Novel pharmaceutical composition of bradykinin potentiating penta peptide with β-cyclodextrin: Physical-chemical characterization and anti-hypertensive evaluation

International Journal of Pharmaceutics

Volumn 336, Issue 1, 2007, Pages 90-98

  Denadai, Ângelo M L ^a   Ianzer, Danielle ^a,b   Alcântara, Antônio Flávio de C ^a   Santoro, Marcelo M ^a   Santos, Cynthia F F ^a   Lula, Ivana Silva ^a   de Camargo, Antônio C M ^b   Faljoni Alario, Adelaide ^c   dos Santos, Robson A S ^a   Sinisterra, Rubén D ^a  

^a FEDERAL UNIVERSITY OF MINAS GERAIS   (Brazil)

^b INSTITUTO BUTANTAN   (Brazil)

^c UNIVERSITY OF SÃO PAULO   (Brazil)

Author keywords

Cyclodextrin; ACE inhibitors; Anti hypertensive activity; Bothrops jararaca; Bradykinin potentiating peptides

Indexed keywords

BATROXOBIN; BETA CYCLODEXTRIN; BRADYKININ POTENTIATING PENTAPEPTIDE 5A; PENTAPEPTIDE; TRYPTOPHAN; UNCLASSIFIED DRUG;

ANIMAL EXPERIMENT; ANTIHYPERTENSIVE ACTIVITY; ARTICLE; CIRCULAR DICHROISM; COMPLEX FORMATION; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; DRUG FORMULATION; ENTROPY; HEART RATE; ISOTHERMAL TITRATION CALORIMETRY; MALE; MEAN ARTERIAL PRESSURE; MOLECULAR INTERACTION; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PHYSICAL CHEMISTRY; PRIORITY JOURNAL; RAT;

ANGIOTENSIN-CONVERTING ENZYME INHIBITORS; ANIMALS; ANTIHYPERTENSIVE AGENTS; BETA-CYCLODEXTRINS; BLOOD PRESSURE; BOTHROPS; CALORIMETRY; CHEMISTRY, PHARMACEUTICAL; CIRCULAR DICHROISM; HEART RATE; MAGNETIC RESONANCE SPECTROSCOPY; MALE; MODELS, MOLECULAR; MOLECULAR STRUCTURE; OLIGOPEPTIDES; RATS; RATS, INBRED SHR; THERMODYNAMICS; VIPER VENOMS;

EID: 34047257335     PISSN: 03785173     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ijpharm.2006.11.040     Document Type: Article

References (51)

