메뉴 건너뛰기




Volumn 13, Issue 11, 2016, Pages 1609-1623

Albumin nanostructures as advanced drug delivery systems

Author keywords

bovine serum albumin; drug delivery systems; Human serum albumin; nanoparticles; ovalbumin

Indexed keywords

ALBUMIN; ALBUMIN CONJUGATE; APOLIPOPROTEIN; BOVINE SERUM ALBUMIN; CELL RECEPTOR; FOLIC ACID; HUMAN ALBUMIN; MACROGOL; MICROSPHERE; MONOCLONAL ANTIBODY; NANOMATERIAL; NANOPARTICLE; OVALBUMIN; RAT SERUM ALBUMIN; SURFACTANT; UNCLASSIFIED DRUG; ALBUMINOID; DRUG; DRUG CARRIER; LIGAND;

EID: 84991384253     PISSN: 17425247     EISSN: 17447593     Source Type: Journal    
DOI: 10.1080/17425247.2016.1193149     Document Type: Review
Times cited : (314)

References (132)
  • 1
    • 84876534007 scopus 로고    scopus 로고
    • Challenges and key considerations of the enhanced permeability and retention effect for nanomedicine drug delivery in oncology
    • U.Prabhakar, H.Maeda, R.K.Jain, et al. Challenges and key considerations of the enhanced permeability and retention effect for nanomedicine drug delivery in oncology. Cancer Res. 2013;73(8):2412–2417.
    • (2013) Cancer Res , vol.73 , Issue.8 , pp. 2412-2417
    • Prabhakar, U.1    Maeda, H.2    Jain, R.K.3
  • 2
    • 84873244450 scopus 로고    scopus 로고
    • Advanced materials and processing for drug delivery: the past and the future
    • Y.Zhang, H.F.Chan, K.W.Leong Advanced materials and processing for drug delivery:the past and the future. Adv Drug Deliv Rev. 2013;65(1):104–120.
    • (2013) Adv Drug Deliv Rev , vol.65 , Issue.1 , pp. 104-120
    • Zhang, Y.1    Chan, H.F.2    Leong, K.W.3
  • 3
    • 84931828272 scopus 로고    scopus 로고
    • Carbon nanotubes part I: preparation of a novel and versatile drug-delivery vehicle
    • M.Karimi, N.Solati, M.Amiri, et al. Carbon nanotubes part I:preparation of a novel and versatile drug-delivery vehicle. Expert Opin Drug Deliv. 2015;12(7):1–17.
    • (2015) Expert Opin Drug Deliv , vol.12 , Issue.7 , pp. 1-17
    • Karimi, M.1    Solati, N.2    Amiri, M.3
  • 4
    • 84961901448 scopus 로고    scopus 로고
    • Bacteriophages and phage-inspired nanocarriers for targeted delivery of therapeutic cargos
    • M.Karimi, H.Mirshekari, M.MoosaviBasri, et al. Bacteriophages and phage-inspired nanocarriers for targeted delivery of therapeutic cargos. Adv Drug Deliv Rev. 2016. doi:10.1016/j.addr.2016.03.003. [Epub ahead of print]
    • (2016) Adv Drug Deliv Rev
    • Karimi, M.1    Mirshekari, H.2    MoosaviBasri, M.3
  • 5
    • 84872728103 scopus 로고    scopus 로고
    • Design, functionalization strategies and biomedical applications of targeted biodegradable/biocompatible polymer-based nanocarriers for drug delivery
    • J.Nicolas, S.Mura, D.Brambilla, et al. Design, functionalization strategies and biomedical applications of targeted biodegradable/biocompatible polymer-based nanocarriers for drug delivery. Chem Soc Rev. 2013;42(3):1147–1235.
    • (2013) Chem Soc Rev , vol.42 , Issue.3 , pp. 1147-1235
    • Nicolas, J.1    Mura, S.2    Brambilla, D.3
  • 6
    • 84931589277 scopus 로고    scopus 로고
    • Carbon nanotubes part II: a remarkable carrier for drug and gene delivery
    • M.Karimi, N.Solati, A.Ghasemi, et al. Carbon nanotubes part II:a remarkable carrier for drug and gene delivery. Expert Opin Drug Deliv. 2015;12(7):1–17.
    • (2015) Expert Opin Drug Deliv , vol.12 , Issue.7 , pp. 1-17
    • Karimi, M.1    Solati, N.2    Ghasemi, A.3
  • 7
    • 84873254187 scopus 로고    scopus 로고
    • Nanoparticles in drug delivery: past, present and future
    • P.Couvreur. Nanoparticles in drug delivery:past, present and future. Adv Drug Deliv Rev. 2013;65(1):21–23.
    • (2013) Adv Drug Deliv Rev , vol.65 , Issue.1 , pp. 21-23
    • Couvreur, P.1
  • 8
    • 84959422707 scopus 로고    scopus 로고
    • Smart micro/nanoparticles in stimulus-responsive drug/gene delivery systems
    • M.Karimi, A.Ghasemi, P.S.Zangabad, et al. Smart micro/nanoparticles in stimulus-responsive drug/gene delivery systems. Chem Soc Rev. 2016;45(5):1457–1501.
    • (2016) Chem Soc Rev , vol.45 , Issue.5 , pp. 1457-1501
    • Karimi, M.1    Ghasemi, A.2    Zangabad, P.S.3
  • 9
    • 56949084877 scopus 로고    scopus 로고
    • Albumin as a drug carrier: design of prodrugs, drug conjugates and nanoparticles
    • F.Kratz. Albumin as a drug carrier:design of prodrugs, drug conjugates and nanoparticles. J Controlled Release. 2008;132(3):171–183.• Good review about albumin-based drug delivery systems (DDSs) especially those in different stages of regulatory approval.
    • (2008) J Controlled Release , vol.132 , Issue.3 , pp. 171-183
    • Kratz, F.1
  • 10
    • 84882837905 scopus 로고    scopus 로고
    • Proteins: emerging carrier for delivery of cancer therapeutics
    • C.Yewale, D.Baradia, I.Vhora, et al. Proteins:emerging carrier for delivery of cancer therapeutics. Expert Opin Drug Deliv. 2013;10(10):1429–1448.
    • (2013) Expert Opin Drug Deliv , vol.10 , Issue.10 , pp. 1429-1448
    • Yewale, C.1    Baradia, D.2    Vhora, I.3
  • 11
    • 0021782306 scopus 로고
    • Serum albumin
    • T.Peters. Serum albumin. Adv Protein Chem. 1985;37:161–245.
    • (1985) Adv Protein Chem , vol.37 , pp. 161-245
    • Peters, T.1
  • 12
    • 84893515418 scopus 로고    scopus 로고
    • Cationic bovine serum albumin based self‐assembled nanoparticles as siRNA delivery vector for treating lung metastatic cancer
    • J.Han, Q.Wang, Z.Zhang, et al. Cationic bovine serum albumin based self‐assembled nanoparticles as siRNA delivery vector for treating lung metastatic cancer. Small. 2014;10(3):524–535.
    • (2014) Small , vol.10 , Issue.3 , pp. 524-535
    • Han, J.1    Wang, Q.2    Zhang, Z.3
  • 13
    • 84890155567 scopus 로고    scopus 로고
    • Enzyme delivery using the 30Kc19 protein and human serum albumin nanoparticles
    • H.J.Lee, H.H.Park, J.A.Kim, et al. Enzyme delivery using the 30Kc19 protein and human serum albumin nanoparticles. Biomaterials. 2014;35(5):1696–1704.• Discusses silk worm-derived 30Kc19 protein functionalized human serum albumin nanoparticles (HSA NPs) for investigation the 30Kc19 impact on cellular uptake and stability.
    • (2014) Biomaterials , vol.35 , Issue.5 , pp. 1696-1704
    • Lee, H.J.1    Park, H.H.2    Kim, J.A.3
  • 14
    • 35148815670 scopus 로고    scopus 로고
    • Mechanisms and optimization of in vivo delivery of lipophilic siRNAs
    • C.Wolfrum, S.Shi, K.N.Jayaprakash, et al. Mechanisms and optimization of in vivo delivery of lipophilic siRNAs. Nat Biotechnol. 2007;25(10):1149–1157.
    • (2007) Nat Biotechnol , vol.25 , Issue.10 , pp. 1149-1157
    • Wolfrum, C.1    Shi, S.2    Jayaprakash, K.N.3
  • 15
    • 84884783869 scopus 로고    scopus 로고
    • Albumin as a delivery carrier for rheumatoid arthritis
    • K.Ren, A.Dusad, R.Dong, et al. Albumin as a delivery carrier for rheumatoid arthritis. J Nanomed Nanotechol. 2013;4(176):2.
