메뉴 건너뛰기




Volumn 28, Issue 3, 2012, Pages 856-861

PEGylation of bovine serum albumin using click chemistry for the application as drug carriers

Author keywords

5 fluorouracil; Bovine serum albumin; Click chemistry; Drug carriers; MPEG; Rifampicin

Indexed keywords

5-FLUOROURACIL; BOVINE SERUM ALBUMINS; CLICK CHEMISTRY; DRUG CARRIER; MPEG; RIFAMPICIN;

EID: 84862787417     PISSN: 87567938     EISSN: 15206033     Source Type: Journal    
DOI: 10.1002/btpr.1526     Document Type: Article
Times cited : (17)

References (41)
  • 2
    • 0017701219 scopus 로고
    • Alteration of immunological properties of bovine serum albumin by covalent attachment of polyethylene glycol
    • Abuchowski A, van Es T, Palczuk NC, Davis FF. Alteration of immunological properties of bovine serum albumin by covalent attachment of polyethylene glycol. J Biol Chem. 1977; 252: 3578-3581.
    • (1977) J Biol Chem. , vol.252 , pp. 3578-3581
    • Abuchowski, A.1    van Es, T.2    Palczuk, N.C.3    Davis, F.F.4
  • 3
    • 0017388651 scopus 로고
    • Effect of covalent attachment of polyethylene glycol on immunogenicity and circulating life of bovine liver catalase
    • Abuchowski A, McCoy JR, Palczuk NC, Van Es T, Davis FF. Effect of covalent attachment of polyethylene glycol on immunogenicity and circulating life of bovine liver catalase. J Biol Chem. 1977; 252: 3582-3586.
    • (1977) J Biol Chem. , vol.252 , pp. 3582-3586
    • Abuchowski, A.1    McCoy, J.R.2    Palczuk, N.C.3    Van Es, T.4    Davis, F.F.5
  • 4
    • 0032870935 scopus 로고    scopus 로고
    • Bioconjugation in pharmaceutical chemistry
    • Veronese FM, Morpurgo M. Bioconjugation in pharmaceutical chemistry. Farmaco. 1999; 54: 497-516.
    • (1999) Farmaco. , vol.54 , pp. 497-516
    • Veronese, F.M.1    Morpurgo, M.2
  • 5
    • 0032126044 scopus 로고    scopus 로고
    • Stabilization of substances in circulation
    • Monfardini C, Veronese FM. Stabilization of substances in circulation. Bioconjugate Chem. 1998; 9: 418-450.
    • (1998) Bioconjugate Chem. , vol.9 , pp. 418-450
    • Monfardini, C.1    Veronese, F.M.2
  • 6
    • 0026124772 scopus 로고
    • The therapeutic value of poly(ethylene glycol)-modified proteins
    • Nucci ML, Shorr R, Abuchowski A. The therapeutic value of poly(ethylene glycol)-modified proteins. Adv Drug Deliv Rev. 1991; 6: 133-151.
    • (1991) Adv Drug Deliv Rev. , vol.6 , pp. 133-151
    • Nucci, M.L.1    Shorr, R.2    Abuchowski, A.3
  • 7
    • 0035291191 scopus 로고    scopus 로고
    • SMANCS and polymer-conjugated macromolecular drugs: advantages in cancer chemotherapy
    • Maeda H. SMANCS and polymer-conjugated macromolecular drugs: advantages in cancer chemotherapy. Adv Drug Deliv Rev. 2001; 46: 169-185.
    • (2001) Adv Drug Deliv Rev. , vol.46 , pp. 169-185
    • Maeda, H.1
  • 8
    • 0026118928 scopus 로고
    • Suppression of antibody responses by conjugates of antigens and monomethoxy poly(ethylene glycol)
    • Sehon AH. Suppression of antibody responses by conjugates of antigens and monomethoxy poly(ethylene glycol). Adv Drug Deliv Rev. 1991; 6: 203-217.
    • (1991) Adv Drug Deliv Rev. , vol.6 , pp. 203-217
    • Sehon, A.H.1
  • 9
    • 0032821439 scopus 로고    scopus 로고