1. Brayden D.J., and O'Mahony J.D. Novel oral drug delivery gateways for biotechnology products polypeptides and vaccines. PSTT 1 (1998) 291-299
2. Cramer F., Saenger W., and Spatz H.C. Inclusion compounds. XIX. Formation of inclusion compounds of alpha-cyclodextrin in aqueous solutions. Thermodynamics and kinetics. J. Am. Chem. Soc. 89 (1967) 14-20
3. Cushman D.W., Cheung H.S., Sabo E.F., Rubin B., and Ondetti M.A. Development of specific inhibitors of angiotensin I converting enzyme (kininase II). Fed. Proc. 38 (1979) 2778-2782
4. Cushman D.W., and Ondetti M.A. Inhibitors of angiotensin-converting enzyme. Prog. Med. Chem. 17 (1980) 41-104
5. De Alvarenga E.S., Lima C.F., and Denadai A.M.L. Study of aqueous solution of sodium dodecylsulfate and polyethyleneoxide 10000 by NMR NOESY. Zeit. Nat. Sec. a-a, J. Phys. Sci. 59 (2004) 291-294
6. Dewar M.J.S., Zoebish E.G., Healy E.F., and Stewart J.J.P. Development and use of quantum mechanical molecular models. 76. AM1: a new general purpose quantum mechanical molecular model. J. Am. Chem. Soc. 107 (1985) 3902-3909
7. Dos Santos H.F., Duarte H.A., Sinisterra R.D., Mattos S.V.D., De Oliveira L.F.C., and De Almeida W.B. Quantum-mechanical study of the interaction of alpha-cyclodextrin with methyl mercury chloride. Chem. Phys. Lett. 319 (2000) 569-575
8. Edery H., Rosenthal T., Amitzur G., and Stern N. Blood kinin system in renal hypertensive patients administered with SQ 20881. Adv. Exp. Med. Biol. B 120 (1979) 571-574
9. Ferreira S.H., Bartelt D.C., and Greene L.J. Isolation of bradykinin-potentiating peptides from Bothrops jararaca venom. Biochemistry 9 13 (1970) 2583-2593
10. Ferreira S.H., Greene L.H., Alabaster V.A., Bakhle Y.S., and Vane J.R. Activity of various fractions of bradykinin potentiating factor against angiotensin I converting enzyme. Nature 225 (1970) 379-380
11. Ferreira S.H., and Rocha e Silva M. Potentiation of bradykinin and eledoisin by BPF (bradykinin potentiating factor) from Bothrops jararaca venom. Experientia 21 (1965) 347-349
12. Freer R.J., and Stewart J.M. Alkylating analogs of peptide hormones. 1. Synthesis and properties of p-(N,N-)-bis(2-chloroethyl)aminophenylbutyryl derivatives of bradykinin and bradykinin potentiating factor. J. Med. Chem. 15 (1972) 1-5
13. Frisch M.J., Trucks G.W., Schlegel H.B., Scuseria G.E., Robb M.A., Cheeseman J.R., Montgomery Jr. J.A., Vreven T., Kudin K.N., Burant J.C., Millam J.M., Iyengar S.S., Tomasi J., Barone V., Mennucci B., Cossi M., Scalmani G., Rega N., Petersson G.A., Nakatsuji H., Hada M., Ehara M., Toyota K., Fukuda R., Hasegawa J., Ishida M., Nakajima T., Honda Y., Kitao O., Nakai H., Klene M., Li X., Knox J.E., Hratchian H.P., Cross J.B., Adamo C., Jaramillo J., Gomperts R., Stratmann R.E., Yazyev O., Austin A.J., Cammi R., Pomelli C., Ochterski J.W., Ayala P.Y., Morokuma K., Voth G.A., Salvador P., Dannenberg J.J., Zakrzewski V.G., Dapprich S., Daniels A.D., Strain M.C., Farkas O., Malick D.K., Rabuck A.D., Raghavachari K., Foresman J.B., Ortiz J.V., Cui Q., Baboul A.G., Clifford S., Cioslowski J., Stefanov B.B., Liu G., Liashenko A., Piskorz P., Komaromi I., Martin R.L., Fox D.J., Keith T., Al-Laham M.A., Peng C.Y., Nanayakkara A., Challacombe M., Gill P.M.W., Johnson B., Chen W., Wong M.W., Gonzalez C., and Pople J.A. Gaussian Revision B.04 (2003), Gaussian, Inc., Pittsburgh, PA
14. Greenfield N., and Fasman G.D. Computed circular dichroism spectra for the evaluation of protein conformation. Biochemistry 8 (1969) 4108-4116
15. Halgren T.A. Merck molecular force field. 1. Basis, form, scope, parameterization, and performance of MMFF94. J. Comp. Chem. 17 (1996) 490-519
16. Halgren T.A. Merck molecular force field. 2. MMFF94 van der Waals and electrostatic parameters for intermolecular interactions. J. Comp. Chem. 17 (1996) 520-552
17. Halgren T.A. Merck molecular force field. 3. Molecular geometries and vibrational frequencies for MMFF94. J. Comp. Chem. 17 (1996) 553-586
18. Halgren T.A. Merck molecular force field. 5. Extension of MMFF94 using experimental data, additional computational data, and empirical rules. J. Comp. Chem. 17 (1996) 616-641
19. Halgren T.A. Characterization of MMFF94, MMFF94s, and other widely available force fields for conformational energies and for intermolecular interaction energies and geometries. Abs. Pap. Am. Chem. Soc. 216 (1998) U702-U702
20. Halgren T.A. MMFF VI. MMFF94 option for energy minimization studies. J. Comp. Chem. 20 (1999) 720-729
21. Halgren T.A., and Nachbar R.B. Merck molecular force field. 4. Conformational energies and geometries for MMFF94. J. Comp. Chem. 17 (1996) 587-615
22. Halperin J.L., Faxon D.P., Creager M.A., Bass T.A., Melidossian C.D., Gavras H., and Ryan T.J. Coronary hemodynamic effects of angiotensin inhibition by captopril and teprotide in patients with congestive heart failure. Am. J. Cardiol. 50 (1982) 967-972