    • (2013) J Nanomed Nanotechol , vol.4 , Issue.176 , pp. 2
    • Ren, K.1    Dusad, A.2    Dong, R.3
  • 16
    • 84862702122 scopus 로고    scopus 로고
    • Clinical impact of serum proteins on drug delivery
    • F.Kratz, B.Elsadek. Clinical impact of serum proteins on drug delivery. J Controlled Release. 2012;161(2):429–445.
    • (2012) J Controlled Release , vol.161 , Issue.2 , pp. 429-445
    • Kratz, F.1    Elsadek, B.2
  • 17
    • 84876367226 scopus 로고    scopus 로고
    • The novel albumin–chitosan core–shell nanoparticles for gene delivery: preparation, optimization and cell uptake investigation
    • M.Karimi, P.Avci, R.Mobasseri, et al. The novel albumin–chitosan core–shell nanoparticles for gene delivery:preparation, optimization and cell uptake investigation. J Nanopart Res. 2013;15(5):1–14.
    • (2013) J Nanopart Res , vol.15 , Issue.5 , pp. 1-14
    • Karimi, M.1    Avci, P.2    Mobasseri, R.3
  • 18
    • 84906788195 scopus 로고    scopus 로고
    • Efficient loading and entrapment of tamoxifen in human serum albumin based nanoparticulate delivery system by a modified desolvation technique
    • H.Kouchakzadeh, S.A.Shojaosadati, F.Shokri. Efficient loading and entrapment of tamoxifen in human serum albumin based nanoparticulate delivery system by a modified desolvation technique. Chem Eng Res Des. 2014;92(9):1681–1692.•• A description of efficient production of HSA nanoparticle-based tamoxifen delivery system.
    • (2014) Chem Eng Res Des , vol.92 , Issue.9 , pp. 1681-1692
    • Kouchakzadeh, H.1    Shojaosadati, S.A.2    Shokri, F.3
  • 19
    • 84891923721 scopus 로고    scopus 로고
    • Albumin‐based nanocomposite spheres for advanced drug delivery systems
    • H.E.Misak, R.Asmatulu, J.S.Gopu, et al. Albumin‐based nanocomposite spheres for advanced drug delivery systems. Biotechnol J. 2014;9(1):163–170.
    • (2014) Biotechnol J , vol.9 , Issue.1 , pp. 163-170
    • Misak, H.E.1    Asmatulu, R.2    Gopu, J.S.3
  • 20
    • 33744986992 scopus 로고    scopus 로고
    • Trastuzumab-modified nanoparticles: optimisation of preparation and uptake in cancer cells
    • I.Steinhauser, B.Spänkuch, K.Strebhardt, et al. Trastuzumab-modified nanoparticles:optimisation of preparation and uptake in cancer cells. Biomaterials. 2006;27(28):4975–4983.
    • (2006) Biomaterials , vol.27 , Issue.28 , pp. 4975-4983
    • Steinhauser, I.1    Spänkuch, B.2    Strebhardt, K.3
  • 21
    • 84956695887 scopus 로고    scopus 로고
    • Chapter four-efficient delivery of therapeutic agents by using targeted albumin nanoparticles
    • H.Kouchakzadeh, M.S.Safavi, S.A.Shojaosadati. Chapter four-efficient delivery of therapeutic agents by using targeted albumin nanoparticles. Adv Protein Chem Struct Biol. 2015;98:121–143.
    • (2015) Adv Protein Chem Struct Biol , vol.98 , pp. 121-143
    • Kouchakzadeh, H.1    Safavi, M.S.2    Shojaosadati, S.A.3
  • 22
    • 9444221978 scopus 로고    scopus 로고
    • Highly specific HER2-mediated cellular uptake of antibody-modified nanoparticles in tumour cells
    • H.Wartlick, K.Michaelis, S.Balthasar, et al. Highly specific HER2-mediated cellular uptake of antibody-modified nanoparticles in tumour cells. J Drug Target. 2004;12(7):461–471.
    • (2004) J Drug Target , vol.12 , Issue.7 , pp. 461-471
    • Wartlick, H.1    Michaelis, K.2    Balthasar, S.3
  • 23
    • 84875683581 scopus 로고    scopus 로고
    • Preparation and characterization of galactosylated bovine serum albumin nanoparticles for liver-targeted delivery of oridonin
    • C.Li, D.Zhang, H.Guo, et al. Preparation and characterization of galactosylated bovine serum albumin nanoparticles for liver-targeted delivery of oridonin. Int J Pharm. 2013;448(1):79–86.
    • (2013) Int J Pharm , vol.448 , Issue.1 , pp. 79-86
    • Li, C.1    Zhang, D.2    Guo, H.3
  • 24
    • 84879069580 scopus 로고    scopus 로고
    • Targeted drug delivery in cancer cells with red-light photoactivated mesoporous silica nanoparticles
    • S.A.Mackowiak, A.Schmidt, V.Weiss, et al. Targeted drug delivery in cancer cells with red-light photoactivated mesoporous silica nanoparticles. Nano Lett. 2013;13(6):2576–2583.
    • (2013) Nano Lett , vol.13 , Issue.6 , pp. 2576-2583
    • Mackowiak, S.A.1    Schmidt, A.2    Weiss, V.3
  • 25
    • 84877744338 scopus 로고    scopus 로고
    • Nanomaterials in cancer-therapy drug delivery system
    • G.Zhang, X.Zeng, P.Li. Nanomaterials in cancer-therapy drug delivery system. J Biomed Nanotechnol. 2013;9(5):741–750.
    • (2013) J Biomed Nanotechnol , vol.9 , Issue.5 , pp. 741-750
    • Zhang, G.1    Zeng, X.2    Li, P.3
  • 26
    • 42649132499 scopus 로고    scopus 로고
    • Protein nanoparticles as drug carriers in clinical medicine
    • M.J.Hawkins, P.Soon-Shiong, N.Desai. Protein nanoparticles as drug carriers in clinical medicine. Adv Drug Deliv Rev. 2008;60(8):876–885.
    • (2008) Adv Drug Deliv Rev , vol.60 , Issue.8 , pp. 876-885
    • Hawkins, M.J.1    Soon-Shiong, P.2    Desai, N.3
  • 27
    • 33745458519 scopus 로고    scopus 로고
    • Albumin-bound paclitaxel: a next-generation taxane
    • W.J.Gradishar. Albumin-bound paclitaxel:a next-generation taxane. Expert Opin Pharmacother. 2006;7:1041–1053.
    • (2006) Expert Opin Pharmacother , vol.7 , pp. 1041-1053
    • Gradishar, W.J.1
  • 28
    • 0026664548 scopus 로고
    • Atomic structure and chemistry of human serum albumin
    • X.M.He, D.C.Carter. 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
  • 29
    • 84877265704 scopus 로고    scopus 로고
    • Subdomain IB is the third major drug binding region of human serum albumin: toward the three-sites model
    • F.Zsila. Subdomain IB is the third major drug binding region of human serum albumin:toward the three-sites model. Mol Pharm. 2013;10(5):1668–1682.•• Introduction of subdomain IB as a new drug-binding region into the HSA protein structure.
    • (2013) Mol Pharm , vol.10 , Issue.5 , pp. 1668-1682
    • Zsila, F.1
  • 31
    • 0024372275 scopus 로고
    • Three-dimensional structure of human serum albumin
    • D.C.Carter, X.-M.He, S.H.Munson, et al. Three-dimensional structure of human serum albumin. Science. 1989;244(4909):1195–1198.
    • (1989) Science , vol.244 , Issue.4909 , pp. 1195-1198
    • Carter, D.C.1    He, X.-M.2    Munson, S.H.3
  • 32
    • 85028125410 scopus 로고    scopus 로고
    • Structural studies of several clinically important oncology drugs in complex with human serum albumin
    • W.Z-MW, J.X.Ho, J.R.Ruble, et al. Structural studies of several clinically important oncology drugs in complex with human serum albumin. Biochimica Et Biophysica Acta (Bba)-Gensubj. 2013;1830(12):5356–5374.
    • (2013) Biochimica Et Biophysica Acta (Bba)-Gensubj , vol.1830 , Issue.12 , pp. 5356-5374
    • Ho, J.X.1    Ruble, J.R.2
  • 33
    • 84855813140 scopus 로고    scopus 로고
    • Albumin-based nanoparticles as potential controlled release drug delivery systems
    • A.O.Elzoghby, W.M.Samy, N.A.Elgindy. Albumin-based nanoparticles as potential controlled release drug delivery systems. J Controlled Release. 2012;157(2):168–182.• Reviews the different types, formulation, and in vitro and in vivo studies concerning albumin DDSs.