    • Preparation and in vitro characterization of HSA-mPEG nanoparticles
    • Wu L, Martin CG, Etienne S, Stanley SD, Lisbeth I. Preparation and in vitro characterization of HSA-mPEG nanoparticles. Int J Pharm. 1999; 189: 161-170.
    • (1999) Int J Pharm. , vol.189 , pp. 161-170
    • Wu, L.1    Martin, C.G.2    Etienne, S.3    Stanley, S.D.4    Lisbeth, I.5
  • 14
    • 36148951016 scopus 로고    scopus 로고
    • Maintaining the dose intensity of ICE chemotherapy with a thrombopoietic agent, PEG-rHuMGDF, may confer a survival advantage in relapsed and refractory aggressive non-Hodgkin lymphoma
    • Moskowitz CH, Hamlin PA, Gabrilove J, Bertino JR, Portlock CS, Straus DJ, Gencarelli AN, Nimer SD, Zelenetz AD. Maintaining the dose intensity of ICE chemotherapy with a thrombopoietic agent, PEG-rHuMGDF, may confer a survival advantage in relapsed and refractory aggressive non-Hodgkin lymphoma. Ann Oncol. 2007; 18: 1842-1850.
    • (2007) Ann Oncol. , vol.18 , pp. 1842-1850
    • Moskowitz, C.H.1    Hamlin, P.A.2    Gabrilove, J.3    Bertino, J.R.4    Portlock, C.S.5    Straus, D.J.6    Gencarelli, A.N.7    Nimer, S.D.8    Zelenetz, A.D.9
  • 15
    • 70349988803 scopus 로고    scopus 로고
    • PEG conjugates in clinical development or use as anticancer agents: an overview
    • Pasut G, Veronese FM. PEG conjugates in clinical development or use as anticancer agents: an overview. Adv Drug Deliv Rev. 2009; 61: 1177-1188.
    • (2009) Adv Drug Deliv Rev. , vol.61 , pp. 1177-1188
    • Pasut, G.1    Veronese, F.M.2
  • 17
    • 50249118650 scopus 로고    scopus 로고
    • Responsive polymer-protein bioconjugates prepared by RAFT polymerization and copper catalyzed azide-alkyne click chemistry
    • Li M, De P, Gondi SR, Sumerlin BS. Responsive polymer-protein bioconjugates prepared by RAFT polymerization and copper catalyzed azide-alkyne click chemistry. Macromol Rapid Commun. 2008; 29: 1172-1176.
    • (2008) Macromol Rapid Commun. , vol.29 , pp. 1172-1176
    • Li, M.1    De, P.2    Gondi, S.R.3    Sumerlin, B.S.4
  • 18
    • 67649211955 scopus 로고    scopus 로고
    • Monitoring protein-polymer conjugation by a fluorogenic Cu(I)-catalyzed azide-alkyne 1,3-dipolar cycloaddition
    • Dirks AT, Cornelissen JJ, Nolte RJ. Monitoring protein-polymer conjugation by a fluorogenic Cu(I)-catalyzed azide-alkyne 1, 3-dipolar cycloaddition. Bioconjugate Chem. 2009; 20: 1129-1138.
    • (2009) Bioconjugate Chem. , vol.20 , pp. 1129-1138
    • Dirks, A.T.1    Cornelissen, J.J.2    Nolte, R.J.3
  • 20
    • 0006302041 scopus 로고
    • Phase transfer catalysis synthesis of α,ω-diallylpoly(ethylene oxide)
    • Dimonie M, Teodorescu M. Phase transfer catalysis synthesis of α, ω-diallylpoly(ethylene oxide). Makromol Chem Rapid Commun. 1993; 14: 303-307.
    • (1993) Makromol Chem Rapid Commun. , vol.14 , pp. 303-307
    • Dimonie, M.1    Teodorescu, M.2
  • 21
    • 19244381301 scopus 로고    scopus 로고
    • A novel in vitro release technique for peptide-containing biodegradable microspheres
    • Kostanski JW, DeLuca PP. A novel in vitro release technique for peptide-containing biodegradable microspheres. AAPS PharmSciTech. 2000; 1: 30-40.
    • (2000) AAPS PharmSciTech. , vol.1 , pp. 30-40
