Effects of phenol and meta-cresol depletion on insulin analog stability at physiological temperature

Journal of Pharmaceutical Sciences

Volumn 103, Issue 8, 2014, Pages 2255-2267

  Teska, Brandon M ^a   Alarcõn, Javier ^b   Pettis, Ronald J ^b   Randolph, Theodore W ^c   Carpenter, John F ^a  

^a UNIVERSITY OF COLORADO   (United States)

^b BD Technologies   (United States)

^c University of Colorado at Boulder   (United States)

Author keywords

drug excipient interaction; excipients; peptides; protein aggregation; protein formulation; proteins; self assembly; stability; stabilization

Indexed keywords

DIMER; DRUG PRESERVATIVE; INSULIN ASPART; INSULIN GLULISINE; INSULIN LISPRO; META CRESOL; MONOMER; PHENOL; 3-CRESOL; ANTIDIABETIC AGENT; CRESOL; EXCIPIENT; INSULIN; PROTEIN AGGREGATE;

ARTICLE; ATOMIC ABSORPTION SPECTROMETRY; CONTROLLED STUDY; DISSOCIATION; DRUG DEGRADATION; DRUG DOSAGE FORM COMPARISON; DRUG STABILITY; GEL PERMEATION CHROMATOGRAPHY; MOLECULAR WEIGHT; REVERSED PHASE LIQUID CHROMATOGRAPHY; SEDIMENTATION RATE; SEDIMENTATION VELOCITY ULTRACENTRIFUGATION; TEMPERATURE; ULTRACENTRIFUGATION; ANALOGS AND DERIVATIVES; CHEMISTRY;

CRESOLS; DRUG STABILITY; EXCIPIENTS; HYPOGLYCEMIC AGENTS; INSULIN; INSULIN ASPART; INSULIN LISPRO; PHENOL; PROTEIN AGGREGATES; TEMPERATURE;

EID: 84905087622     PISSN: 00223549     EISSN: 15206017     Source Type: Journal    
DOI: 10.1002/jps.24039     Document Type: Article

References (70)