    • (2012) J Controlled Release , vol.157 , Issue.2 , pp. 168-182
    • Elzoghby, A.O.1    Samy, W.M.2    Elgindy, N.A.3
  • 34
    • 84861558520 scopus 로고    scopus 로고
    • Characterization and side effect analysis of a newly designed nanoemulsion targeting human serum albumin for drug delivery
    • A.Divsalar, A.A.Saboury, M.Nabiuni, et al. Characterization and side effect analysis of a newly designed nanoemulsion targeting human serum albumin for drug delivery. Colloids Surf B. 2012;98:80–84.
    • (2012) Colloids Surf B , vol.98 , pp. 80-84
    • Divsalar, A.1    Saboury, A.A.2    Nabiuni, M.3
  • 35
    • 84902665558 scopus 로고    scopus 로고
    • Pt (IV) prodrugs designed to bind non-covalently to human serum albumin for drug delivery
    • Y.-R.Zheng, K.Suntharalingam, T.C.Johnstone, et al. Pt (IV) prodrugs designed to bind non-covalently to human serum albumin for drug delivery. J Am Chem Soc. 2014;136(24):8790–8798.
    • (2014) J Am Chem Soc , vol.136 , Issue.24 , pp. 8790-8798
    • Zheng, Y.-R.1    Suntharalingam, K.2    Johnstone, T.C.3
  • 36
    • 33644681693 scopus 로고    scopus 로고
    • Stereoselective binding of human serum albumin
    • V.T.G.Chuang, M.Otagiri. Stereoselective binding of human serum albumin. Chirality. 2006;18(3):159–166.
    • (2006) Chirality , vol.18 , Issue.3 , pp. 159-166
    • Chuang, V.T.G.1    Otagiri, M.2
  • 37
    • 84912076277 scopus 로고    scopus 로고
    • Inhalable self-assembled albumin nanoparticles for treating drug-resistant lung cancer
    • S.H.Choi, H.J.Byeon, J.S.Choi, et al. Inhalable self-assembled albumin nanoparticles for treating drug-resistant lung cancer. J Controlled Release. 2015;197:199–207.• Uses octyl aldehyde, doxorubicin, and TRAIL protein to form composite HSA NPs that can be inhaled, and studies the anticancer effects.
    • (2015) J Controlled Release , vol.197 , pp. 199-207
    • Choi, S.H.1    Byeon, H.J.2    Choi, J.S.3
  • 38
    • 83355162399 scopus 로고    scopus 로고
    • Doxorubicin-loaded human serum albumin nanoparticles surface-modified with TNF-related apoptosis-inducing ligand and transferrin for targeting multiple tumor types
    • S.Bae, K.Ma, T.H.Kim, et al. Doxorubicin-loaded human serum albumin nanoparticles surface-modified with TNF-related apoptosis-inducing ligand and transferrin for targeting multiple tumor types. Biomaterials. 2012;33(5):1536–1546.
    • (2012) Biomaterials , vol.33 , Issue.5 , pp. 1536-1546
    • Bae, S.1    Ma, K.2    Kim, T.H.3
  • 39
    • 0035845748 scopus 로고    scopus 로고
    • Poly (ethylene glycol)–human serum albumin–paclitaxel conjugates: preparation, characterization and pharmacokinetics
    • F.Dosio, S.Arpicco, P.Brusa, et al. Poly (ethylene glycol)–human serum albumin–paclitaxel conjugates:preparation, characterization and pharmacokinetics. J Controlled Release. 2001;76(1):107–117.
    • (2001) J Controlled Release , vol.76 , Issue.1 , pp. 107-117
    • Dosio, F.1    Arpicco, S.2    Brusa, P.3
  • 40
    • 84894483438 scopus 로고    scopus 로고
    • Glucose‐and pH‐responsive controlled release of cargo from protein‐gated carbohydrate‐functionalized mesoporous silica nanocontainers
    • S.Wu, X.Huang, X.Du. Glucose‐and pH‐responsive controlled release of cargo from protein‐gated carbohydrate‐functionalized mesoporous silica nanocontainers. Angewandte Chemie. 2013;125(21):5690–5694.
    • (2013) Angewandte Chemie , vol.125 , Issue.21 , pp. 5690-5694
    • Wu, S.1    Huang, X.2    Du, X.3
  • 41
    • 84923079818 scopus 로고    scopus 로고
    • Bovine serum albumin nanoparticles for delivery of tacrolimus to reduce its kidney uptake and functional nephrotoxicity
    • L.Zhao, Y.Zhou, Y.Gao, et al. Bovine serum albumin nanoparticles for delivery of tacrolimus to reduce its kidney uptake and functional nephrotoxicity. Int J Pharm. 2015;483(1):180–187.
    • (2015) Int J Pharm , vol.483 , Issue.1 , pp. 180-187
    • Zhao, L.1    Zhou, Y.2    Gao, Y.3
  • 42
    • 0027371531 scopus 로고
    • Determination of the magnitude and enantioselectivity of ligand binding to rat and rabbit serum albumins using immobilized-protein high performance liquid chromatography stationary phases
    • G.Massolini, A.-F.Aubry, A.Mcgann, et al. Determination of the magnitude and enantioselectivity of ligand binding to rat and rabbit serum albumins using immobilized-protein high performance liquid chromatography stationary phases. Biochem Pharmacol. 1993;46(7):1285–1293.
    • (1993) Biochem Pharmacol , vol.46 , Issue.7 , pp. 1285-1293
    • Massolini, G.1    Aubry, A.-F.2    Mcgann, A.3
  • 44
    • 84923845180 scopus 로고    scopus 로고
    • Structural properties of condensed ovalbumin systems following application of high pressure
    • S.Savadkoohi, A.Bannikova, N.Mantri, et al. Structural properties of condensed ovalbumin systems following application of high pressure. Food Hydrocoll. 2014;53:104–114.
    • (2014) Food Hydrocoll , vol.53 , pp. 104-114
    • Savadkoohi, S.1    Bannikova, A.2    Mantri, N.3
  • 45
    • 84908393452 scopus 로고    scopus 로고
    • Phase separation behavior and structural analysis of ovalbumin–gum arabic complex coacervation
    • F.Niu, Y.Dong, F.Shen, et al. Phase separation behavior and structural analysis of ovalbumin–gum arabic complex coacervation. Food Hydrocoll. 2014;43:1–7.
    • (2014) Food Hydrocoll , vol.43 , pp. 1-7
    • Niu, F.1    Dong, Y.2    Shen, F.3
  • 46
    • 62549146577 scopus 로고    scopus 로고
    • Antigen delivery with poly (propylacrylic acid) conjugation enhances MHC-1 presentation and T-cell activation
    • S.Flanary, A.S.Hoffman, P.S.Stayton. Antigen delivery with poly (propylacrylic acid) conjugation enhances MHC-1 presentation and T-cell activation. Bioconjug Chem. 2009;20(2):241–248.
    • (2009) Bioconjug Chem , vol.20 , Issue.2 , pp. 241-248
    • Flanary, S.1    Hoffman, A.S.2    Stayton, P.S.3
  • 47
    • 0028227096 scopus 로고
    • Structure of serum albumin
    • D.C.Carter, J.X.Ho. Structure of serum albumin. Adv Protein Chem. 1994;45(45):153–203.
    • (1994) Adv Protein Chem , vol.45 , Issue.45 , pp. 153-203
    • Carter, D.C.1    Ho, J.X.2
  • 48
    • 0036828938 scopus 로고    scopus 로고
    • Predicting plasma protein binding of drugs: a new approach
    • N.A.Kratochwil, W.Huber, F.Müller, et al. Predicting plasma protein binding of drugs:a new approach. Biochem Pharmacol. 2002;64(9):1355–1374.
    • (2002) Biochem Pharmacol , vol.64 , Issue.9 , pp. 1355-1374
    • Kratochwil, N.A.1    Huber, W.2    Müller, F.3
  • 49
    • 36849050779 scopus 로고    scopus 로고
    • Structural and ligand‐binding properties of serum albumin species interacting with a biomembrane interface
    • T.Kosa, K.Nishi, T.Maruyama, et al. Structural and ligand‐binding properties of serum albumin species interacting with a biomembrane interface. J Pharm Sci. 2007;96(11):3117–3124.
    • (2007) J Pharm Sci , vol.96 , Issue.11 , pp. 3117-3124
    • Kosa, T.1    Nishi, K.2    Maruyama, T.3
  • 50
    • 11844253806 scopus 로고    scopus 로고
    • Flavonoid–serum albumin complexation: determination of binding constants and binding sites by fluorescence spectroscopy
    • C.Dufour, O.Dangles. Flavonoid–serum albumin complexation:determination of binding constants and binding sites by fluorescence spectroscopy. Biochimica Et Biophysica Acta (Bba)-Gensubj. 2005;1721(1):164–173.
