 33645470859 scopus 로고    scopus 로고
    • Effect of N-1 and N-2 residues on peptide deamidation rate in solution and solid state
    • Li B, Schowen RL, Topp EM, Borchardt RT. 2006. Effect of N-1 and N-2 residues on peptide deamidation rate in solution and solid state. AAPS J 8:E166-E173.
    • (2006) AAPS J , vol.8
    • Li, B.1    Schowen, R.L.2    Topp, E.M.3    Borchardt, R.T.4
  • 37
    • 0025788030 scopus 로고
    • Effects of amino acid sequence, buffers, and ionic strength on the rate and mechanism of deamidation of asparagine residues in small peptides
    • Tyler-Cross R, Schirch V. 1991. Effects of amino acid sequence, buffers, and ionic strength on the rate and mechanism of deamidation of asparagine residues in small peptides. J Biol Chem 266:22549-22556.
    • (1991) J Biol Chem , vol.266 , pp. 22549-22556
    • Tyler-Cross, R.1    Schirch, V.2


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