메뉴 건너뛰기




Volumn 16, Issue 7, 1999, Pages 1125-1131

Complex formation between the anionic polymer (PAA) and a cationic drug (procaine HCl): Characterization by microcalorimetric studies

Author keywords

Drug polymer interactions; Electrostatic and non electrostatic interactions; Isothermal titration microcalorimetry; Salt dependence

Indexed keywords

POLYACRYLIC ACID; PROCAINE;

EID: 0032772646     PISSN: 07248741     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1018912522342     Document Type: Article
Times cited : (21)

References (30)
  • 1
    • 0027979462 scopus 로고
    • Characterisation of acrylic resin matrix films and mechanisms of drug-polymer interactions
    • M. R. Jenquin and J. W. McGinity. Characterisation of acrylic resin matrix films and mechanisms of drug-polymer interactions. Int. J. Pharm. 101:23-34 (1994).
    • (1994) Int. J. Pharm. , vol.101 , pp. 23-34
    • Jenquin, M.R.1    McGinity, J.W.2
  • 2
    • 0031646316 scopus 로고    scopus 로고
    • Novel polyion complex micelles entrapping enzyme molecules in the core: Preparation of narrowly distributed micelles from lysozyme and poly (ethylene glycol)- poly(aspartic acid) block copolymer in aqueous medium
    • A. Harada and K. Kataoka. Novel polyion complex micelles entrapping enzyme molecules in the core: Preparation of narrowly distributed micelles from lysozyme and poly (ethylene glycol)- poly(aspartic acid) block copolymer in aqueous medium. Macromolecules 31:288-294 (1998).
    • (1998) Macromolecules , vol.31 , pp. 288-294
    • Harada, A.1    Kataoka, K.2
  • 3
    • 0027432534 scopus 로고
    • Drug loaded nanoparticles: Preparation methods and drug targeting issues
    • E. Allémann, R. Gurny, and E. Doelker. Drug loaded nanoparticles: Preparation methods and drug targeting issues. Eur. J. Pharm. Biopharm. 39:173-191 (1993).
    • (1993) Eur. J. Pharm. Biopharm. , vol.39 , pp. 173-191
    • Allémann, E.1    Gurny, R.2    Doelker, E.3
  • 4
    • 0030988750 scopus 로고    scopus 로고
    • Biomedical applications of nanotechnology-implications for drug targeting and gene therapy
    • S. S Davis. Biomedical applications of nanotechnology-implications for drug targeting and gene therapy. Trends Biotechnol. 15:217-224 (1997).
    • (1997) Trends Biotechnol. , vol.15 , pp. 217-224
    • Davis, S.S.1
  • 5
    • 0032952283 scopus 로고    scopus 로고
    • PLGA nanoparticles prepared by nanoprecipitation: Drug loading and release studies of a water soluble drug
    • T. Govender, S. Stolnik, M. C. Garnett, L. Illum, and S. S. Davis. PLGA nanoparticles prepared by nanoprecipitation: Drug loading and release studies of a water soluble drug. J. Contr. Rel. 57:171-185 (1999).
    • (1999) J. Contr. Rel. , vol.57 , pp. 171-185
    • Govender, T.1    Stolnik, S.2    Garnett, M.C.3    Illum, L.4    Davis, S.S.5
  • 6
    • 0030865986 scopus 로고    scopus 로고
    • Synthetic polymers for vectorial delivery of DNA: Characterisation of polymer-DNA complexes by photon correlation spectroscopy and stability to nuclease degradation and disruption by polyanions in vitro
    • P. R. Dash, V. Toncheva, E. Schacht, and L. W. Seymour. Synthetic polymers for vectorial delivery of DNA: characterisation of polymer-DNA complexes by photon correlation spectroscopy and stability to nuclease degradation and disruption by polyanions in vitro. J. Contr. Rel. 48:269-276 (1997).
    • (1997) J. Contr. Rel. , vol.48 , pp. 269-276
    • Dash, P.R.1    Toncheva, V.2    Schacht, E.3    Seymour, L.W.4
  • 7
    • 0024356301 scopus 로고
    • Rapid measurement of binding constants and heats of binding using a new titration calorimeter
    • T. Wiseman, S. Williston, J. F. Brandts, and L. N. Lin. Rapid measurement of binding constants and heats of binding using a new titration calorimeter. Anal. Biochem. 179:131-137 (1989).
    • (1989) Anal. Biochem. , vol.179 , pp. 131-137
    • Wiseman, T.1    Williston, S.2    Brandts, J.F.3    Lin, L.N.4
  • 8
    • 0031027122 scopus 로고    scopus 로고
    • Characterisation of binding interactions by isothermal titration calorimetry