    • (2005) Biochimica Et Biophysica Acta (Bba)-Gensubj , vol.1721 , Issue.1 , pp. 164-173
    • Dufour, C.1    Dangles, O.2
  • 51
    • 84991298623 scopus 로고    scopus 로고
    • Albumin binding sites for evaluating drug interactions and methods of evaluating or designing drugs based on their albumin binding properties
    • D.Carter, J.Ho, Z.Wang Albumin binding sites for evaluating drug interactions and methods of evaluating or designing drugs based on their albumin binding properties. Google Patents. 2004.
    • (2004) Google Patents
    • Carter, D.1    Ho, J.2    Wang, Z.3
  • 52
    • 84858289984 scopus 로고    scopus 로고
    • Crystallographic survey of albumin drug interaction and preliminary applications in cancer chemotherapy
    • D.C.Carter. Crystallographic survey of albumin drug interaction and preliminary applications in cancer chemotherapy. Burger’s Med Chem Drug Discov. 2010;437–468. doi:10.1002/0471266949.bmc166
    • (2010) Burger’s Med Chem Drug Discov , pp. 437-468
    • Carter, D.C.1
  • 53
    • 0026768567 scopus 로고
    • A comparison of drug binding sites on mammalian albumins
    • M.R.Panjehshahin, M.S.Yates, C.J.Bowmer. A comparison of drug binding sites on mammalian albumins. Biochem Pharmacol. 1992;44(5):873–879.
    • (1992) Biochem Pharmacol , vol.44 , Issue.5 , pp. 873-879
    • Panjehshahin, M.R.1    Yates, M.S.2    Bowmer, C.J.3
  • 54
    • 84986392752 scopus 로고
    • Peptides isolated from tryptic and chymotryptic digest of fragment CB6 (Pro) of human plasma albumin
    • L.Morávek, V.Kostka, M.Saber, et al. Peptides isolated from tryptic and chymotryptic digest of fragment CB6 (Pro) of human plasma albumin. Collect Czechoslov Chem Commun. 1975;40(4):1103–1111.
    • (1975) Collect Czechoslov Chem Commun , vol.40 , Issue.4 , pp. 1103-1111
    • Morávek, L.1    Kostka, V.2    Saber, M.3
  • 55
    • 84885477849 scopus 로고    scopus 로고
    • Binding, unfolding and refolding dynamics of serum albumins
    • U.Anand, S.Mukherjee. Binding, unfolding and refolding dynamics of serum albumins. Biochimica Et Biophysica Acta (Bba)-Gensubj. 2013;1830(12):5394–5404.
    • (2013) Biochimica Et Biophysica Acta (Bba)-Gensubj , vol.1830 , Issue.12 , pp. 5394-5404
    • Anand, U.1    Mukherjee, S.2
  • 56
    • 0033992170 scopus 로고    scopus 로고
    • Desolvation process and surface characterisation of protein nanoparticles
    • C.Weber, C.Coester, J.Kreuter, et al. Desolvation process and surface characterisation of protein nanoparticles. Int J Pharm. 2000;194(1):91–102.
    • (2000) Int J Pharm , vol.194 , Issue.1 , pp. 91-102
    • Weber, C.1    Coester, C.2    Kreuter, J.3
  • 57
    • 84906524526 scopus 로고    scopus 로고
    • The effect of different desolvating agents on BSA nanoparticle properties and encapsulation of curcumin
    • R.Sadeghi, A.Moosavi-Movahedi, Z.Emam-jomeh, et al. The effect of different desolvating agents on BSA nanoparticle properties and encapsulation of curcumin. J Nanoparticle Res. 2014;16(9):1–14.
    • (2014) J Nanoparticle Res , vol.16 , Issue.9 , pp. 1-14
    • Sadeghi, R.1    Moosavi-Movahedi, A.2    Emam-jomeh, Z.3
  • 58
    • 84888354180 scopus 로고    scopus 로고
    • Preparation of Bovine Serum Albumin (BSA) nanoparticles by desolvation using a membrane contactor: A new tool for large scale production
    • B.Yedomon, H.Fessi, C.Charcosset. Preparation of Bovine Serum Albumin (BSA) nanoparticles by desolvation using a membrane contactor:A new tool for large scale production. Eur J Pharmaceutics Biopharmaceutics. 2013;85(3):398–405.
    • (2013) Eur J Pharmaceutics Biopharmaceutics , vol.85 , Issue.3 , pp. 398-405
    • Yedomon, B.1    Fessi, H.2    Charcosset, C.3
  • 59
    • 80052040096 scopus 로고    scopus 로고
    • Preparation, characterization and targeting of micronized 10-hydroxycamptothecin-loaded folate-conjugated human serum albumin nanoparticles to cancer cells
    • Q.Y.Li, C.Liu, X.H.Zhao, et al. Preparation, characterization and targeting of micronized 10-hydroxycamptothecin-loaded folate-conjugated human serum albumin nanoparticles to cancer cells. Int J Nanomedicine. 2011;6:397–405.•• Reports a method for cancer cell targeting using folate-conjugated HSA NPs loaded with 10-hydroxycamptothecin.
    • (2011) Int J Nanomedicine , vol.6 , pp. 397-405
    • Li, Q.Y.1    Liu, C.2    Zhao, X.H.3
  • 60
    • 84960385935 scopus 로고    scopus 로고
    • Preparation of albumin based nanoparticles for delivery of fisetin and evaluation of its cytotoxic activity
    • P.Ghosh, A.S.Roy, S.Chaudhury, et al. Preparation of albumin based nanoparticles for delivery of fisetin and evaluation of its cytotoxic activity. Int J Biol Macromol. 2016;86:408–417.
    • (2016) Int J Biol Macromol , vol.86 , pp. 408-417
    • Ghosh, P.1    Roy, A.S.2    Chaudhury, S.3
  • 61
    • 84923363133 scopus 로고    scopus 로고
    • The potential use of lapatinib-loaded human serum albumin nanoparticles in the treatment of triple-negative breast cancer
    • X.Wan, X.Zheng, X.Pang, et al. The potential use of lapatinib-loaded human serum albumin nanoparticles in the treatment of triple-negative breast cancer. Int J Pharm. 2015;484(1):16–28.
    • (2015) Int J Pharm , vol.484 , Issue.1 , pp. 16-28
    • Wan, X.1    Zheng, X.2    Pang, X.3
  • 62
    • 84938388018 scopus 로고    scopus 로고
    • Long-circulating self-assembled cholesteryl albumin nanoparticles enhance tumor accumulation of hydrophobic anticancer drug
    • G.Battogtokh, J.H.Kang, Y.T.Ko. Long-circulating self-assembled cholesteryl albumin nanoparticles enhance tumor accumulation of hydrophobic anticancer drug. Eur J Pharmaceutics Biopharmaceutics. 2015;96:96–105.
    • (2015) Eur J Pharmaceutics Biopharmaceutics , vol.96 , pp. 96-105
    • Battogtokh, G.1    Kang, J.H.2    Ko, Y.T.3
  • 63
    • 84937787787 scopus 로고    scopus 로고
    • Dual-peptide-functionalized albumin-based nanoparticles with pH-dependent self-assembly behavior for drug delivery
    • B.Chen, X.-Y.He, X.-Q.Yi, et al. Dual-peptide-functionalized albumin-based nanoparticles with pH-dependent self-assembly behavior for drug delivery. ACS Appl Mater Interfaces. 2015;7(28):15148–15153.
    • (2015) ACS Appl Mater Interfaces , vol.7 , Issue.28 , pp. 15148-15153
    • Chen, B.1    He, X.-Y.2    Yi, X.-Q.3
  • 64
    • 84931260741 scopus 로고    scopus 로고
    • nab-Paclitaxel dose and schedule in breast cancer
    • M.Martín. nab-Paclitaxel dose and schedule in breast cancer. Breast Cancer Res. 2015;17(1):1–10.
    • (2015) Breast Cancer Res , vol.17 , Issue.1 , pp. 1-10
    • Martín, M.1
  • 65
    • 84991298508 scopus 로고    scopus 로고
    • Delta-tocotrienol potentiates the antitumor activity of standard chemotherapy with gemcitabine and abraxane in metastatic pancreatic cancer
    • K.Husain, S.M.Sebti, M.P.Malafa. Delta-tocotrienol potentiates the antitumor activity of standard chemotherapy with gemcitabine and abraxane in metastatic pancreatic cancer. Cancer Res. 2014;74(19 Supplement):1699–99.
    • (2014) Cancer Res , vol.74 , pp. 1699
    • Husain, K.1    Sebti, S.M.2    Malafa, M.P.3
  • 66
    • 84924663015 scopus 로고    scopus 로고
    • Evaluation of berberine/bovine serum albumin nanoparticles for liver fibrosis therapy
    • P.-L.Lam, S.-L.Kok, R.Gambari, et al. Evaluation of berberine/bovine serum albumin nanoparticles for liver fibrosis therapy. Green Chem. 2015;17(3):1640–1646.
