Characterization of physiochemical and biological properties of an insulin/lauryl sulfate complex formed by hydrophobic ion pairing

International Journal of Pharmaceutics

Volumn 336, Issue 1, 2007, Pages 58-66

  Dai, Wei Guo ^a   Dong, Liang C ^a  

^a ALZA CORPORATION   (United States)

Author keywords

Hydrophobic ion pairing; In vivo bioactivity; Insulin complex; Protein structure

Indexed keywords

DODECYL SULFATE SODIUM; OCTANOL; RECOMBINANT HUMAN INSULIN;

ANIMAL EXPERIMENT; ARTICLE; CIRCULAR DICHROISM; COMPLEX FORMATION; CONTROLLED STUDY; DRUG ACTIVITY; FEMALE; GLUCOSE BLOOD LEVEL; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HYDROPHOBICITY; INFRARED SPECTROSCOPY; ISOTHERMAL TITRATION CALORIMETRY; LIPOPHILICITY; MALE; NONHUMAN; PHYSICAL CHEMISTRY; PRIORITY JOURNAL; RAT; STOICHIOMETRY;

1-OCTANOL; ANIMALS; AREA UNDER CURVE; BLOOD GLUCOSE; CALORIMETRY, DIFFERENTIAL SCANNING; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; CIRCULAR DICHROISM; FEMALE; HYDROPHOBICITY; INSULIN; MALE; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; RATS; RATS, SPRAGUE-DAWLEY; SODIUM DODECYL SULFATE; SOLUBILITY; SPECTROSCOPY, FOURIER TRANSFORM INFRARED;

EID: 34047249414     PISSN: 03785173     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ijpharm.2006.11.035     Document Type: Article

References (45)

