메뉴 건너뛰기




Volumn 17, Issue 7, 1996, Pages 715-723

Degradation of poly(D,L-lactic acid) nanoparticles coated with albumin in model digestive fluids (USP XXII)

Author keywords

Albumin; Enzymatic degradation; Gastric fluid; Intestinal fluid; Poly(D,L lactic acid)

Indexed keywords

COATINGS; DEGRADATION; ENZYMES; EVAPORATION; HYDROLYSIS; PHYSIOLOGICAL MODELS; PROTEINS; SIMULATION; SIZE EXCLUSION CHROMATOGRAPHY; SOLVENTS; SYNTHESIS (CHEMICAL);

EID: 0030131048     PISSN: 01429612     EISSN: None     Source Type: Journal    
DOI: 10.1016/0142-9612(96)86742-1     Document Type: Article
Times cited : (64)

References (34)
  • 1
    • 0026186291 scopus 로고
    • Peroral administration of nanoparticles
    • Kreuter J. Peroral administration of nanoparticles. Adv Drug Del Rew 1991; 7: 71-86.
    • (1991) Adv Drug Del Rew , vol.7 , pp. 71-86
    • Kreuter, J.1
  • 3
    • 0022966767 scopus 로고
    • Disposition kinetics and oral bioavailability of vincamine-loaded polyalkyl cyanoacrylate nanoparticles
    • Maincent P, Le Verge R, Sado P, Couvreur P, Devissaguet JP. Disposition kinetics and oral bioavailability of vincamine-loaded polyalkyl cyanoacrylate nanoparticles. J Pharm Sci 1986; 75: 955-958.
    • (1986) J Pharm Sci , vol.75 , pp. 955-958
    • Maincent, P.1    Le Verge, R.2    Sado, P.3    Couvreur, P.4    Devissaguet, J.P.5
  • 4
    • 0023856501 scopus 로고
    • New approach for oral administration of insulin with polyalkylcylanoacrylate nanocapsules as drug carriers
    • Damgé C, Michel C, Aprahamian M, Couvreur P. New approach for oral administration of insulin with polyalkylcylanoacrylate nanocapsules as drug carriers. Diabetes 1988; 37: 246-251.
    • (1988) Diabetes , vol.37 , pp. 246-251
    • Damgé, C.1    Michel, C.2    Aprahamian, M.3    Couvreur, P.4
  • 5
    • 0023578342 scopus 로고
    • Transmucosal passage of polyalkylcyanoacrylate nanocapsules as a new drug carrier in the small intestine
    • Apprahamian M, Michel C, Humbert W, Devissaguet JP, Damgé C. Transmucosal passage of polyalkylcyanoacrylate nanocapsules as a new drug carrier in the small intestine. Biol Cell 1987; 61: 69-76.
    • (1987) Biol Cell , vol.61 , pp. 69-76
    • Apprahamian, M.1    Michel, C.2    Humbert, W.3    Devissaguet, J.P.4    Damgé, C.5
  • 6
    • 0025674686 scopus 로고
    • Nanoparticle uptake by the rat gastrointestinal mucosa: Quantitation and particle size dependency
    • Jani P, Halbert GW, Langridge J, Florence T. Nanoparticle uptake by the rat gastrointestinal mucosa: quantitation and particle size dependency. J Pharm Pharmacol 1990; 42: 821-826.
    • (1990) J Pharm Pharmacol , vol.42 , pp. 821-826
    • Jani, P.1    Halbert, G.W.2    Langridge, J.3    Florence, T.4
  • 8
    • 0017363309 scopus 로고
    • Persorption of particles: Physiology and pharmacology
    • Volkheimer G. Persorption of particles: physiology and pharmacology. Pharmacol Chemother 1977; 14: 163-187.
    • (1977) Pharmacol Chemother , vol.14 , pp. 163-187
    • Volkheimer, G.1
  • 9
    • 0026475525 scopus 로고
    • Nanospheres and microspheres uptake via Peyer's patches: Observation on the rate of uptake in the rat after single oral dose
    • Jani PU, McCarthy DE, Florence AT. Nanospheres and microspheres uptake via Peyer's patches: observation on the rate of uptake in the rat after single oral dose. Int J Pharm 1992; 86: 239-246.
    • (1992) Int J Pharm , vol.86 , pp. 239-246
    • Jani, P.U.1    McCarthy, D.E.2    Florence, A.T.3
  • 10
    • 0025069886 scopus 로고
    • Controlled vaccine release in the gut-associated lymphoid tissues. I. Orally administered biodegradable microspheres target the Payer's patches
    • Eldridge JH, Hammon CJ, Muelbroek JA. Controlled vaccine release in the gut-associated lymphoid tissues. I. Orally administered biodegradable microspheres target the Payer's patches. J Contr Rel 1990; 11: 205-214.
    • (1990) J Contr Rel , vol.11 , pp. 205-214
    • Eldridge, J.H.1    Hammon, C.J.2    Muelbroek, J.A.3