    • (2015) Green Chem , vol.17 , Issue.3 , pp. 1640-1646
    • Lam, P.-L.1    Kok, S.-L.2    Gambari, R.3
  • 67
    • 48349096755 scopus 로고    scopus 로고
    • Effect of trastuzumab-modified antisense oligonucleotide-loaded human serum albumin nanoparticles prepared by heat denaturation
    • I.M.Steinhauser, K.Langer, K.M.Strebhardt, et al. Effect of trastuzumab-modified antisense oligonucleotide-loaded human serum albumin nanoparticles prepared by heat denaturation. Biomaterials. 2008;29(29):4022–4028.
    • (2008) Biomaterials , vol.29 , Issue.29 , pp. 4022-4028
    • Steinhauser, I.M.1    Langer, K.2    Strebhardt, K.M.3
  • 68
    • 79961154440 scopus 로고    scopus 로고
    • Review on microparticulate drug delivery system
    • N.S.Madhav, S.Kala. Review on microparticulate drug delivery system. Int J PharmTech Res. 2011;3:1242–1254.
    • (2011) Int J PharmTech Res , vol.3 , pp. 1242-1254
    • Madhav, N.S.1    Kala, S.2
  • 69
    • 84865478439 scopus 로고    scopus 로고
    • A review of delivery systems in cosmetics
    • F.G.Hougeir, L.Kircik. A review of delivery systems in cosmetics. Dermatol Ther. 2012;25(3):234–237.
    • (2012) Dermatol Ther , vol.25 , Issue.3 , pp. 234-237
    • Hougeir, F.G.1    Kircik, L.2
  • 70
    • 70449558745 scopus 로고    scopus 로고
    • Formulation and in vitro characterization of spray-dried antisense oligonucleotide to NF-κ B encapsulated albumin microspheres
    • S.G.Gayakwad, N.K.Bejugam, N.Akhavein, et al. Formulation and in vitro characterization of spray-dried antisense oligonucleotide to NF-κ B encapsulated albumin microspheres. J Microencapsul. 2009;26(8):692–700.
    • (2009) J Microencapsul , vol.26 , Issue.8 , pp. 692-700
    • Gayakwad, S.G.1    Bejugam, N.K.2    Akhavein, N.3
  • 71
    • 0026488546 scopus 로고
    • Topical application of albumin microspheres containing vitamin A drug release and availability
    • S.Torrado, J.J.Torrado, R.Cadórniga. Topical application of albumin microspheres containing vitamin A drug release and availability. Int J Pharm. 1992;86(2):147–152.
    • (1992) Int J Pharm , vol.86 , Issue.2 , pp. 147-152
    • Torrado, S.1    Torrado, J.J.2    Cadórniga, R.3
  • 72
    • 84938215932 scopus 로고    scopus 로고
    • Arginine-conjugated albumin microspheres inhibits proliferation and migration in lung cancer cells
    • H.-Y.Lee, K.A.Mohammed, E.P.Goldberg, et al. Arginine-conjugated albumin microspheres inhibits proliferation and migration in lung cancer cells. Am J Cancer Res. 2013;3(3):266.
    • (2013) Am J Cancer Res , vol.3 , Issue.3 , pp. 266
    • Lee, H.-Y.1    Mohammed, K.A.2    Goldberg, E.P.3
  • 73
    • 56049114432 scopus 로고    scopus 로고
    • Novel microbubble preparation technologies
    • E.Stride, M.Edirisinghe. Novel microbubble preparation technologies. Soft Matter. 2008;4(12):2350–2359.
    • (2008) Soft Matter , vol.4 , Issue.12 , pp. 2350-2359
    • Stride, E.1    Edirisinghe, M.2
  • 74
    • 79958035832 scopus 로고    scopus 로고
    • A novel transfection method for eukaryotic cells using polyethylenimine coated albumin microbubbles
    • S.-P.Dang, R.-X.Wang, Y.Zhang, et al. A novel transfection method for eukaryotic cells using polyethylenimine coated albumin microbubbles. Plasmid. 2011;66(1):19–25.
    • (2011) Plasmid , vol.66 , Issue.1 , pp. 19-25
    • Dang, S.-P.1    Wang, R.-X.2    Zhang, Y.3
  • 76
    • 3042544619 scopus 로고    scopus 로고
    • Microbubbles in medical imaging: current applications and future directions
    • J.R.Lindner. Microbubbles in medical imaging:current applications and future directions. Nat Rev Drug Discov. 2004;3(6):527–533.
    • (2004) Nat Rev Drug Discov , vol.3 , Issue.6 , pp. 527-533
    • Lindner, J.R.1
  • 77
    • 44249105593 scopus 로고    scopus 로고
    • Microbubbles in ultrasound-triggered drug and gene delivery
    • S.Hernot, A.L.Klibanov. Microbubbles in ultrasound-triggered drug and gene delivery. Adv Drug Deliv Rev. 2008;60(10):1153–1166.
    • (2008) Adv Drug Deliv Rev , vol.60 , Issue.10 , pp. 1153-1166
    • Hernot, S.1    Klibanov, A.L.2
  • 78
    • 84863800625 scopus 로고    scopus 로고
    • Microencapsulated drug delivery: a new approach to pro-inflammatory cytokine inhibition
    • C.W.Oettinger, M.J.D’souza. Microencapsulated drug delivery:a new approach to pro-inflammatory cytokine inhibition. J Microencapsul. 2012;29(5):455–462.
    • (2012) J Microencapsul , vol.29 , Issue.5 , pp. 455-462
    • Oettinger, C.W.1    D’souza, M.J.2
  • 79
    • 84859105871 scopus 로고    scopus 로고
    • Folic acid-functionalized human serum albumin nanocapsules for targeted drug delivery to chronically activated macrophages
    • A.Rollett, T.Reiter, P.Nogueira, et al. Folic acid-functionalized human serum albumin nanocapsules for targeted drug delivery to chronically activated macrophages. Int J Pharm. 2012;427(2):460–466.
    • (2012) Int J Pharm , vol.427 , Issue.2 , pp. 460-466
    • Rollett, A.1    Reiter, T.2    Nogueira, P.3
  • 80
    • 75749128139 scopus 로고    scopus 로고
    • Increased stability in plasma and enhanced cellular uptake of thermally denatured albumin-coated liposomes
    • S.H.Jung, S.K.Kim, S.H.Jung, et al. Increased stability in plasma and enhanced cellular uptake of thermally denatured albumin-coated liposomes. Colloids Surf B. 2010;76(2):434–440.
    • (2010) Colloids Surf B , vol.76 , Issue.2 , pp. 434-440
    • Jung, S.H.1    Kim, S.K.2    Jung, S.H.3
  • 81
    • 84866256041 scopus 로고    scopus 로고
    • Growth inhibition and chemosensitization of human carcinoma cells by human serum albumin-coated liposomal antisense oligodeoxyribonucleotide against bcl-2
    • W.Weecharangsan, R.J.Lee. Growth inhibition and chemosensitization of human carcinoma cells by human serum albumin-coated liposomal antisense oligodeoxyribonucleotide against bcl-2. Drug Deliv. 2012;19(6):292–297.
    • (2012) Drug Deliv , vol.19 , Issue.6 , pp. 292-297
    • Weecharangsan, W.1    Lee, R.J.2
  • 82
    • 0038555755 scopus 로고    scopus 로고
    • Biopolymer albumin for diagnosis and in drug delivery
    • G.V.Patil. Biopolymer albumin for diagnosis and in drug delivery. Drug Dev Res. 2003;58(3):219–247.
    • (2003) Drug Dev Res , vol.58 , Issue.3 , pp. 219-247
    • Patil, G.V.1
  • 83
    • 0037274873 scopus 로고    scopus 로고
    • Cardiac toxicity of antineoplastic anthracyclines
    • R.Zucchi, R.Danesi. Cardiac toxicity of antineoplastic anthracyclines. Curr Med Chem Anticancer Agents. 2003;3:151–171.
    • (2003) Curr Med Chem Anticancer Agents , vol.3 , pp. 151-171
    • Zucchi, R.1    Danesi, R.2
  • 84
    • 34248529700 scopus 로고    scopus 로고
    • Influence of the formulation on the tolerance profile of nanoparticle-bound doxorubicin in healthy rats: focus on cardio- and testicular toxicity
    • E.Pereverzeva, I.Treschalin, D.Bodyagin, et al. Influence of the formulation on the tolerance profile of nanoparticle-bound doxorubicin in healthy rats:focus on cardio- and testicular toxicity. Int J Pharm. 2007;337(1–2):346–356.•• Evaluation of the cardiotoxicity and testicular toxicity of doxorubicin-loaded HSA NPs.