1. Pocker Y, Biswas SB,. 1981. Self-association of insulin and the role of hydrophobic bonding: A thermodynamic model of insulin dimerization. Biochemistry 20 (15): 4354-4361.
2. Huus K, Havelund S, Olsen HB, Van De Weert M, Frokjaer S., 2005. Thermal dissociation and unfolding of insulin. Biochemistry 44 (33): 11171-11177.
3. Brange J, Andersen L, Laursen ED, Meyn G, Rasmussen E., 1997. Toward understanding insulin fibrillation. J Pharm Sci 86 (5): 517-525.
4. Kaarsholm NC, Ko HC, Dunn MF., 1989. Comparison of solution structural flexibility and zinc binding domains for insulin, proinsulin, and miniproinsulin. Biochemistry 28 (10): 4427-4435.
5. Derewenda U, Derewenda Z, Dodson GG, Hubbard RE, Korber F., 1989. Molecular structure of insulin: The insulin monomer and its assembly. Br Med Bull 45 (1): 4-18.
6. Wollmer A, Rannefeld B, Johansen BR, Hejnaes KR, Balschmidt P, Hansen FB,. 1987. Phenol-promoted structural transformation of insulin in solution. Biol Chem Hoppe Seyler 368 (8): 903.
7. Rahuel-Clermont S, French CA, Kaarsholm NC, Dunn MF., 1997. Mechanisms of stabilization of the insulin hexamer through allosteric ligand interactions. Biochemistry 36 (19): 5837-5845.
8. Whittingham JL, Edwards DJ, Antson AA, Clarkson JM, Dodson GG., 1998. Interactions of phenol and m-cresol in the insulin hexamer, and their effect on the association properties of B28 pro->asp insulin analogues. Biochemistry 37 (33): 11516-11523.
9. Derewenda U, Derewenda Z, Dodson EJ, Dodson GG, Reynolds CD, Smith GD, Sparks C, Swenson D., 1989. Phenol stabilizes more helix in a new symmetrical zinc insulin hexamer. Nature 338 (6216): 594-596.
10. Krüger P, Gilge G, Çabuk Y, Wollmer A., 2009. Cooperativity and intermediate states in the t to r-structural transformation of insulin. Biol Chem Hoppe Seyler 371 (2): 669-674.
11. Brader ML, Kaarsholm NC, Lee Robert WK, Dunn MF., 1991. Characterization of the r-state insulin hexamer and its derivatives. The hexamer is stabilized by heterotropic ligand binding interactions. Biochemistry 30 (27): 6636-6645.
12. Choi WE, Brader ML, Aguilar V, Kaarsholm NC, Dunn MF., 1993. Allosteric transition of the insulin hexamer is modulated by homotropic and heterotropic interactions. Biochemistry 32 (43): 11638-11645.
13. Bloom CR, Wu N, Dunn A, Kaarsholm NC, Dunn MF., 1998. Comparison of the allosteric properties of the co (ii)-and zn (ii)-substituted insulin hexamers. Biochem 37 (31): 10937-10944.
14. Brange J, Owens DR, Kang S, Vølund A., 1990. Monomeric insulins and their experimental and clinical implications. Diabetes Care 13 (9): 923-954.
15. Nielsen L, Frokjaer S, Brange J, Uversky VN, Fink AL., 2001. Probing the mechanism of insulin fibril formation with insulin mutants. Biochemistry 40 (28): 8397-8409.
16. Phillips NB, Whittaker J, Ismail-Beigi F, Weiss MA., 2012. Insulin fibrillation and protein design: Topological resistance of single-chain analogs to thermal degradation with application to a pump reservoir. J Diabetes Sci Technol 6 (2): 277-288.
17. Brange J, Langkjaer L,. 1992. Chemical stability of insulin. 3. Influence of excipients, formulation, and pH. Acta Pharm Nord 4 (3): 149.
18. Vajo Z, Duckworth WC,. 2000. Genetically engineered insulin analogs: Diabetes in the new millenium. Pharmacol Rev 52 (1): 1-10.
19. Brange J,. 1997. The new era of biotech insulin analogues. Diabetologia 40: 48-53.
20. Brange J, Vølund A., 1999. Insulin analogs with improved pharmacokinetic profiles. Adv Drug Deliv Rev 35 (2-3): 307-335.
21. Brems DN, Alter LA, Beckage MJ, Chance RE, Di Marchi RD, Green LK, Long HB, Pekar AH, Shields JE, Frank BH., 1992. Altering the association properties of insulin by amino acid replacement. Protein Eng 5 (6): 527-533.
22. B29-human insulin. Structure 3 (6): 615-622.
23. B29-insulin: Dissociation of a protein-ligand complex. Protein Sci 5 (12): 2521-2531.