  • 12
    • 0020603897 scopus 로고
    • An in vitro evaluation on the stability of mechanical properties of surgical suture materials in various ph conditions
    • Chu CC, Moncrief G. An in vitro evaluation on the stability of mechanical properties of surgical suture materials in various pH conditions. Ann Surg 1983; 198: 223-228.
    • (1983) Ann Surg , vol.198 , pp. 223-228
    • Chu, C.C.1    Moncrief, G.2
  • 13
    • 0023024294 scopus 로고
    • Mechanism of hydrolytic degradation of poly(L-lactide) microcapsules: Effect of pH, ionic strength and buffer concentration
    • Makino K, Oshima H, Kondo T. Mechanism of hydrolytic degradation of poly(L-lactide) microcapsules: effect of pH, ionic strength and buffer concentration. J Microenc 1986; 3: 203-212.
    • (1986) J Microenc , vol.3 , pp. 203-212
    • Makino, K.1    Oshima, H.2    Kondo, T.3
  • 14
    • 0021559912 scopus 로고
    • Melt spining of poly-L-lactide and hydrolysis of the fiber in vitro
    • Shalaby SW, ed. New York: Plenum
    • Hyon SH, Jamshidi K, Ikada Y. Melt spining of poly-L-lactide and hydrolysis of the fiber in vitro. In: Shalaby SW, ed. Polymers as Biomaterials. New York: Plenum, 1984: 51-65.
    • (1984) Polymers As Biomaterials , pp. 51-65
    • Hyon, S.H.1    Jamshidi, K.2    Ikada, Y.3
  • 15
    • 0019379821 scopus 로고
    • Enzymatic hydrolysis of polylactic acid
    • Williams DF. Enzymatic hydrolysis of polylactic acid. Eng Med 1981; 10: 5-7.
    • (1981) Eng Med , vol.10 , pp. 5-7
    • Williams, D.F.1
  • 16
    • 0017522703 scopus 로고    scopus 로고
    • Enzyme-accelerated hydrolysis of polyglycolic acid
    • Williams DF, Mort E. Enzyme-accelerated hydrolysis of polyglycolic acid. J Bioeng 1977: 231-238.
    • J Bioeng , vol.1977 , pp. 231-238
    • Williams, D.F.1    Mort, E.2
  • 17
    • 0017260859 scopus 로고
    • Polyglactin 910 suture absorption and the role of cellular enzymes. Surg
    • Salthouse TN, Matlaga BF. Polyglactin 910 suture absorption and the role of cellular enzymes. Surg Gynecol Obstet 1976; 142: 544-550.
    • (1976) Gynecol Obstet , vol.142 , pp. 544-550
    • Salthouse, T.N.1    Matlaga, B.F.2
  • 18
    • 0021705531 scopus 로고
    • The enzymatic surface erosion of aliphatic polyesters
    • Pitt CG, Wayne Hendren R, Schindler A. The enzymatic surface erosion of aliphatic polyesters. J Contr Rel 1984; 1: 3-14.
    • (1984) J Contr Rel , vol.1 , pp. 3-14
    • Pitt, C.G.1    Wayne Hendren, R.2    Schindler, A.3
  • 19
    • 0022975567 scopus 로고
    • Polymers for biodegradable medical devices. 1. The potential of polyesters as controlled macromolecular release systems
    • Holland SJ, Tighe BJ, Gould PL. Polymers for biodegradable medical devices. 1. The potential of polyesters as controlled macromolecular release systems. J Contr Rel 1986; 4: 155-180.
    • (1986) J Contr Rel , vol.4 , pp. 155-180
    • Holland, S.J.1    Tighe, B.J.2    Gould, P.L.3
  • 20
    • 0024789505 scopus 로고
    • Synthesis of copoly(D,L-lactic acid) with relatively low molecular weight and in vitro degradation
    • Fukusaki H, Yoshida M, Asano M, Kumakura M. Synthesis of copoly(D,L-lactic acid) with relatively low molecular weight and in vitro degradation. Eur Polym J 1989; 25: 1019-1026.
    • (1989) Eur Polym J , vol.25 , pp. 1019-1026
    • Fukusaki, H.1    Yoshida, M.2    Asano, M.3    Kumakura, M.4
  • 21
    • 84954940327 scopus 로고
    • Hydrolysis of polyesters by Rhizopus arrhizus lipase
    • Tokiwa Y, Suzuki T, Takeda K. Hydrolysis of polyesters by Rhizopus arrhizus lipase. Agric Biol Chem 1986; 50: 1323-1325.
    • (1986) Agric Biol Chem , vol.50 , pp. 1323-1325
    • Tokiwa, Y.1    Suzuki, T.2    Takeda, K.3
  • 22
    • 85012738381 scopus 로고
    • The estimation of pepsin, trypsin, papain and cathepsin with hemoglobin
    • Anson. The estimation of pepsin, trypsin, papain and cathepsin with hemoglobin. J Gen Physiol 1938; 22: 79-89.
    • (1938) J Gen Physiol , vol.22 , pp. 79-89
  • 23