    • (2007) Int J Pharm , vol.337 , Issue.1-2 , pp. 346-356
    • Pereverzeva, E.1    Treschalin, I.2    Bodyagin, D.3
  • 85
    • 78649903242 scopus 로고    scopus 로고
    • Optimization of PEGylation conditions for BSA nanoparticles using response surface methodology
    • H.Kouchakzadeh, S.A.Shojaosadati, A.Maghsoudi, et al. Optimization of PEGylation conditions for BSA nanoparticles using response surface methodology. AAPS PharmSciTech. 2010;11(3):1206–1211.
    • (2010) AAPS PharmSciTech , vol.11 , Issue.3 , pp. 1206-1211
    • Kouchakzadeh, H.1    Shojaosadati, S.A.2    Maghsoudi, A.3
  • 86
    • 0035848399 scopus 로고    scopus 로고
    • Preparation and characterisation of rose Bengal-loaded surface-modified albumin nanoparticles
    • W.Lin, M.C.Garnett, S.S.Davis, et al. Preparation and characterisation of rose Bengal-loaded surface-modified albumin nanoparticles. J Controlled Release. 2001;71(1):117–126.
    • (2001) J Controlled Release , vol.71 , Issue.1 , pp. 117-126
    • Lin, W.1    Garnett, M.C.2    Davis, S.S.3
  • 87
    • 70649083100 scopus 로고    scopus 로고
    • Polyethylenimine-PEG coated albumin nanoparticles for BMP-2 delivery
    • S.F.Zhang, C.Kucharski, M.R.Doschak, et al. Polyethylenimine-PEG coated albumin nanoparticles for BMP-2 delivery. Biomaterials. 2010;31(5):952–963.
    • (2010) Biomaterials , vol.31 , Issue.5 , pp. 952-963
    • Zhang, S.F.1    Kucharski, C.2    Doschak, M.R.3
  • 88
    • 84870244558 scopus 로고    scopus 로고
    • Folate-mediated delivery of macromolecular anticancer therapeutic agents
    • Y.Lu, P.S.Low. Folate-mediated delivery of macromolecular anticancer therapeutic agents. Adv Drug Deliv Rev. 2012;64:342–352.
    • (2012) Adv Drug Deliv Rev , vol.64 , pp. 342-352
    • Lu, Y.1    Low, P.S.2
  • 89
    • 79952118190 scopus 로고    scopus 로고
    • Preparation, characterization, and in vitro targeted delivery of folate-decorated paclitaxel-loaded bovine serum albumin nanoparticles
    • D.M.Zhao, X.H.Zhao, Y.G.Zu, et al. Preparation, characterization, and in vitro targeted delivery of folate-decorated paclitaxel-loaded bovine serum albumin nanoparticles. Int J Nanomedicine. 2010;5:669–677.
    • (2010) Int J Nanomedicine , vol.5 , pp. 669-677
    • Zhao, D.M.1    Zhao, X.H.2    Zu, Y.G.3
  • 90
    • 79151482015 scopus 로고    scopus 로고
    • Improved drug targeting of cancer cells by utilizing actively targetable folic acid-conjugated albumin nanospheres
    • Z.Y.Shen, Y.Li, K.Kohama, et al. Improved drug targeting of cancer cells by utilizing actively targetable folic acid-conjugated albumin nanospheres. Pharmacological Res. 2011;63(1):51–58.
    • (2011) Pharmacological Res , vol.63 , Issue.1 , pp. 51-58
    • Shen, Z.Y.1    Li, Y.2    Kohama, K.3
  • 91
    • 67349121612 scopus 로고    scopus 로고
    • Albumin nanoparticles targeted with Apo E enter the CNS by transcytosis and are delivered to neurones
    • A.Zensi, D.Begley, C.Pontikis, et al. Albumin nanoparticles targeted with Apo E enter the CNS by transcytosis and are delivered to neurones. J Controlled Release. 2009;137(1):78–86.
    • (2009) J Controlled Release , vol.137 , Issue.1 , pp. 78-86
    • Zensi, A.1    Begley, D.2    Pontikis, C.3
  • 92
    • 33847116764 scopus 로고    scopus 로고
    • Covalent attachment of apolipoprotein A-I and apolipoprotein B-100 to albumin nanoparticles enables drug transport into the brain
    • J.Kreuter, T.Hekmatara, S.Dreis, et al. Covalent attachment of apolipoprotein A-I and apolipoprotein B-100 to albumin nanoparticles enables drug transport into the brain. J Controlled Release. 2007;118(1):54–58.• Invokes multiple mechanisms for interactions of NPs with the central nervous system.
    • (2007) J Controlled Release , vol.118 , Issue.1 , pp. 54-58
    • Kreuter, J.1    Hekmatara, T.2    Dreis, S.3
  • 93
    • 84857747571 scopus 로고    scopus 로고
    • Uptake mechanism of ApoE-modified nanoparticles on brain capillary endothelial cells as a blood-brain barrier model
    • S.Wagner, A.Zensi, S.L.Wien, et al. Uptake mechanism of ApoE-modified nanoparticles on brain capillary endothelial cells as a blood-brain barrier model. Plos One. 2012;7(3):e32568.
    • (2012) Plos One , vol.7 , Issue.3
    • Wagner, S.1    Zensi, A.2    Wien, S.L.3
  • 94
    • 33646796753 scopus 로고    scopus 로고
    • Covalent linkage of apolipoprotein E to albumin nanoparticles strongly enhances drug transport into the brain
    • K.Michaelis, M.M.Hoffmann, S.Dreis, et al. Covalent linkage of apolipoprotein E to albumin nanoparticles strongly enhances drug transport into the brain. J Pharmacol Exp Ther. 2006;317(3):1246–1253.
    • (2006) J Pharmacol Exp Ther , vol.317 , Issue.3 , pp. 1246-1253
    • Michaelis, K.1    Hoffmann, M.M.2    Dreis, S.3
  • 95
    • 58149098874 scopus 로고    scopus 로고
    • Specific targeting of HER2 overexpressing breast cancer cells with doxorubicin-loaded trastuzumab-modified human serum albumin nanoparticles
    • M.G.Anhorn, S.Wagner, J.Kreuter, et al. Specific targeting of HER2 overexpressing breast cancer cells with doxorubicin-loaded trastuzumab-modified human serum albumin nanoparticles. Bioconjug Chem. 2008;19(12):2321–2331.
    • (2008) Bioconjug Chem , vol.19 , Issue.12 , pp. 2321-2331
    • Anhorn, M.G.1    Wagner, S.2    Kreuter, J.3
  • 96
    • 84874940184 scopus 로고    scopus 로고
    • Optimization of an anti-HER2 monoclonal antibody targeted delivery system using PEGylated human serum albumin nanoparticles
    • H.Kouchakzadeh, S.A.Shojaosadati, F.Tahmasebi, et al. Optimization of an anti-HER2 monoclonal antibody targeted delivery system using PEGylated human serum albumin nanoparticles. Int J Pharm. 2013;447(1–2):62–69.
    • (2013) Int J Pharm , vol.447 , Issue.1-2 , pp. 62-69
    • Kouchakzadeh, H.1    Shojaosadati, S.A.2    Tahmasebi, F.3
  • 97
    • 79960703255 scopus 로고    scopus 로고
    • Targeted human serum albumin nanoparticles for specific uptake in EGFR-expressing colon carcinoma cells
    • K.Löw, M.Wacker, S.Wagner, et al. Targeted human serum albumin nanoparticles for specific uptake in EGFR-expressing colon carcinoma cells. Nanomedicine. 2011;7:454–463.•• Describes the targeted accumulation of albumin NPs in EGFR-expressing cancer cells.
    • (2011) Nanomedicine , vol.7 , pp. 454-463
    • Löw, K.1    Wacker, M.2    Wagner, S.3
  • 98
    • 74449089443 scopus 로고    scopus 로고
    • Enhanced drug targeting by attachment of an anti alpha v integrin antibody to doxorubicin loaded human serum albumin nanoparticles
    • S.Wagner, F.Rothweiler, M.G.Anhorn, et al. Enhanced drug targeting by attachment of an anti alpha v integrin antibody to doxorubicin loaded human serum albumin nanoparticles. Biomaterials. 2010;31(8):2388–2398.
    • (2010) Biomaterials , vol.31 , Issue.8 , pp. 2388-2398
    • Wagner, S.1    Rothweiler, F.2    Anhorn, M.G.3
  • 99
    • 85027921424 scopus 로고    scopus 로고
    • Chapter one-protein–and peptide–drug conjugates: an emerging drug delivery technology
    • I.Vhora, S.Patil, P.Bhatt, et al. Chapter one-protein–and peptide–drug conjugates:an emerging drug delivery technology. Adv Protein Chem Struct Biol. 2015;98:1–55.
