Development of calcitonin salmon nasal spray: Similarity of peptide formulated in chlorobutanol compared to benzalkonium chloride as preservative

Journal of Pharmaceutical Sciences

Volumn 98, Issue 10, 2009, Pages 3691-3706

  Costantino, Henry R ^a   Culley, Heather ^a   Chen, Lishan ^a   Morris, Daniel ^a   Houston, Michael ^a   Roth, Sharin ^a   Phoenix, Mary Jo ^a   Foerder, Chuck ^a   Philo, John S ^b   Arakawa, Tsutomu ^b   Eidenschink, Lisa ^c   Andersen, Niels H ^c   Brandt, Gordon ^a   Quay, Steven C ^a  

^a Nastech Pharmaceutical Company Inc   (United States)

^b ALLIANCE PROTEIN LABORATORIES   (United States)

^c UNIVERSITY OF WASHINGTON   (United States)

Author keywords

Nasal drug delivery; Nuclear magnetic resonance (NMR) spectroscopy; Physical characterization; Physicochemical properties; Regulatory science; Stability

Indexed keywords

BENZALKONIUM CHLORIDE; CHLORBUTOL; SALCATONIN;

AMINO ACID ANALYSIS; AMINO TERMINAL SEQUENCE; ARTICLE; CIRCULAR DICHROISM; CONTROLLED STUDY; DIFFERENTIAL SCANNING CALORIMETRY; DRUG FORMULATION; DRUG STABILITY; DRUG STORAGE; ENZYME LINKED IMMUNOSORBENT ASSAY; GEL PERMEATION CHROMATOGRAPHY; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; MASS SPECTROMETRY; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; MOLECULAR DYNAMICS; NUCLEAR OVERHAUSER EFFECT; PH MEASUREMENT; PROTEIN CONFORMATION; REVERSED PHASE LIQUID CHROMATOGRAPHY; SEDIMENTATION; TEMPERATURE SENSITIVITY;

EID: 70349247789     PISSN: 00223549     EISSN: 15206017     Source Type: Journal    
DOI: 10.1002/jps.21690     Document Type: Article

References (36)