    • M. L. Doyle. Characterisation of binding interactions by isothermal titration calorimetry. Curr. Opin. Biotechnol. 8:31-35 (1997).
    • (1997) Curr. Opin. Biotechnol. , vol.8 , pp. 31-35
    • Doyle, M.L.1
  • 10
    • 0030248568 scopus 로고    scopus 로고
    • An in situ gelling system for parenteral delivery
    • B. O. Haglund, R. Joshi, and K. J. Himmelstein. An in situ gelling system for parenteral delivery. J. Contr. Rel. 41:229-235 (1996).
    • (1996) J. Contr. Rel. , vol.41 , pp. 229-235
    • Haglund, B.O.1    Joshi, R.2    Himmelstein, K.J.3
  • 11
    • 0028314775 scopus 로고
    • Vaginal and reproductive system treatments using a bioadhesive polymer
    • J. R. Robinson and W. J. Bologna. Vaginal and reproductive system treatments using a bioadhesive polymer. J. Contr. Rel. 28:87-94 (1994).
    • (1994) J. Contr. Rel. , vol.28 , pp. 87-94
    • Robinson, J.R.1    Bologna, W.J.2
  • 12
    • 0000162429 scopus 로고    scopus 로고
    • Salt dependence of free energy, enthalpy, and entropy of nonsequcncc specific DNA binding
    • T. Lundback and T. Hard. Salt dependence of free energy, enthalpy, and entropy of nonsequcncc specific DNA binding. J. Phys. Chem. 100:17690-17695 (1996).
    • (1996) J. Phys. Chem. , vol.100 , pp. 17690-17695
    • Lundback, T.1    Hard, T.2
  • 13
    • 0017895903 scopus 로고
    • The molecular theory of polyelectrolyte solutions with applications to the electrostatic properties of polynucleotides
    • G. S. Manning. The molecular theory of polyelectrolyte solutions with applications to the electrostatic properties of polynucleotides. Quart. Rev. Biophys. 2:179-246 (1978).
    • (1978) Quart. Rev. Biophys. , vol.2 , pp. 179-246
    • Manning, G.S.1
  • 14
    • 11644276439 scopus 로고
    • Limiting laws and counterion condensation in polyelectrolyte solutions. I. Colligative properties
    • G. S. Manning. Limiting laws and counterion condensation in polyelectrolyte solutions. I. Colligative properties. J. Phys. Chem. 51:924-933 (1969).
    • (1969) J. Phys. Chem. , vol.51 , pp. 924-933
    • Manning, G.S.1
  • 15
    • 0015274187 scopus 로고
    • On the application of polyelectrolyte limiting laws to the helix-coil transition of DNA. I. Excess univalent cations
    • G. S. Manning. On the application of polyelectrolyte limiting laws to the helix-coil transition of DNA. I. Excess univalent cations. BIPMA. 11:937-949 (1972).
    • (1972) BIPMA , vol.11 , pp. 937-949
    • Manning, G.S.1
  • 16
    • 0017820499 scopus 로고
    • Thermodynamic analysis of ion effects on the binding and conformational equilibria of proteins and nucleic acids: The roles of ion association or release, screening, and ion effects on water activity
    • M. T. Jr. Record, C. F. Anderson, and T. M. Lohman. Thermodynamic analysis of ion effects on the binding and conformational equilibria of proteins and nucleic acids: the roles of ion association or release, screening, and ion effects on water activity. Quart. Rev. Biophys. 2:103-178 (1978).
    • (1978) Quart. Rev. Biophys. , vol.2 , pp. 103-178
    • Record M.T., Jr.1    Anderson, C.F.2    Lohman, T.M.3
  • 17
    • 0017146579 scopus 로고
    • Ion effects on ligand-nucleic acid interactions
    • M. T. Jr. Record, M. T. Lohman, and P. de Haseth. Ion effects on ligand-nucleic acid interactions. J. Mol. Bio. 107:145-158 (1976).
    • (1976) J. Mol. Bio. , vol.107 , pp. 145-158
    • Record M.T., Jr.1    Lohman, M.T.2    De Haseth, P.3
  • 19
    • 0032489503 scopus 로고    scopus 로고
    • Thermodynamic characterization of non-sequence-specific DNA- binding by the sso7d protein from sulfolobus solfataricus
    • T. Lundback, H. Hansson, S. Knapp, R. Ladenstein, and T. Hard. Thermodynamic characterization of non-sequence-specific DNA- binding by the sso7d protein from sulfolobus solfataricus. J. Mol. Biol. 276:775-786 (1998).
    • (1998) J. Mol. Biol. , vol.276 , pp. 775-786
    • Lundback, T.1    Hansson, H.2    Knapp, S.3    Ladenstein, R.4    Hard, T.5
  • 20
    • 0019330787 scopus 로고
    • Pentalysine- deoxyribonucleic acid interactions: A model for the general effects of ion concentrations on the interactions of proteins with nucleic acids