    • (2015) Adv Protein Chem Struct Biol , vol.98 , pp. 1-55
    • Vhora, I.1    Patil, S.2    Bhatt, P.3
  • 101
    • 0033674934 scopus 로고    scopus 로고
    • Ganciclovir-loaded albumin nanoparticles: characterization and in vitro release properties
    • M.Merodio, A.Arnedo, M.J.Renedo, et al. Ganciclovir-loaded albumin nanoparticles:characterization and in vitro release properties. Eur J Pharm Sci. 2001;12(3):251–259.
    • (2001) Eur J Pharm Sci , vol.12 , Issue.3 , pp. 251-259
    • Merodio, M.1    Arnedo, A.2    Renedo, M.J.3
  • 102
    • 0347996094 scopus 로고    scopus 로고
    • Albumin nanoparticles improved the stability, nuclear accumulation and anticytomegaloviral activity of a phosphodiester oligonucleotide
    • A.Arnedo, J.Irache, M.Merodio, et al. Albumin nanoparticles improved the stability, nuclear accumulation and anticytomegaloviral activity of a phosphodiester oligonucleotide. J Controlled Release. 2004;94(1):217–227.
    • (2004) J Controlled Release , vol.94 , Issue.1 , pp. 217-227
    • Arnedo, A.1    Irache, J.2    Merodio, M.3
  • 103
    • 80455134830 scopus 로고    scopus 로고
    • Albumin nanoparticles carrying cyclodextrins for nasal delivery of the anti-Alzheimer drug tacrine
    • B.Luppi, F.Bigucci, G.Corace, et al. Albumin nanoparticles carrying cyclodextrins for nasal delivery of the anti-Alzheimer drug tacrine. Eur J Pharm Sci. 2011;44(4):559–565.
    • (2011) Eur J Pharm Sci , vol.44 , Issue.4 , pp. 559-565
    • Luppi, B.1    Bigucci, F.2    Corace, G.3
  • 104
    • 14744297235 scopus 로고    scopus 로고
    • Albumin nanoparticles for the intravitreal delivery of anticytomegaloviral drugs
    • J.Irache, M.Merodio, A.Arnedo, et al. Albumin nanoparticles for the intravitreal delivery of anticytomegaloviral drugs. Mini Rev Med Chem. 2005;5(3):293–305.
    • (2005) Mini Rev Med Chem , vol.5 , Issue.3 , pp. 293-305
    • Irache, J.1    Merodio, M.2    Arnedo, A.3
  • 105
    • 84866564523 scopus 로고    scopus 로고
    • Nanoparticles based on albumin: preparation, characterization and the use for 5-flurouracil delivery
    • B.Wilson, T.Ambika, R.D.K.Patel, et al. Nanoparticles based on albumin:preparation, characterization and the use for 5-flurouracil delivery. Int J Biol Macromol. 2012;51(5):874–878.
    • (2012) Int J Biol Macromol , vol.51 , Issue.5 , pp. 874-878
    • Wilson, B.1    Ambika, T.2    Patel, R.D.K.3
  • 106
    • 37349029650 scopus 로고    scopus 로고
    • Preparation and characterization of sodium ferulate entrapped bovine serum albumin nanoparticles for liver targeting
    • F.-Q.Li, H.Su, J.Wang, et al. Preparation and characterization of sodium ferulate entrapped bovine serum albumin nanoparticles for liver targeting. Int J Pharm. 2008;349(1):274–282.
    • (2008) Int J Pharm , vol.349 , Issue.1 , pp. 274-282
    • Li, F.-Q.1    Su, H.2    Wang, J.3
  • 107
    • 84904792690 scopus 로고    scopus 로고
    • Albumin nanoparticles for the delivery of gabapentin: preparation, characterization and pharmacodynamic studies
    • B.Wilson, Y.Lavanya, S.Priyadarshini, et al. Albumin nanoparticles for the delivery of gabapentin:preparation, characterization and pharmacodynamic studies. Int J Pharm. 2014;473(1):73–79.•• Enhanced the concentration of an antiepileptic drug in the brain by delivery with albumin NPs.
    • (2014) Int J Pharm , vol.473 , Issue.1 , pp. 73-79
    • Wilson, B.1    Lavanya, Y.2    Priyadarshini, S.3
  • 108
    • 79952118190 scopus 로고    scopus 로고
    • Preparation, characterization, and in vitro targeted delivery of folate-decorated paclitaxel-loaded bovine serum albumin nanoparticles
    • D.Zhao, X.Zhao, Y.Zu, et al. Preparation, characterization, and in vitro targeted delivery of folate-decorated paclitaxel-loaded bovine serum albumin nanoparticles. Int J Nanomedicine. 2010;5:669.
    • (2010) Int J Nanomedicine , vol.5 , pp. 669
    • Zhao, D.1    Zhao, X.2    Zu, Y.3
  • 109
    • 77949507492 scopus 로고    scopus 로고
    • Optimization of the preparation process of vinblastine sulfate (VBLS)-loaded folateconjugated bovine serum albumin (BSA) nanoparticles for tumor-targeted drug delivery using response surface methodology (RSM)
    • Y.Zu, Y.Zhang, X.Zhao, et al. Optimization of the preparation process of vinblastine sulfate (VBLS)-loaded folateconjugated bovine serum albumin (BSA) nanoparticles for tumor-targeted drug delivery using response surface methodology (RSM). Int J Nanomedicine. 2009;4:321.
    • (2009) Int J Nanomedicine , vol.4 , pp. 321
    • Zu, Y.1    Zhang, Y.2    Zhao, X.3
  • 110
    • 80051824807 scopus 로고    scopus 로고
    • HI 6 human serum albumin nanoparticles—development and transport over an in vitro blood–brain barrier model
    • M.Dadparvar, S.Wagner, S.Wien, et al. HI 6 human serum albumin nanoparticles—development and transport over an in vitro blood–brain barrier model. Toxicol Lett. 2011;206(1):60–66.
    • (2011) Toxicol Lett , vol.206 , Issue.1 , pp. 60-66
    • Dadparvar, M.1    Wagner, S.2    Wien, S.3
  • 111
    • 45149130972 scopus 로고    scopus 로고
    • Aspirin loaded albumin nanoparticles by coacervation: implications in drug delivery
    • S.Das, R.Banerjee, J.Bellare. Aspirin loaded albumin nanoparticles by coacervation:implications in drug delivery. Trends Biomater Artif Organs. 2005;18(2):203–212.
    • (2005) Trends Biomater Artif Organs , vol.18 , Issue.2 , pp. 203-212
    • Das, S.1    Banerjee, R.2    Bellare, J.3
  • 112
    • 84864416863 scopus 로고    scopus 로고
    • Trastuzumab decorated methotrexate–human serum albumin conjugated nanoparticles for targeted delivery to HER2 positive tumor cells
    • A.Taheri, R.Dinarvand, F.Atyabi, et al. Trastuzumab decorated methotrexate–human serum albumin conjugated nanoparticles for targeted delivery to HER2 positive tumor cells. Eur J Pharm Sci. 2012;47(2):331–340.
    • (2012) Eur J Pharm Sci , vol.47 , Issue.2 , pp. 331-340
    • Taheri, A.1    Dinarvand, R.2    Atyabi, F.3
  • 113
    • 84907853742 scopus 로고    scopus 로고
    • Structural basis and anticancer properties of ruthenium-based drug complexed with human serum albumin
    • Y.Zhang, A.Ho, J.Yue, et al. Structural basis and anticancer properties of ruthenium-based drug complexed with human serum albumin. Eur J Med Chem. 2014;86:449–455.
    • (2014) Eur J Med Chem , vol.86 , pp. 449-455
    • Zhang, Y.1    Ho, A.2    Yue, J.3
  • 114
    • 84906785349 scopus 로고    scopus 로고
    • Preparation and sonodynamic activities of water-soluble tetra-α-(3-carboxyphenoxyl) zinc (II) phthalocyanine and its bovine serum albumin conjugate
    • H.-N.Xu, H.-J.Chen, B.-Y.Zheng, et al. Preparation and sonodynamic activities of water-soluble tetra-α-(3-carboxyphenoxyl) zinc (II) phthalocyanine and its bovine serum albumin conjugate. Ultrason Sonochem. 2015;22:125–131.
    • (2015) Ultrason Sonochem , vol.22 , pp. 125-131
    • Xu, H.-N.1    Chen, H.-J.2    Zheng, B.-Y.3
  • 115
    • 78650261890 scopus 로고    scopus 로고
    • Synthesis and characterization of thiolated alginate-albumin nanoparticles stabilized by disulfide bonds
    • A.Martínez, I.Iglesias, R.Lozano, et al. Synthesis and characterization of thiolated alginate-albumin nanoparticles stabilized by disulfide bonds. Eval Drug Delivery Syst Carbohydr Polym. 2011;83(3):1311–1321.