1. Chirino AJ, Mire-Sluis A. 2004. Characterizing biological products and assessing comparability following manufacturing changes. Nat Biotechnol 22:1383-1391. (Pubitemid 39482857)
2. Deechongkit S, Aoki KH, Park SS, Kerwin BA. 2006. Biophysical comparability of the same protein from different manufacturers: A case study using Epoetin alfa from Epogen and Eprex. J Pharm Sci 95:1931-1943. (Pubitemid 44433025)
3. Galson SK. 2006. FDA response to citizen's petition Docket nos. 2004P-023 11CP1 and SUP 1,2003P-0 1 76lCP 1 and EMC 1, 2004P-0171lCP1, and 2004N- 0355, letter dated 30 May. http://www.fda.gov/ ohrms/dockets/dockets/04P0231/04P-0231- pdn0001.pdf.
4. Rosenberg A. 2006. Effect of protein aggregates: An immunological perspective. AAPS J 8:E501-E507. (Pubitemid 44294011)
5. Rosenberg AS, Worobec A. 2004. A risk-based approach to immunogenicity concerns of therapeutic protein products, Part 1: Considering consequences of the immune response to a protein. Biopharm Int 17:22-26. (Pubitemid 39573552)
6. Casadevall N, Eckardt K-U, Rossert J. 2005. Epoetin-induced autoimmune pure red cell aplasia. J Am Soc Nephrol 16:S67-S69. (Pubitemid 41725087)
7. Niall HD, Keutmann HT, Copp DH, Potts JT. 1969. Amino acid sequence of salmon ultimobranchial calcitonin. Proc Natl Acad Sci USA 64:771-778.
8. Grauer A. 1995. Clinical significance of antibodies against calcitonin. Exp Clin Endocrinol Diabetes 103:345-351.
9. Haddad JG, Caldwell JG. 1972. Calcitonin resistance: Clinical immunological studies in subjects with Paget's disease of bone treated with porcine and salmon calcitonins. J Clin Invest 51:3133-3141.
10. Singer FR, Fredericks RS, Minkin C. 1980. Salmon calcitonin therapy for Paget's disease of bone: The problem of acquired clinical resistance. Arthritis Rheum 23:1148-1154. (Pubitemid 10021691)
11. Bohm G, Muhr G, Jaenicke R. 1992. Quantitative analysis of protein far UV circular dichroism spectra by neural net works. Protein Eng 5:191-195.
12. Braun S, Kalinowski H-O, Berger S. 1998. 150 and more basic NMR experiments. Weinheim, Germany: Wiley-VCH Verlag GmbH.
13. Bax A, Davis DG. 1985. MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy. J Magn Reson 65:355-360.
14. Neidigh JW, Fesinmeyer RM, Prickett KS, Andersen NH. 2001. Exendin-4 and glucagon-like-peptide 1: NMR structural comparisons in the solution and micelle- associated states. Biochemistry 40:13188-13200.
15. Neidigh JW, Fesinmeyer RM, Andersen NH. 2002. Designing a 20-residue protein. Nat Struct Biol 9:425-430.
16. Andersen NH, Olsen KA, Fesinmeyer RM, Tan X, Hudson FM, Eidenschink LA, Farazi SR. 2006. Minimization and optimization of designed b hairpin folds. J Am Chem Soc 128:6101-6110.
17. D'Aquino JA, Gomez J, Hilser VJ, Lee KH, Amzel LM, Freire E. 1996. The magnitude of the backbone conformational entropy change in protein folding. Proteins 25:143-156. (Pubitemid 26231105)
18. Ahrer K, Buchacher A, Iberer G, Jungbauer A. 2006. Thermodynamic stability and formation of aggregates of human immunoglobulin G characterised by differential scanning calorimetry and dynamic light scattering. J Biochem Biophys Methods 66:73-86. (Pubitemid 43254628)
19. Streicher W, Makhatadze GI. 2006. Calorimetric evidence for a two-state unfolding of the β-hairpin peptide Trpzip4. J Am Chem Soc 128:30-31. (Pubitemid 43100834)
20. Schuck P. 2000. Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling. Biophys J 78:1606-1619. (Pubitemid 30141584)
21. Laue TM, Shah BD, Ridgeway TM, Pelletier SL. 1992. Computer-aided interpretation of analytical sedimentation data for proteins. In: Harding SE, Rowe AJ, Horton JC, editors. Analytical ultracentrifugation in biochemistry and polymer science. Cambridge: Royal Society of Chemistry. pp 90-125.
22. Pelton JT, McLean LR. 2000. Spectroscopic methods for analysis of protein secondary structure. Anal Chem 277:167-176. (Pubitemid 30055864)
23. Kelly SM, Jess TJ, Price NC. 2005. How to study proteins by circular dichroism. Biochim Biophys Acta 1751:119-139.
24. Epand RF, Orlowski RC, Epand RM. 2004. The biological potency of a series of analogs of human calcitonin correlates with their interactions with phospholipids. Biopolymers 76:258-265.
25. Andersen NH, Cort J, Liu Z, Sjoberg S, Tong H. 1996. Cold denaturation of monomeric peptide helices. J Am Chem Soc 118:10309-10310. (Pubitemid 26375220)
26. Andersen NH, Neidigh J, Harris SM, Lee GM, Liu Z, Tong H. 1997. Extracting information from the temperature gradients of polypeptide NH chemical shifts: I. The importance of conformational averaging. J Am Chem Soc 119:8547-8561. (Pubitemid 27404581)
27. Vermeer AW, Norde W. 2000. The thermal stability of immunoglobulin: Unfolding and aggregation of a multi-domain protein. Biophys J 78:394-404. (Pubitemid 30207148)
28. Kang F, Singh J. 2003. Conformational stability of a model protein (bovine serum albumin) during primary emulsification process of PLGA microspheres synthesis. Int J Pharm 260:149-156. (Pubitemid 36724869)
29. Cueto M, Dorta MJ, Munguia O, Llabres M. 2003. New approach to stability assessment of protein solution formulations by differential scanning calorimetry. Int J Pharm 252:159-166. (Pubitemid 36126624)
30. Hudson FM, Andersen NH. 2004. Exenatide: NMR/CD evaluation of the medium dependence of conformation and aggregation state. Peptide Sci 4:298-308.
31. Wüthrich K. 1986. NMR of proteins and nucleic acids. New York: John Wiley.
32. Gidding JC. 1993. Field-flow fractionation: Analysis of macromolecular, colloidal and particulate materials. Science 260:1456-1465.
33. Reschiglian P, Zattoni A, Roda B, Michelini E, Roda A. 2005. Field-flow fractionation and biotechnology. Trends Biotechnol 23:475-483.
34. Windisch V, DeLuccia F, DuHau L, Herman F, Mencel JJ, Tang S, Vuilhorgne M. 1997. Degradation pathways of salmon calcitonin in aqueous solution. J Pharm Sci 86:359-364. (Pubitemid 27113772)
35. Findlay DM, Michelangeli VP, Moseley JM, Martin TJ. 1981. Calcitonin binding and degradation by two cultured human breast cancer cell lines (MCF 7 and T 47D). Biochem J 196:513-520.
36. Andreotti G, Mendez BL, Amodeo P, Morelli MA, Nakamuta H, Motta A. 2006. Structural determinants of salmon calcitonin bioactivity: The role of the Leu-based amphipathic alpha-helix. J Biol Chem 281:24193-24203. (Pubitemid 44274193)