    • Kostanski, J.W.1    DeLuca, P.P.2
  • 22
    • 37349075235 scopus 로고    scopus 로고
    • The immobilization of proteins on biodegradable polymer fibers via click chemistry
    • Shi Q, Chen XS, Lu TC, Jing XB. The immobilization of proteins on biodegradable polymer fibers via click chemistry. Biomaterials. 2008; 29: 1118-1126.
    • (2008) Biomaterials. , vol.29 , pp. 1118-1126
    • Shi, Q.1    Chen, X.S.2    Lu, T.C.3    Jing, X.B.4
  • 23
    • 34250810836 scopus 로고    scopus 로고
    • 'Click' bioconjugation of a well-defined synthetic polymer and a protein transduction domain
    • Lutz JF, Borner HG, Weichenhan K. 'Click' bioconjugation of a well-defined synthetic polymer and a protein transduction domain. Aust J Chem. 2007; 60: 410-413.
    • (2007) Aust J Chem. , vol.60 , pp. 410-413
    • Lutz, J.F.1    Borner, H.G.2    Weichenhan, K.3
  • 27
    • 33748933568 scopus 로고    scopus 로고
    • Stealth PEG-PHDCA niosomes: effects of chain length of PEG and particle size on niosomes surface properties, in vitro drug release, phagocytic uptake, in vivo pharmacokinetics and antitumor activity
    • Shi B, Fang C, Pei YY. Stealth PEG-PHDCA niosomes: effects of chain length of PEG and particle size on niosomes surface properties, in vitro drug release, phagocytic uptake, in vivo pharmacokinetics and antitumor activity. J Pharm Sci. 2006; 95: 1873-1887.
    • (2006) J Pharm Sci. , vol.95 , pp. 1873-1887
    • Shi, B.1    Fang, C.2    Pei, Y.Y.3
  • 28
    • 33845544743 scopus 로고    scopus 로고
    • Synthesis of protein-polymer conjugates
    • Heredia KL, Maynard HD. Synthesis of protein-polymer conjugates. Org Biomol Chem. 2007; 5: 45-53.
    • (2007) Org Biomol Chem. , vol.5 , pp. 45-53
    • Heredia, K.L.1    Maynard, H.D.2
  • 29
    • 33947553005 scopus 로고
    • The structure of water and hydrophobic bonding in proteins. III. The thermodynamic properties of hydrophobic bonds in proteins
    • Nemethy G, Scheraga HA. The structure of water and hydrophobic bonding in proteins. III. The thermodynamic properties of hydrophobic bonds in proteins. J Phys Chem. 1962; 66: 1773-1789.
    • (1962) J Phys Chem. , vol.66 , pp. 1773-1789
    • Nemethy, G.1    Scheraga, H.A.2
  • 31
    • 0019889063 scopus 로고
    • Thermodynamics of protein association reactions: forces contributing to stability
    • Ross PD, Subramanian S. Thermodynamics of protein association reactions: forces contributing to stability. Biochemistry. 1981; 20: 3096-3102.
    • (1981) Biochemistry. , vol.20 , pp. 3096-3102
    • Ross, P.D.1    Subramanian, S.2
  • 32
    • 0026664548 scopus 로고
    • Atomic structure and chemistry of human serum albumin
    • He XM, Carter DC. Atomic structure and chemistry of human serum albumin. Nature. 1992; 358: 209-215.
    • (1992) Nature. , vol.358 , pp. 209-215
    • He, X.M.1    Carter, D.C.2
  • 34
    • 42949132820 scopus 로고    scopus 로고
    • Thermochemical studies on the reaction of barbital sodium with bovine serum albumin
    • Lin J, Zhao W, Ding F, Jiang ZQ. Thermochemical studies on the reaction of barbital sodium with bovine serum albumin. Spectrosc Spect Anal. 2008; 28: 648-651.
    • (2008) Spectrosc Spect Anal. , vol.28 , pp. 648-651