    • (2011) Eval Drug Delivery Syst Carbohydr Polym , vol.83 , Issue.3 , pp. 1311-1321
    • Martínez, A.1    Iglesias, I.2    Lozano, R.3
  • 117
    • 84930947243 scopus 로고    scopus 로고
    • A novel drug-polyethylene glycol liquid compound method to prepare 10-hydroxycamptothecin loaded human serum albumin nanoparticle
    • Z.Yang, W.Gong, Z.Wang, et al. A novel drug-polyethylene glycol liquid compound method to prepare 10-hydroxycamptothecin loaded human serum albumin nanoparticle. Int J Pharm. 2015;490(1–2):412–428.
    • (2015) Int J Pharm , vol.490 , Issue.1-2 , pp. 412-428
    • Yang, Z.1    Gong, W.2    Wang, Z.3
  • 118
    • 84922586767 scopus 로고    scopus 로고
    • Self-assembled serum albumin–poly (l-lactic acid) nanoparticles: a novel nanoparticle platform for drug delivery in cancer
    • L.Dai, C.-X.Li, K.-F.Liu, et al. Self-assembled serum albumin–poly (l-lactic acid) nanoparticles:a novel nanoparticle platform for drug delivery in cancer. RSC Adv. 2015;5(20):15612–15620.
    • (2015) RSC Adv , vol.5 , Issue.20 , pp. 15612-15620
    • Dai, L.1    Li, C.-X.2    Liu, K.-F.3
  • 119
    • 84961290908 scopus 로고    scopus 로고
    • Bionanotherapeutics: niclosamide encapsulated albumin nanoparticles as a novel drug delivery system for cancer therapy
    • B.Bhushan, P.Dubey, S.U.Kumar, et al. Bionanotherapeutics:niclosamide encapsulated albumin nanoparticles as a novel drug delivery system for cancer therapy. RSC Adv. 2015;5(16):12078–12086.
    • (2015) RSC Adv , vol.5 , Issue.16 , pp. 12078-12086
    • Bhushan, B.1    Dubey, P.2    Kumar, S.U.3
  • 120
    • 84899935673 scopus 로고    scopus 로고
    • Graphene quantum dots conjugated albumin nanoparticles for targeted drug delivery and imaging of pancreatic cancer
    • P.Nigam, S.Waghmode, M.Louis, et al. Graphene quantum dots conjugated albumin nanoparticles for targeted drug delivery and imaging of pancreatic cancer. J Mater Chem B. 2014;2(21):3190–3195.• Theranostic application of graphene quantum dot-labeled HSA NPs.
    • (2014) J Mater Chem B , vol.2 , Issue.21 , pp. 3190-3195
    • Nigam, P.1    Waghmode, S.2    Louis, M.3
  • 121
    • 84929620327 scopus 로고    scopus 로고
    • In vivo biocompatibility, clearance, and biodistribution of albumin vehicles for pulmonary drug delivery
    • A.Woods, A.Patel, D.Spina, et al. In vivo biocompatibility, clearance, and biodistribution of albumin vehicles for pulmonary drug delivery. J Controlled Release. 2015;210:1–9.
    • (2015) J Controlled Release , vol.210 , pp. 1-9
    • Woods, A.1    Patel, A.2    Spina, D.3
  • 122
    • 77955444543 scopus 로고    scopus 로고
    • Adsorption of obidoxime onto human serum albumin nanoparticles: drug loading, particle size and drug release
    • J.Kufleitner, S.Wagner, F.Worek, et al. Adsorption of obidoxime onto human serum albumin nanoparticles:drug loading, particle size and drug release. J Microencapsul. 2010;27(6):506–513.
    • (2010) J Microencapsul , vol.27 , Issue.6 , pp. 506-513
    • Kufleitner, J.1    Wagner, S.2    Worek, F.3
  • 123
    • 84886256332 scopus 로고    scopus 로고
    • Carbopol gel containing chitosan-egg albumin nanoparticles for transdermal aceclofenac delivery
    • S.Jana, S.Manna, A.K.Nayak, et al. Carbopol gel containing chitosan-egg albumin nanoparticles for transdermal aceclofenac delivery. Colloids Surf B. 2014;114:36–44.
    • (2014) Colloids Surf B , vol.114 , pp. 36-44
    • Jana, S.1    Manna, S.2    Nayak, A.K.3
  • 124
    • 80053212172 scopus 로고    scopus 로고
    • Nanotechnologies for Alzheimer’s disease: diagnosis, therapy, and safety issues
    • D.Brambilla, B.Le Droumaguet, J.Nicolas, et al. Nanotechnologies for Alzheimer’s disease:diagnosis, therapy, and safety issues. Nanomed Nanotechnol Biol Med. 2011;7(5):521–540.
    • (2011) Nanomed Nanotechnol Biol Med , vol.7 , Issue.5 , pp. 521-540
    • Brambilla, D.1    Le Droumaguet, B.2    Nicolas, J.3
  • 125
    • 84860333852 scopus 로고    scopus 로고
    • Drug delivery to the brain in Alzheimer’s disease: consideration of the blood–brain barrier
    • W.A.Banks. Drug delivery to the brain in Alzheimer’s disease:consideration of the blood–brain barrier. Adv Drug Deliv Rev. 2012;64(7):629–639.
    • (2012) Adv Drug Deliv Rev , vol.64 , Issue.7 , pp. 629-639
    • Banks, W.A.1
  • 126
  • 127
    • 84885156655 scopus 로고    scopus 로고
    • Mapping the interactions between the Alzheimer’s A β-peptide and human serum albumin beyond domain resolution
    • M.Algamal, J.Milojevic, N.Jafari, et al. Mapping the interactions between the Alzheimer’s A β-peptide and human serum albumin beyond domain resolution. Biophys J. 2013;105(7):1700–1709.
    • (2013) Biophys J , vol.105 , Issue.7 , pp. 1700-1709
    • Algamal, M.1    Milojevic, J.2    Jafari, N.3
  • 128
    • 84875077230 scopus 로고    scopus 로고
    • Current and emerging antiviral treatments for hepatitis C infection
    • J.S.Doyle, E.Aspinall, D.Liew, et al. Current and emerging antiviral treatments for hepatitis C infection. Br J Clin Pharmacol. 2013;75(4):931–943.
    • (2013) Br J Clin Pharmacol , vol.75 , Issue.4 , pp. 931-943
    • Doyle, J.S.1    Aspinall, E.2    Liew, D.3
  • 129
    • 34249980937 scopus 로고    scopus 로고
    • DOXO-EMCH (INNO-206): the first albumin-binding prodrug of doxorubicin to enter clinical trials
    • F.Kratz. DOXO-EMCH (INNO-206):the first albumin-binding prodrug of doxorubicin to enter clinical trials. Expert Opin Investig Drugs. 2007;16:855–866.
    • (2007) Expert Opin Investig Drugs , vol.16 , pp. 855-866
    • Kratz, F.1
  • 130
    • 0032822827 scopus 로고    scopus 로고
    • Enhanced hepatocyte uptake and liver targeting of methotrexate using galactosylated albumin as a carrier
    • J.H.Han, Y.K.Oh, D.S.Kim, et al. Enhanced hepatocyte uptake and liver targeting of methotrexate using galactosylated albumin as a carrier. Int J Pharm. 1999;188(1):39–47.
    • (1999) Int J Pharm , vol.188 , Issue.1 , pp. 39-47
    • Han, J.H.1    Oh, Y.K.2    Kim, D.S.3
  • 131
    • 84940789824 scopus 로고    scopus 로고
    • Gold nanocluster embedded albumin nanoparticles for two‐photon imaging of cancer cells accompanying drug delivery
    • R.Khandelia, S.Bhandari, U.N.Pan, et al. Gold nanocluster embedded albumin nanoparticles for two‐photon imaging of cancer cells accompanying drug delivery. Small. 2015;11(33):4075–4081.
    • (2015) Small , vol.11 , Issue.33 , pp. 4075-4081
    • Khandelia, R.1    Bhandari, S.2    Pan, U.N.3
  • 132
    • 84981729562 scopus 로고    scopus 로고
    • pH‐Sensitive stimulus‐responsive nanocarriers for targeted delivery of therapeutic agents
    • M.Karimi, M.Eslami, P.Sahandi‐Zangabad, et al. pH‐Sensitive stimulus‐responsive nanocarriers for targeted delivery of therapeutic agents. Wiley Interdiscip Rev. 2016. doi:10.1002/wnan.1389. [Epub ahead of print]
    • (2016) Wiley Interdiscip Rev
    • Karimi, M.1    Eslami, M.2    Sahandi‐Zangabad, P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.