    • T. M. Lohman, P. L. de Haseth, and M. T. Jr. Record. Pentalysine- deoxyribonucleic acid interactions: A model for the general effects of ion concentrations on the interactions of proteins with nucleic acids. Biochemistry 19:3522-3530 (1980).
    • (1980) Biochemistry , vol.19 , pp. 3522-3530
    • Lohman, T.M.1    De Haseth, P.L.2    Record M.T., Jr.3
  • 21
    • 0026808625 scopus 로고
    • Thermodynamics of ligandnucleic acid interactions
    • T. M. Lohman and D. P. Mascotti. Thermodynamics of ligandnucleic acid interactions. Methods Enzymol. 221:400-424 (1992).
    • (1992) Methods Enzymol. , vol.221 , pp. 400-424
    • Lohman, T.M.1    Mascotti, D.P.2
  • 22
    • 0024284762 scopus 로고
    • 65 binding mode. Cation and anion effects and polynucleotide specificity
    • 65 binding mode. Cation and anion effects and polynucleotide specificity. Biochemistry 27:456-471 (1988).
    • (1988) Biochemistry , vol.27 , pp. 456-471
    • Overman, L.B.1    Bujalowski, W.2    Lohman, T.M.3
  • 23
    • 0028297873 scopus 로고
    • Linkage of pH, anion and cation effects in protein-nucleic acid equilibria
    • L. B. Overman and T. M. Lohman. Linkage of pH, anion and cation effects in protein-nucleic acid equilibria. J. Mol. Biol. 236:165-178. (1994).
    • (1994) J. Mol. Biol. , vol.236 , pp. 165-178
    • Overman, L.B.1    Lohman, T.M.2
  • 24
    • 0026730188 scopus 로고
    • Thermodynamics of single- strand RNA binding to oligosines containing tryptophan
    • D. P. Mascotti and T. M. Lohman. Thermodynamics of single- strand RNA binding to oligosines containing tryptophan. Biochemistry 31:8932-8946 (1992).
    • (1992) Biochemistry , vol.31 , pp. 8932-8946
    • Mascotti, D.P.1    Lohman, T.M.2
  • 25
    • 0027412944 scopus 로고
    • Biothermodynamic characterization of monocarboxylic and dicarboxylic aliphatic acids binding to human serum albumin: A flow microcalorimetric study
    • H. Aki and M. Yamamoto. Biothermodynamic characterization of monocarboxylic and dicarboxylic aliphatic acids binding to human serum albumin: A flow microcalorimetric study. Biophys. Chem. 46:91-99 (1993).
    • (1993) Biophys. Chem. , vol.46 , pp. 91-99
    • Aki, H.1    Yamamoto, M.2
  • 26
    • 0009574845 scopus 로고
    • Thermodynamic aspects of the molecular recognition of drugs by human serum albumin
    • H. Aki, M. Goto, and M. Yamamoto. Thermodynamic aspects of the molecular recognition of drugs by human serum albumin. Thermochimica Acta 251:379-388 (1995).
    • (1995) Thermochimica Acta , vol.251 , pp. 379-388
    • Aki, H.1    Goto, M.2    Yamamoto, M.3
  • 27
    • 0016175370 scopus 로고
    • Theoretical aspects of DNA- protein interactions: Co-operative and non-co-operative binding of large ligands to a one-dimensional homogeneous lattice
    • J. D. McGhee and P. J. Hippel. Theoretical aspects of DNA- protein interactions: Co-operative and non-co-operative binding of large ligands to a one-dimensional homogeneous lattice. J. Mol. Biol. 86:469-489 (1974).
    • (1974) J. Mol. Biol. , vol.86 , pp. 469-489
    • McGhee, J.D.1    Hippel, P.J.2
  • 29
    • 0028105270 scopus 로고
    • Quantitative evaluation of electrostatic and hydrogen-binding contributions to metal cofactor binding to nucleic acids
    • C. B. Black and J, A. Cowan. Quantitative evaluation of electrostatic and hydrogen-binding contributions to metal cofactor binding to nucleic acids. J. Am. Chem. Soc. 116:1174-1178 (1994).
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 1174-1178
    • Black, C.B.1    Cowan, J.A.2
  • 30
    • 0027595827 scopus 로고
    • Interaction of tetradecyltrimethylammonium bromide with poly (acrylic acid) and poly (methacrylic acid). Effect of charge density
    • J. J. Kiefer, P. Somasundaran, and K. P. Ananthapadmanabhan. Interaction of tetradecyltrimethylammonium bromide with poly (acrylic acid) and poly (methacrylic acid). Effect of charge density. Langmuir 9:1187-1192 (1993).
    • (1993) Langmuir , vol.9 , pp. 1187-1192
    • Kiefer, J.J.1    Somasundaran, P.2    Ananthapadmanabhan, K.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.