1. Adjei A., Rao S., Garren J., Menon G., and Vadnere M. Effect of ion-pairing on 1-octanol-water partitioning of peptide drugs. I: the nonapeptide leuprolide acetate. Int. J. Pharm. 90 (1993) 141-149
2. Anderberg E.K., and Artursson P. Epithelial transport of drugs in cell culture. VIII: effects of sodium dodecyl sulfate on cell membrane and tight junction permeability in human intestinal epithelial (Caco-2) cells. J. Pharm. Sci. 82 (1993) 392-398
3. Anderberg E.K., Lindmark T., and Artursson P. Sodium caprate elicits dilatations in human intestinal tight junctions and enhances drug absorption by the paracellular route. Pharm. Res. 10 (1993) 857-864
4. Aungst B.J., and Hussain M.A. Sustained propranolol delivery and increased oral bioavailability in dogs given a propranolol Laurate salt. Pharm. Res. 9 (1992) 1507-1509
5. Baker E.N., Blundell T.L., Cutfield J.F., Cutfield S.M., Dodson E.J., Dodson G.G., Hodgkin D.M., Hubbard R.E., Isaacs N.W., and Reynolds C.D. The structure of 2Zn pig insulin crystals at 1.5 A resolution. Philos. Trans. R. Soc. Lond., Ser. B, Biol. Sci. 319 (1988) 369-456
6. Byler D.M., Brouillette J.N., and Susi H. Quantitative studies of protein structure by FT-IR spectral deconvolution and curve fitting. Spectroscopy 1 (1986) 29-32
7. Cabiaux V., Goormaghtigh E., Wattiez R., Falmagne P., and Ruysschaert J.M. Secondary structure changes of diphtheria toxin interacting with asolectin liposomes: an infrared spectroscopy study. Biochimie 71 (1989) 153-158
8. Choi S.H., and Park T.G. Hydrophobic ion pair formation between leuprolide and sodium oleate for sustained release from biodegradable polymeric microspheres. Int. J. Pharm. 203 (2000) 193-202
9. Chung H., Kim J., Um J.Y., Kwon I.C., and Jeong S.Y. Self-assembled "nanocubicle" as a carrier for peroral insulin delivery. Diabetologia 45 (2002) 448-451
10. Dong A., Huang P., and Caughey W.S. Protein secondary structures in water from second-derivative amide I infrared spectra. Biochemistry 29 (1990) 3303-3308
11. Dong A., Prestrelski S.J., Allison S.D., and Carpenter J.F. Infrared spectroscopic studies of lyophilization- and temperature-induced protein aggregation. J. Pharm. Sci. 84 (1995) 415-424
12. Dong A., Meyer J.D., Brown J.L., Manning M.C., and Carpenter J.F. Comparative Fourier transform infrared and circular dichroism spectroscopic analysis of a 1-proteinase inhibitor and ovalbumin in aqueous solution. Arch. Biochem. Biophys. 383 (2000) 148-155
13. Ettinger M.J., and Timasheff S.N. Optical activity of insulin. I. On the nature of the circular dichroism bands. Biochemistry 10 (1971) 824-831
14. Falk R., Randolph T.W., Meyer J.D., Kelly R.M., and Manning M.C. Controlled release of ionic compounds from poly(l-lactide) microspheres produced by precipitation with a compressed antisolvent. J. Control. Rel. 44 (1997) 77-85
15. Garrett R.H., and Grisham C.M. Biochemistry (1995), Harcourt Brace College Publishers
16. Haris P.I., and Chapman D. Analysis of polypeptide and protein structures using Fourier transform infrared spectroscopy. Meth. Mol. Biol. 22 (1994) 183-202
17. Hegg P.O. Precipitation of egg white proteins below their isoelectric points by sodium dodecyl sulfate and temperature. Biochim. Biophys. Acta 579 (1979) 73-87
18. Kendrick B.S., Meyer J.D., Matsuura J.E., Carpenter J.F., and Manning M.C. Hydrophobic ion pairing as a method for enhancing structure and activity of lyophilized subtilisin BPN' suspended in isooctane. Arch. Biochem. Biophys. 347 (1997) 113-118
19. Kim A., Yun M.-O., Oh Y.-K., Ahn W.-S., and Kim C.-K. Pharmacodynamics of insulin in polyethylene glycol-coated liposomes. Int. J. Pharm. 180 (1999) 75-81
20. Lee V.H., Yamamoto A., and Kompella U.B. Mucosal penetration enhancers for facilitation of peptide and protein drug absorption. Crit. Rev. Ther. Drug Carrier Syst. 8 (1991) 91-192
21. Lengsfeld C.S., Pitera D., Manning M., and Randolph T.W. Dissolution and partitioning behavior of hydrophobic ion-paired compounds. Pharm. Res. 19 (2002) 1572-1576
22. Matsuura J., Powers M.E., Manning M.C., and Shefter E. Structure and stability of insulin dissolved in 1-octanol. J. Am. Chem. Soc. 115 (1993) 1261-1264
23. Melberg S.G., and Johnson Jr. W.C. Changes in secondary structure follow the dissociation of human insulin hexamers: a circular dichroism study. Proteins: Struct., Funct. Genet. 8 (1990) 280-286
