The effects of alpha-helix on the stability of Asn residues: Deamidation rates in peptides of varying helicity

Protein Science

Volumn 8, Issue 11, 1999, Pages 2519-2523

  Kosky, Andrew A ^a   Razzaq, Ursula O ^a   Treuheit, Michael J ^a   Brems, David N ^a  

^a AMGEN INC   (United States)

Author keywords

Deamidation; Peptides; Succinimide; helicity

Indexed keywords

OCTAPEPTIDE; SUCCINIMIDE;

ALPHA HELIX; AMINO ACID SUBSTITUTION; ARTICLE; CIRCULAR DICHROISM; DEAMINATION; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; PRIORITY JOURNAL; PROTEIN STABILITY; SEQUENCE ANALYSIS; STRUCTURE ANALYSIS;

EID: 0032743230     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.8.11.2519     Document Type: Article

References (30)

1. Aswad DW. 1995. Deamidation and isoAsp formation in peptides and proteins. Boca Raton, FL: CRC Press.
2. Baldwin RL. 1995. α-Helix formation by peptides of defined sequence. Biophys Chem 55:127-135.
3. Brennan TV, Clarke S. 1993. Spontaneous degradation of polypeptides at aspartyl and asparaginyl residues: Effects of the solvent dielectric. Protein Sci 2:331-338.
4. Capasso S, Mazzarella L, Sica F, Zagari A. 1989. Deamidation via cyclic imide in asparaginyl peptides. Peptide Res 2:195-200.
5. Capasso S, Mazzarella L, Zagari A. 1991. Deamidation via cyclic imide of asparaginyl peptides: Dependence on salts, buffers and organic solvents. Peptide Res 4:234-238.
6. Chakrabartty A, Kortemme T, Baldwin RL. 1994. Helix propensities of the amino acids measured in Ala-based peptides without helix-stabilizing side-chain interactions. Protein Sci 3:843-852.
7. Chakrabartty A, Kortemme T, Padmanabhan S, Baldwin RL. 1993. Aromatic side-chain contribution to far-ultraviolet circular dichroism of helical peptides and its effects on measurement of helix propensities. Biochemistry 32:5560-5565.
8. Chakrabartty A, Schellman JA, Baldwin RL. 1991. Large differences in the helix propensities of Ala and Gly. Nature 351:586-588.
9. Clarke S. 1987. Propensity for spontaneous succinimide formation from aspartyl and asparaginyl residues in cellular proteins. Int J Peptide Protein Res 30:808-821.
10. Dempsey CE. 1986. pH Dependence of hydrogen exchange from backbone peptide amides in Apamin. Biochemistry 25:3904-3911.
11. Geiger T, Clarke S. 1987. Deamidation, isomerization, and racemization at asparaginyl and aspartyl residues in peptides. J Biol Chem 262:785-794.
12. Kossiakoff AA. 1988. Tertiary structure is a principle determinant to protein deamidation. Science 240:191-194.
13. Lifson S, Roig A. 1961. On the theory of the helix-coil transition in polypeptides. J Chem Phys 34:1963-1974.
14. Manning MC, Patel K, Borchardt RT. 1989. Stability of protein pharmaceuticals. Pharm Res 6:903-918.
15. Marqusee S, Robbins VH, Baldwin RL. 1989. Unusually stable helix formation in short Ala-based peptides. Proc Natl Acad Sci USA 86:5286-5290.
16. Pace CN, Vajdos, F, Fee L, Grimsley G, Gray T. 1995. How to measure and predict the molar absorption coefficient of a protein. Protein Sci 4:2411-2423.
17. Patel K, Borchardt RT. 1990a. Chemical pathways of peptide degradation. II. Kinetics of deamidation of an asparaginyl residue in a model hexapeptide. Pharm Res 7:703-711.
18. Patel K, Borchardt RT. 1990b. Chemical pathways of peptide degradation. III. Effect of primary sequence on the pathways of deamidation of asparaginyl residues in hexapeptides. Pharm Res 7:787-793.
19. Powell MF. 1996. A compendium and hydropathy/flexibility analysis of common reactive sites in proteins: Reactivity at Asn, Asp, Gln, and Met motifs in neutral pH solution. In: Pearlman R, Wang YJ, eds. Formulation, characterization and stability of protein drugs. New York: Plenum Press. pp 1-140.
20. Rohl C, Chakrabartty A, Baldwin RL. 1996. Helix propagation and N-cap propensities of the amino acids measured in Ala-based peptides in 40 volume percent trifluoroethanol. Protein Sci 5:2623-2637.
21. 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.
22. 27 hGRF(1-32)NH2 and its deamidation products by 2D NMR. Int J Peptide Protein Res 42:24-32.
23. Stevenson CL, Friedman AR, Kubiak TM, Donlan ME, Borchardt RT. 1993b. Effect of secondary structure on the rate of deamidation of several growth hormone releasing factor analogs. Int J Peptide Protein Res 42:497-503.
24. Tyler-Cross R, Schirch V. 1991. Effects of amino acid sequence, buffers, and ionic strength on the rate and mechanism of deamidation of Asn residues in small peptides. J Biol Chem 266:22549-22556.
25. Voorter CEM, de Haard-Hoekman WA, van den Oetelaar PJM, Bloemendal H, de Jong WW. 1988. Spontaneous peptide bond cleavage in aging α-crystallin through a succinimide intermediate. J Biol Chem 263:19020-19023.
26. Wagner DS, Melton LG, Yan Y, Erickson BW, Anderegg RJ. 1994. Deuterium exchange of α-helices and α-sheets as monitored by electrospray ionization mass spectrometry. Protein Sci 3:1305-1314.
27. Wearne SJ, Creighton TE. 1989. Effect of protein conformation on the rate of deamidation: Ribonuclease A. Proteins Struct Fund Genet 5:8-12.
28. Wright HT. 1991a. Nonenzymatic deamidation of asparaginyl and glutaminyl residues in proteins. Crit Rev Biochem Mol Biol 26:1-52.
29. Wright HT. 1991b. Sequence and structure determinants of the nonenzymatic deamidation of Asn and glutamine in proteins. Protein Eng 4:283-294.
30. Zimm BH, Bragg JR. 1959. Theory of the phase transition between helix and random coil in polypeptide chains. J Chem Phys 31:526-535.