Controlling the mechanism of trypsin inhibition by the numbers of α-cyclodextrins and carboxyl groups in carboxyethylester-polyrotaxanes

Journal of Controlled Release

Volumn 96, Issue 2, 2004, Pages 301-307

  Eguchi, Masaru ^a   Ooya, Tooru ^a   Yui, Nobuhiko ^a  

^a JAPAN ADVANCED INSTITUTE OF SCIENCE AND TECHNOLOGY   (Japan)

Author keywords

Calcium binding; Polyrotaxanes; Trypsin inhibition

Indexed keywords

CALCIUM; DRUG PRODUCTS; ORGANIC ACIDS;

BINDING AFFINITY; INHIBITION MECHANISM;

ENZYME INHIBITION;

ALPHA CYCLODEXTRIN; CARBOXYETHYL ESTER POLYROTAXANE; CARBOXYL GROUP; DRUG CARRIER; ROTAXANE; TRYPSIN; UNCLASSIFIED DRUG;

ARTICLE; BINDING AFFINITY; CALCIUM BINDING; CORRELATION ANALYSIS; DENSITY; DRUG STRUCTURE; INHIBITION KINETICS; MOLECULAR INTERACTION; PRIORITY JOURNAL; PROTEIN ANALYSIS;

ALPHA-CYCLODEXTRINS; ANTHRACENES; CALCIUM; POLYCYCLIC COMPOUNDS; STRUCTURE-ACTIVITY RELATIONSHIP; TIME FACTORS; TRYPSIN; TRYPSIN INHIBITORS;

EID: 1842689086     PISSN: 01683659     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jconrel.2004.02.013     Document Type: Article

References (17)

1. Lehr G.M., Bouwstra J.A., Kok W., de Boer A.G., Tukker J.J., Verhoef J.C., Bremier D.D., Junginger H.E. Effects of the mucoadhesive polycarbophil on the intestinal absorption of a peptide drug in the rat. J. Pharm. Pharmacol. 4:1992;403-407.
2. Nozawa T., Toyobuku H., Kobayashi D., Kuruma K., Tsuji A., Tamai I. Enhanced intestinal absorption of drugs by activation of peptide transporter PEPT1 using proton-releasing polymer. J. Pharm. Sci. 92:2003;2208-2216.
3. Morimoto K., Kayama E., Takeda T., Nakamoto Y., Morisaka K. Enhance of rectal absorption of insulin in polyacrylic acid aqueous gel bases containing long chain fatty acid in rats. Int. J. Pharm. 14:1983;149-157.
4. Morimoto K., Akatsuchi H., Aikawa R., Morishita M., Morisaka K. Enhanced rectal absorption of [Asu1,7]-eel calcitonin in rats using polyacrylic acid aqueous gel base. J. Pharm. Sci. 73:1984;1366-1368.
5. Walker G.F., Ledger R., Tucker I.G. Carbomer inhibits tryptic proteolysis of luteinizing hormone-releasing hormone and N-α-benzoyl-L-arginine ethyl ester by binding the enzyme. Pharm. Res. 16:1999;1074-1080.
6. Lueßen H.L., de Leeuw B.J., Pérard D., Lehr C.-M., de Boer A.G., Verhoef J.C., Junginger H.E. Mucoadhesive polymers in peroral peptide drug delivery: I. Influence of mucoadhesive excipients on the proteolytic activity of intestinal enzymes. Eur. J. Pharm. Sci. 4:1996;117-128.
7. Akiyama Y., Lueßen H.L., de Boer A.G., Verhoef J.C., Junginer H.E. Novel peroral dosage forms with protease inhibitory activities: II. Design of fast dissolving poly(acrylate) and controlled drug-releasing capsule formations with trypsin inhibiting properties. Int. J. Pharm. 138:1996;13-23.
8. Ameye D., Voorspoels J., Foreman P., Tsai J., Richardson P., Geresh S., Remon J.P. Trypsin inhibition, calcium and zinc binding of starch-g-poly(acrylic acid) copolymers and starch/poly(acrylic acid) mixtures for peroral peptide drug delivery. J. Control. Release. 75:2001;357-364.
9. Madsen F., Peppas N. Complexation graft copolymer networks: swelling properties, calcium binding and proteolytic enzyme inhibition. Biomaterials. 20:1999;1701-1708.
10. Lueßen H.L., Verhoef J.C., Borchard G., Lehr C.M., de Boer A.G., Junginger H.E. Mucoadhesive polymer in peroral peptide drug delivery: II. Carbomer and polycarbophil are potent inhibitors of the intestinal proteolytic enzyme trypsin. Pharm. Res. 12:1995;1293-1298.
11. Ooya T., Yui N. Polyrotaxanes: synthesis, structure, and potential in drug delivery. Crit. Rev. Ther. Drug Carr. Syst. 16:1999;289-330.
12. Ooya T., Eguchi M., Ozaki A., Yui N. Carboxyethylester-polyrotaxanes as a new calcium chelating polymer: synthesis, calcium binding and mechanism of trypsin inhibition. Int. J. Pharm. 242:2002;47-54.
13. Harada A., Li J., Kamachi M. The molecular necklace: a rotaxane containing many threaded α-cyclodextrins. Nature. 356:1992;325-327.
14. Tamura M., Ueno A. Energy transfer and guest responsive fluorescence spectra of polyrotaxane consisting of α-cyclodextrins bearing naphthyl moieties. Bull. Chem. Soc. Jpn. 73:2000;147-154.
15. Castro B., Dormoy J.R., Dourtoglou B., Evin G., Selve C., Ziegler J.C. Peptide coupling reagents: VI. A novel, cheaper preparation of benzotriazolylxytris[dimethylamino] phosponium hexafluorophosphate (BOP reagent). Synthesis. 3:1976;751-752.
16. Rypniewski W.R., Perrakis A., Vorgias C.E., Wilson K.S. Evolutionary divergence and conservation of trypsin. Protein Eng. 7:1994;57-64.
17. Bartunik H.D., Summers L.J., Bartsch H.H. Crystal structure of bovine β-trypsin at 1.5 Å resolution in a crystal form with low molecular packaging density-active site geometry, ion pairs and solvent structure. J. Mol. Biol. 210:1989;813-828.