24. Bode BW,. 2011. Comparison of pharmacokinetic properties, physicochemical stability, and pump compatibility of 3 rapid-acting insulin analogues-aspart, lispro, and glulisine. Endocr Pract 17 (2): 271-280.
25. Anderson JH, Brunelle RL, Koivisto VA, Trautmann ME, Vignati L, Di Marchi R., 1997. Improved mealtime treatment of diabetes mellitus using an insulin analogue. Clin Ther 19 (1): 62-72.
26. Richards JP, Stickelmeyer MP, Flora DB, Chance RE, Frank BH, DeFelippis MR., 1998. Self-association properties of monomeric insulin analogs under formulation conditions. Pharm Res 15 (9): 1434-1441.
27. Lougheed WD, Zinman B, Strack TR, Janis LJ, Weymouth AB, Bernstein EA, Korbas AM, Frank BH., 1997. Stability of insulin lispro in insulin infusion systems. Diabetes Care 20 (7): 1061-1065.
28. B28 human insulin) derivatives formed in pharmaceutical solutions. Pharm Res 19 (5): 621-628.
29. Becker RHA,. 2007. Insulin glulisine complementing basal insulins: A review of structure and activity. Diabetes Technol Ther 9 (1): 109-121.
30. Woods RJ, Alarcõn J, McVey E, Pettis RJ., 2012. Intrinsic fibrillation of fast-acting insulin analogs. J Diabetes Sci Technol 6 (2): 265.
31. Strauss K, De Gols H, Hannet I, Partanen TM, Frid A., 2002. A pan-European epidemiologic study of insulin injection technique in patients with diabetes. Pract Diabetes Int 19 (3): 71-76.
32. Bode BW, Gross TM, Thornton KR, Mastrototaro JJ., 1999. Continuous glucose monitoring used to adjust diabetes therapy improves glycosylated hemoglobin: A pilot study. Diabetes Res Clin Pract 46 (3): 183-190.
33. Kaufman FR, Gibson LC, Halvorson M, Carpenter S, Fisher LK, Pitukcheewanont P., 2001. A pilot study of the continuous glucose monitoring system. Diabetes Care 24 (12): 2030.
34. Klonoff DC,. 2005. Continuous glucose monitoring. Diabetes Care 28 (5): 1231.
35. Melberg SG, Havelund S, Villumsen J, Brange J., 1988. Insulin compatibility with polymer materials used in external pump infusion systems. Diabet Med 5 (3): 243-247.
36. James DE, Jenkins AB, Kraegen EW, Chisholm DJ., 1981. Insulin precipitation in artificial infusion devices. Diabetologia 21 (6): 554-557.
37. Schade DS, Eaton RP, DeLongo J, Saland LC, Ladman AJ, Carlson GA., 1982. Electron microscopy of insulin precipitates. Diabetes Care 5 (1): 25-30.
38. Brennan JR, Gebhart SS, Blackard WG., 1985. Pump-induced insulin aggregation. A problem with the Biostator. Diabetes 34 (4): 353-359.
39. Feingold V, Jenkins AB, Kraegen EW., 1984. Effect of contact material on vibration-induced insulin aggregation. Diabetologia 27 (3): 373-378.
40. Selam JL, Zirinis P, Mellet M, Mirouze J., 1987. Stable insulin for implantable delivery systems: In vitro studies with different containers and solvents. Diabetes Care 10 (3): 343-347.
41. Mecklenburg RS, Guinn TS., 1985. Complications of insulin pump therapy: The effect of insulin preparation. Diabetes Care 8 (4): 367.
42. Pryce R,. 2009. Diabetic ketoacidosis caused by exposure of insulin pump to heat and sunlight. BMJ 338.
43. Wright AW, Little JA., 1998. Cannula occlusion with use of insulin lispro and insulin infusion system. Diabetes Care 21 (5): 874-875.
44. Wolpert HA, Faradji RN, Bonner-Weir S, Lipes MA., 2002. Metabolic decompensation in pump users due to lispro insulin precipitation. BMJ 324: 1253.
45. Martindale H, Marsh J, Hallett FR, Albisser AM., 1982. Examination of insulin formulations using quasi-elastic light scattering. Diabetes 31 (4): 364-366.
46. Guilhem I, Leguerrier AM, Lecordier F, Poirier JY, Maugendre D., 2006. Technical risks with subcutaneous insulin infusion. Diabetes Metab 32 (3): 279-284.
47. Renner R, Pfutzner A, Trautmann M, Harzer O, Sauter K, Landgraf R., 1999. Use of insulin lispro in continuous subcutaneous insulin infusion treatment. Results of a multicenter trial. German Humalog-CSII study group. Diabetes Care 22 (5): 784-788.