24. Meyer J.D., and Manning M.C. Hydrophobic ion pairing: altering the solubility properties of biomolecules. Pharm. Res. 15 (1998) 188-193
25. Meyer J.D., Matsuura J.E., Kendrick B.S., Evans E.S., Evans G.J., and Manning M.C. Solution behavior of a-chymotrypsin dissolved in nonpolar organic solvents via hydrophobic ion pairing. Biopolymers 35 (1995) 451-456
26. Meyer J.D., Kendrick B.S., Matsuura J.E., Ruth J.A., Bryan P.N., and Manning M.C. Generation of soluble and active subtilisin and a-chymotrypsin in organic solvents via hydrophobic ion pairing. Int. J. Pept. Protein Res. 47 (1996) 177-181
27. Niwa T., Takeuchi H., Hino T., Kunou N., and Kawashima Y. Preparations of biodegradable nanospheres of water-soluble and insoluble drugs with dl-lactide/glycolide copolymer by a novel spontaneous emulsification solvent diffusion method, and the drug release behavior. J. Control. Rel. 25 (1993) 89-98
28. Niwa T., Takeuchi H., Hino T., Kunou N., and Kawashima Y. In vitro drug release behavior of d,l-lactide/glycolide copolymer (PLGA) nanospheres with nafarelin acetate prepared by a novel spontaneous emulsification solvent diffusion method. J. Pharm. Sci. 83 (1994) 727-732
29. Paradkar V.M., and Dordick J.S. Aqueous-like activity of a-chymotrypsin dissolved in nearly anhydrous organic solvents. J. Am. Chem. Soc. 116 (1994) 5009-5010
30. Paradkar V.M., and Dordick J.S. Mechanism of extraction of chymotrypsin into isooctane at very low concentrations of aerosol OT in the absence of reversed micelles. Biotechnol. Bioeng. 43 (1994) 529-540
31. Pikal M.J., and Rigsbee D.R. The stability of insulin in crystalline and amorphous solids: observation of greater stability for the amorphous form. Pharm. Res. 14 (1997) 1379-1387
32. Powers M.E., Matsuura J., Brassell J., Manning M.C., and Shefter E. Enhanced solubility of proteins and peptides in nonpolar solvents through hydrophobic ion pairing. Biopolymers 33 (1993) 927-932
33. Quintanar-Guerrero D., Allemann E., Fessi H., and Doelker E. Applications of the ion-pair concept to hydrophilic substances with special emphasis on peptides. Pharm. Res. 14 (1997) 119-127
34. Sergeeva M.V., Paradkar V.M., and Dordick J.S. Peptide synthesis using proteases dissolved in organic solvents. Enzyme Micro. Technol. 20 (1997) 623-628
35. Susi H., and Byler D.M. Resolution-enhanced Fourier transform infrared spectroscopy of enzymes. Meth. Enzymol. 130 (1986) 290-311
36. Van Stokkum I.H.M., Spoelder H.J.W., Bloemendal M., Van Grondelle R., and Groen F.C.A. Estimation of protein secondary structure and error analysis from circular dichroism spectra. Anal. Biochem. 191 (1990) 110-118
37. Varshosaz J., Sadrai H., and Alinagari R. Nasal delivery of insulin using chitosan microspheres. J. Microencapsul. 21 (2004) 761-774
38. Varshosaz J., Sadrai H., and Heidari A. Nasal delivery of insulin using bioadhesive chitosan gels. Drug Deliv. 13 (2006) 31-38
39. Vecchio G., Bossi A., Pasta P., and Carrea G. Fourier-transform infrared conformational study of bovine insulin in surfactant solutions. Int. J. Pept. Protein Res. 48 (1996) 113-117
40. Wang L.Y., Ma J.K., Pan W.F., Toledo-Velasquez D., Malanga C.J., and Rojanasakul Y. Alveolar permeability enhancement by oleic acid and related fatty acids: evidence for a calcium-dependent mechanism. Pharm. Res. 11 (1994) 513-517
41. Wangikar P.P., Michels P.C., Clark D.S., and Dordick J.S. Structure and function of subtilisin BPN' solubilized in organic solvents. J. Am. Chem. Soc. 119 (1997) 70-76
42. Wei J.A., Lin Y.Z., Zhou J.M., and Tsou C.L. FTIR studies of secondary structures of bovine insulin and its derivatives. Biochim. Biophy. Acta 1080 (1991) 29-33
43. Yamakawa I., Tsushima Y., Machida R., and Watanabe S. Preparation of neurotensin analogue-containing poly(dl-lactic acid) microspheres formed by oil-in-water solvent evaporation. J. Pharm. Sci. 81 (1992) 899-903
44. Yoo H.S., and Park T.G. Biodegradable nanoparticles containing protein-fatty acid complexes for oral delivery of salmon calcitonin. J. Pharm. Sci. 93 (2004) 488-495
45. Yoo H.S., Choi H.K., and Park T.G. Protein-fatty acid complex for enhanced loading and stability within biodegradable nanoparticles. J. Pharm. Sci. 90 (2001) 194-201