    • Lin, J.1    Zhao, W.2    Ding, F.3    Jiang, Z.Q.4
  • 35
    • 0035848399 scopus 로고    scopus 로고
    • Preparation and characterization of rose Bengal-loaded surface-modified albumin nanoparticles
    • Lin W, Garnett MC, Davis SS, Schacht E, Ferruti P, Illum L. Preparation and characterization of rose Bengal-loaded surface-modified albumin nanoparticles. J Controlled Release. 2001; 71: 117-126.
    • (2001) J Controlled Release. , vol.71 , pp. 117-126
    • Lin, W.1    Garnett, M.C.2    Davis, S.S.3    Schacht, E.4    Ferruti, P.5    Illum, L.6
  • 36
    • 0036414516 scopus 로고    scopus 로고
    • A study on the preparation and anti-tumor efficacy of bovine serum albumin nanospheres containing 5-fluorouracil
    • Santhi K, Dhanaraj SA, Joseph V, Ponnusankar S, Suresh B. A study on the preparation and anti-tumor efficacy of bovine serum albumin nanospheres containing 5-fluorouracil. Drug Dev Ind Pharm. 2002; 28: 1171-1179.
    • (2002) Drug Dev Ind Pharm. , vol.28 , pp. 1171-1179
    • Santhi, K.1    Dhanaraj, S.A.2    Joseph, V.3    Ponnusankar, S.4    Suresh, B.5
  • 37
    • 0030948510 scopus 로고    scopus 로고
    • PEG-coated nanospheres from amphiphilic diblock and multiblock copolymers: investigation of their drug encapsulation and release characteristics
    • Peracchia MT, Gref R, Minamitake Y, Domb A, Lotan N, Langer R. PEG-coated nanospheres from amphiphilic diblock and multiblock copolymers: investigation of their drug encapsulation and release characteristics. J Controlled Release. 1997; 46: 223-231.
    • (1997) J Controlled Release. , vol.46 , pp. 223-231
    • Peracchia, M.T.1    Gref, R.2    Minamitake, Y.3    Domb, A.4    Lotan, N.5    Langer, R.6
  • 38
    • 33846868640 scopus 로고    scopus 로고
    • Synthesis of poly(ethylene glycol)-metaxalone conjugates and study of its controlled release in vitro
    • Zhang J, Fan XD, Liu YF, Bo L, Liu X. Synthesis of poly(ethylene glycol)-metaxalone conjugates and study of its controlled release in vitro. Int J Pharm. 2007; 332: 125-131.
    • (2007) Int J Pharm. , vol.332 , pp. 125-131
    • Zhang, J.1    Fan, X.D.2    Liu, Y.F.3    Bo, L.4    Liu, X.5
  • 40
    • 41649108815 scopus 로고    scopus 로고
    • Interaction of gold nanoparticles with protein: a spectroscopic study to monitor protein conformational changes
    • Wangoo N, Suri CR, Shekhawat G. Interaction of gold nanoparticles with protein: a spectroscopic study to monitor protein conformational changes. Appl Phys Lett. 2008; 92: 133104/1-3.
    • (2008) Appl Phys Lett. , vol.92
    • Wangoo, N.1    Suri, C.R.2    Shekhawat, G.3
  • 41
    • 33646774999 scopus 로고    scopus 로고
    • Adsorption-induced conformational changes of proteins onto ceramic particles: differential scanning calorimetry and FTIR analysis
    • Brandes N, Welzel PB, Werner C, Kroh LW. Adsorption-induced conformational changes of proteins onto ceramic particles: differential scanning calorimetry and FTIR analysis. J Colloid Interface Sci. 2006; 299: 56-69.
    • (2006) J Colloid Interface Sci. , vol.299 , pp. 56-69
    • Brandes, N.1    Welzel, P.B.2    Werner, C.3    Kroh, L.W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.