48. Lougheed WD, Woulfe-Flanagan H, Clement JR, Albisser AM., 1980. Insulin aggregation in artificial delivery systems. Diabetologia 19 (1): 1-9.
49. Kerr D, Morton J, Whately-Smith C, Everett J, Begley JP., 2008. Laboratory-based non-clinical comparison of occlusion rates using three rapid-acting insulin analogs in continuous subcutaneous insulin infusion catheters using low flow rates. J Diabetes Sci Technol 2 (3): 450-455.
50. Chantelau E, Lange G, Gasthaus M, Boxberger M, Berger M., 1987. Interaction between plastic catheter tubings and regular insulin preparations used for continuous subcutaneous insulin-infusion therapy. Diabetes Care 10 (3): 348.
51. De Felippis MR, Bell MA, Heyob JA, Storms SM., 2006. In vitro stability of insulin lispro in continuous subcutaneous insulin infusion. Diabetes Technol Ther 8 (3): 358-368.
52. Teska BM,. 2011. Unpublished observations.
53. Humalog [package insert]. 2011. Eli Lilly and Company.
54. Novolog [package insert]. 2009. Novo Nordisk Inc.
55. Apidra [package insert]. 2009. Sanofi-Aventis LLC US.
56. Jiskoot W,. 2011. Personal communication.
57. Tantipolphan R, Romeijn S, Engelsman J, Torosantucci R, Rasmussen T, Jiskoot W., 2010. Elution behavior of insulin on high-performance size exclusion chromatography at neutral pH. J Pharm Biomed Anal 52 (2): 195-202.
58. Stafford III WF,. 1992. Boundary analysis in sedimentation transport experiments: A procedure for obtaining sedimentation coefficient distributions using the time derivative of the concentration profile. Anal Biochem 203 (2): 295-301.
59. B29-insulin hexamers: A comparison study. Pharm Res 14 (1): 25-36.
60. Schuck P,. 2000. Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling. Biophys J 78 (3): 1606-1619.
61. Beckman-Coulter. 2001. Chemical resistances for Beckman-Coulter centrifugation products. Accessed May 1, 2014, at: https://www.beckmancoulter. com/wsrportal/bibliography?docname=chemres.pdf.
62. Beckman-Coulter. 2011. An-50Ti and An-60Ti analytical rotor, cells, and counterbalance. Accessed May 1, 2014, at: https://www.beckmancoulter.com/ wsrportal/techdocs?docname=LXLA-TB-003. pp 3-2.
63. Brange J., 1994. Stability of insulin: Studies on the physical and chemical stability of insulin in pharmaceutical formulation. Kluwer Academic Pub.
64. Dunn MF,. 2005. Zinc-ligand interactions modulate assembly and stability of the insulin hexamer-A review. Biometals 18 (4): 295-303.
65. Brange J,. 1992. Chemical stability of insulin. 4. Mechanisms and kinetics of chemical transformations in pharmaceutical formulation. Acta Pharm Nord 4 (4): 209-222.
66. Olsen HB, Ludvigsen S, Kaarsholm NC., 1996. Solution structure of an engineered insulin monomer at neutral pH. Biochemistry 35 (27): 8836-8845.
67. Ludvigsen S, Roy M, Thoegersen H, Kaarsholm NC., 1994. High-resolution structure of an engineered biologically potent insulin monomer, B16 Tyr.fwdarw. His, as determined by nuclear magnetic resonance spectroscopy. Biochemistry 33 (26): 7998-8006.
68. Carpenter JF, Randolph TW, Jiskoot WIM, Crommelin DJA, Middaugh CR, Winter G, Fan Y-X, Kirshner S, Verthelyi D, Kozlowski S, Clouse KA, Swann PG, Rosenberg A, Cherney B,. 2008. Overlooking subvisible particles in therapeutic protein products: Gaps that may compromise product quality. J Pharm Sci 98 (4): 1201-1205.
69. Simler BR, Hui G, Dahl JE, Perez-Ramirez B., 2012. Mechanistic complexity of subvisible particle formation: Links to protein aggregation are highly specific. J Pharm Sci 101 (11): 4140-4154.
70. Heavner GA, Arakawa T, Philo JS, Calmann MA, Labrenz S., 2007. Protein isolated from biopharmaceutical formulations cannot be used for comparative studies: Follow-up to "a case study using Epoetin Alfa from Epogen and EPREX." J Pharm Sci 96 (12): 3214-3225.