    • 85030191316 scopus 로고    scopus 로고
    • Sigma: Lipase Diagnostic Kit (Procedure No. 800), F-St-Quentin-Fallavier
    • Sigma: Lipase Diagnostic Kit (Procedure No. 800), F-St-Quentin-Fallavier.
  • 24
    • 0000864899 scopus 로고
    • Adsorption of proteins onto polymeric surfaces of different hydrophilicities
    • Lee SH, Rückenstein E. Adsorption of proteins onto polymeric surfaces of different hydrophilicities. J Colloid Interface Sci 1988; 125: 365-379.
    • (1988) J Colloid Interface Sci , vol.125 , pp. 365-379
    • Lee, S.H.1    Rückenstein, E.2
  • 25
    • 0027643021 scopus 로고
    • Adsorption/desorption of human serum albumin at the surface of poly(lactic acid) nanoparticles prepared by a solvent evaporation process
    • Verrecchia T, Huve P, Bazile D, Veillard M, Spenlehauer G, Couvreur P. Adsorption/desorption of human serum albumin at the surface of poly(lactic acid) nanoparticles prepared by a solvent evaporation process. J Biomed Mater Res 1993; 27: 1019-1028.
    • (1993) J Biomed Mater Res , vol.27 , pp. 1019-1028
    • Verrecchia, T.1    Huve, P.2    Bazile, D.3    Veillard, M.4    Spenlehauer, G.5    Couvreur, P.6
  • 26
    • 0021042546 scopus 로고
    • Purification and characterization of peptic fragments derived from the carboxyl-terminal half of human albumin
    • Ledden DJ, Feldhoff RC. Purification and characterization of peptic fragments derived from the carboxyl-terminal half of human albumin. J Prot Chem 1983; 2: 303-319.
    • (1983) J Prot Chem , vol.2 , pp. 303-319
    • Ledden, D.J.1    Feldhoff, R.C.2
  • 27
    • 0343929030 scopus 로고
    • Immunochemical study of the enzymatic degradation of human serum albumin: An analysis of the antigenic structure of a protein molecule
    • Lapresle C, Kaminski M, Tanner CE. Immunochemical study of the enzymatic degradation of human serum albumin: an analysis of the antigenic structure of a protein molecule. J. Immunol 1959; 82: 94-102.
    • (1959) J. Immunol , vol.82 , pp. 94-102
    • Lapresle, C.1    Kaminski, M.2    Tanner, C.E.3
  • 30
    • 0343493329 scopus 로고
    • Serin, zinc, thiol, and carboxyl proteases are the major families of proteolytic enzymes
    • Stryer L, ed. New York: W.H. Freeman and Company
    • Stryer L. Serin, zinc, thiol, and carboxyl proteases are the major families of proteolytic enzymes. In: Stryer L, ed. Biochemistry, 2nd edn. New York: W.H. Freeman and Company, 1981: 170-171.
    • (1981) Biochemistry, 2nd Edn. , pp. 170-171
    • Stryer, L.1
  • 31
    • 11744364078 scopus 로고
    • Structure property relationship in the case of the degradation of massive aliphatic poly-(α-hydroxy acids) in aqueous media, part I: Poly(DL-lactic acid)
    • Li SM. Structure property relationship in the case of the degradation of massive aliphatic poly-(α-hydroxy acids) in aqueous media, Part I: poly(DL-lactic acid). J. Mater Sci: Mater Med 1990; 1: 123-130.
    • (1990) J. Mater Sci: Mater Med , vol.1 , pp. 123-130
    • Li, S.M.1
  • 32
    • 0024061331 scopus 로고
    • Effect of particle size on the in vitro and in vivo degradation rates of poly(DL-lactide-co-glycolide) microcapsules
    • Vischer GE, Pearson JE, Fong JW, Argentieri GJ, Robinson RL, Maulding HV. Effect of particle size on the in vitro and in vivo degradation rates of poly(DL-lactide-co-glycolide) microcapsules. J Biomed Mater Res 1988; 22: 733-746.
    • (1988) J Biomed Mater Res , vol.22 , pp. 733-746
    • Vischer, G.E.1    Pearson, J.E.2    Fong, J.W.3    Argentieri, G.J.4    Robinson, R.L.5    Maulding, H.V.6
  • 34
    • 0002911289 scopus 로고
    • Enzymatically degradable bonds in synthetic polymers
    • Bruck SD, ed. Boca Raton, FL: CRC Press
    • Kopecek J, Rejmanova P. Enzymatically degradable bonds in synthetic polymers. In: Bruck SD, ed. Controlled Drug Delivery, Vol. 1. Boca Raton, FL: CRC Press, 1983: 81-124.
    • (1983) Controlled Drug Delivery , vol.1 , pp. 81-124
    • Kopecek, J.1    Rejmanova, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.