23. Hayashi M.A., Murbach A.F., Ianzer D., Portaro F.C., Prezoto B.C., Fernandes B.L., Silveira P.F., Silva C.A., Pires R.S., Britto L.R., Dive V., and Camargo A.C. The C-type natriuretic peptide precursor of snake brain contains highly specific inhibitors of the angiotensin-converting enzyme. J. Neurochem. 85 (2003) 969-977
24. Hedges A.R. Industrial applications of cyclodextrins. Chem. Rev. 98 (1998) 2035-2044
25. Hovgaard L., and Brondsted H. Dextran hydrogels for colon-specific drug-delivery. J. Contr. Rel. 36 (1995) 159-166
26. Ianzer D., Konno K., Marques-Porto R., Vieira Portaro F.C., Stocklin R., Camargo A.C.M., and Pimenta D.C. Identification of five new bradykinin potentiating peptides (BPPs) from Bothrops jararaca crude venom by using electrospray ionization tandem mass spectrometry after a two-step liquid chromatography. Peptides 25 (2004) 1085-1092
27. Irie T., and Uekama K. Cyclodextrins in peptide and protein delivery. Adv. Drug Del. Rev. 36 (1999) 101-123
28. Loftsson T., and Brewster M.E. Pharmaceutical applications of cyclodextrins 1. Drug solubilization and stabilization. J. Pharm. Sci. 85 (1996) 1017-1025
29. ®. Tutorial Guide. www.microcalorimetry.com. The Calorimetry Experts.
30. MicroCal, 1998b. VP-ITC MicroCalorimeter. User's Manual. www.microcalorimetry.com. The Calorimetry ExpertsMicroCal.
31. Morawietz H., Goettsch W., Szibor M., Barton M., Shaw S., Hakim K., Zerkowski H.R., and Holtz J. Angiotensin-converting enzyme inhibitor therapy prevents upregulation of endothelin-converting enzyme-1 in failing human myocardium. Biochem. Biophys. Res. Commun. 295 (2002) 1057-1061
32. Murayama N., Hayashi M.A., Ohi H., Ferreira L.A., Hermann V.V., Saito H., Fujita Y., Higuchi S., Fernandes B.L., Yamane T., and de Camargo A.C. Cloning and sequence analysis of a Bothrops jararaca cDNA encoding a precursor of seven bradykinin-potentiating peptides and a C-type natriuretic peptide. Proc. Natl. Acad. Sci. USA 94 4 (1997 Feb 18) 1189-1193
33. Ng K.K., and Vane J.R. Some properties of angiotensin converting enzyme in the lung in vivo. Nature 225 (1970) 1142-1144
34. Ondetti M.A., Rubin B., and Cushman D.W. Design of specific inhibitors of angiotensin-converting enzyme: new class of orally active antihypertensive agents. Science 196 (1977) 441-444
35. Ondetti M.A., Williams N.J., Sabo E.F., Pluscec J., Weaver E.R., and Kocy O. Angiotensin-converting enzyme inhibitors from the venom of Bothrops jararaca. Isolation, elucidation of structure, and synthesis. Biochemistry 10 22 (1971) 4033-4039
36. Rahman A. One and Two Dimensional NMR Spectroscopy (1989), Elsevier, New York
37. Reed J.R., and Reed T.A. A set of constructed type spectra for the practical estimation of peptide secondary structure from circular dichroism. Anal. Biochem. 254 (1997) 36-40
38. Rekharsky M., and Inoue Y. Chiral recognition thermodynamics of beta-cyclodextrin: the thermodynamic origin of enantioselectivity and the enthalpy-entropy compensation effect. J. Am. Chem. Soc. 122 (2000) 4418-4435
39. Rekharsky M.V., Goldberg R.N., Schwarz F.P., Tewari Y.B., Ross P.D., Yamashoji Y., and Inoue Y. Thermodynamic and nuclear magnetic resonance study of the interactions of alpha-cyclodextrin and beta-cyclodextrin with model substances-phenethylamine, ephedrines, and related substances. J. Am. Chem. Soc. 117 (1995) 8830-8840
40. Rekharsky M.V., and Inoue Y. Complexation thermodynamics of cyclodextrins. Chem. Rev. 98 (1998) 1875-1917
41. Rubinstein A., Tirosh B., Baluom M., Nassar T., David A., Radai R., Gliko-Kabir I., and Friedman M. The rationale for peptide drug delivery to the colon and the potential of polymeric carriers as effective tools. J. Contr. Rel. 46 (1997) 59-73
42. Saenger W. Cyclodextrin inclusion-compounds in research and industry. Ang. Chem. Int. Ed. Engl. 19 (1980) 344-362
43. Schneider H.J., Hacket F., Rudiger V., and Ikeda H. NMR studies of cyclodextrins and cyclodextrin complexes. Chem. Rev. 98 (1998) 1755-1785
44. Sinha V.R., and Kumria R. Polysaccharides in colon-specific drug delivery. Int. J. Pharm. 224 (2001) 19-38
45. Spartan '04 Windows: Tutorial and User's Guide, 2003. W., Inc. 18401 Von karman Avenue, Suite 370, Irvine, CA 92612, USA.
46. Stella V.J., Rao V.M., Zannou E.A., and Zia V. Mechanisms of drug release from cyclodextrin complexes. Adv. Drug Del. Rev. 36 (1999) 3-16
47. Teixeira L.R., Sinisterra R.D., Vieira R.P., Scarlatelli-Lima A., Moraes M.F.D., Doretto M.C., Denadai A.M., and Beraldo H. An inclusion compound of the anticonvulsant sodium valproate into alpha-cyclodextrin: physico-chemical characterization. J. Incl. Phen. Macroc. Chem. 54 (2006) 133-138
48. The Sadtler Standard Spectra, 1972. Sadtlet Research Laboratories.
49. Turnbull W.B., and Daranas A.H. On the value of c: can low affinity systems be studied by isothermal titration calorimetry?. J. Am. Chem. Soc. 125 (2003) 14859-14866
50. Villard E., and Soubrier F. Molecular biology and genetics of the angiotensin-I-converting enzyme: potential implications in cardiovascular diseases. Cardiovasc. Res. 32 (1996) 999-1007
51. Werner, M.H., 1994 Advance User's Guide. Brucker. <940712>. In: Spectrospin A.G. (Ed.) Fallanden.