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Volumn 6, Issue 7, 2012, Pages 5897-5908

PEGylated nanoparticles bind to and alter amyloid-beta peptide conformation: Toward engineering of functional nanomedicines for alzheimer's disease

Author keywords

A 1 42; Alzheimer's disease; binding; nanoparticles; polyethylene glycol

Indexed keywords

ALZHEIMER'S DISEASE; AMYLOID BETAS; BINDING; CONFORMATIONAL CHANGE; CYANOACRYLATES; IN-SILICO; NANOMEDICINES; NANOPARTICLE SURFACE; PEGYLATED NANOPARTICLE; PEGYLATION; PEPTIDE AGGREGATION; PEPTIDE BINDING; PEPTIDE CONFORMATION; POLY LACTIC ACID; POLYMERIC NANOPARTICLES; SYSTEMIC CIRCULATION; THIOFLAVIN T;

EID: 84864273268     PISSN: 19360851     EISSN: 1936086X     Source Type: Journal    
DOI: 10.1021/nn300489k     Document Type: Article
Times cited : (172)

References (56)
  • 2
    • 10644276189 scopus 로고    scopus 로고
    • Mitochondria as a primary target for vascular hypoperfusion and oxidative stress in Alzheimer's disease
    • DOI 10.1016/j.mito.2004.07.018, PII S1567724904001539
    • Aliev, G.; Smith, M. A.; de la Torre, J. C.; Perry, G. Mitochondria as a Primary Target for Vascular Hypoperfusion and Oxidative Stress in Alzheimer's Disease Mitochondrion 2004, 4, 649-663 (Pubitemid 39650918)
    • (2004) Mitochondrion , vol.4 , Issue.SPEC. ISS. , pp. 649-663
    • Aliev, G.1    Smith, M.A.2    De La Torre, J.C.3    Perry, G.4
  • 3
    • 67649366042 scopus 로고    scopus 로고
    • Neuroprotective Secreted Amyloid Precursor Protein Acts by Disrupting Amyloid Precursor Protein Dimers
    • Gralle, M.; Botelho, M. G.; Wouters, F. S. Neuroprotective Secreted Amyloid Precursor Protein Acts by Disrupting Amyloid Precursor Protein Dimers J. Biol. Chem. 2009, 284, 15016-15025
    • (2009) J. Biol. Chem. , vol.284 , pp. 15016-15025
    • Gralle, M.1    Botelho, M.G.2    Wouters, F.S.3
  • 4
    • 36348935683 scopus 로고    scopus 로고
    • Soluble Aβ inhibits specific signal transduction cascades common to the insulin receptor pathway
    • DOI 10.1074/jbc.M610390200
    • Townsend, M.; Mehta, T.; Selkoe, D. J. Soluble Aβ Inhibits Specific Signal Transduction Cascades Common to the Insulin Receptor Pathway J. Biol. Chem. 2007, 282, 33305-33312 (Pubitemid 350159548)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.46 , pp. 33305-33312
    • Townsend, M.1    Mehta, T.2    Selkoe, D.J.3
  • 6
    • 42149164312 scopus 로고    scopus 로고
    • Processing of Amyloid Precursor Protein and Amyloid Peptide Neurotoxicity
    • Pierrot, N.; Octave, J. Processing of Amyloid Precursor Protein and Amyloid Peptide Neurotoxicity Curr. Alzheimer Res. 2008, 5, 92-99
    • (2008) Curr. Alzheimer Res. , vol.5 , pp. 92-99
    • Pierrot, N.1    Octave, J.2
  • 7
    • 79954520806 scopus 로고    scopus 로고
    • Peripheral Reduction of Beta-Amyloid Is Sufficient to Reduce Brain Beta-Amyloid: Implications for Alzheimer's Disease
    • Sutcliffe, J. G.; Hedlund, P. B.; Thomas, E. A.; Bloom, F. E.; Hilbush, B. S. Peripheral Reduction of Beta-Amyloid Is Sufficient To Reduce Brain Beta-Amyloid: Implications for Alzheimer's Disease J. Neurosci. Res. 2011, 89, 808-814
    • (2011) J. Neurosci. Res. , vol.89 , pp. 808-814
    • Sutcliffe, J.G.1    Hedlund, P.B.2    Thomas, E.A.3    Bloom, F.E.4    Hilbush, B.S.5
  • 10
    • 2542475986 scopus 로고    scopus 로고
    • Clearing amyloid through the blood-brain barrier
    • DOI 10.1111/j.1471-4159.2004.02385.x
    • Zlokovic, B. V. Clearing Amyloid through the Blood-Brain Barrier J. Neurochem. 2004, 89, 807-811 (Pubitemid 38684728)
    • (2004) Journal of Neurochemistry , vol.89 , Issue.4 , pp. 807-811
    • Zlokovic, B.V.1
  • 11
    • 0036438914 scopus 로고    scopus 로고
    • Solution Structure of the Alzheimer Amyloid Beta-Peptide (1-42) in an Apolar Microenvironment. Similarity with a Virus Fusion Domain
    • Crescenzi, O.; Tomaselli, S.; Guerrini, R.; Salvadori, S.; D'Ursi, A. M.; Temussi, P. A.; Picone, D. Solution Structure of the Alzheimer Amyloid Beta-Peptide (1-42) in an Apolar Microenvironment. Similarity with a Virus Fusion Domain Eur. J. Biochem. 2002, 269, 5642-6548
    • (2002) Eur. J. Biochem. , vol.269 , pp. 5642-6548
    • Crescenzi, O.1    Tomaselli, S.2    Guerrini, R.3    Salvadori, S.4    D'Ursi, A.M.5    Temussi, P.A.6    Picone, D.7
  • 12
    • 77149162414 scopus 로고    scopus 로고
    • From Alpha to Omega with Aβ: Targeting the Multiple Molecular Appearances of the Pathogenic Peptide in Alzheimer's Disease
    • De Kimpe, L.; Scheper, W. From Alpha to Omega with Aβ: Targeting the Multiple Molecular Appearances of the Pathogenic Peptide in Alzheimer's Disease Curr. Med. Chem. 2010, 17, 198-212
    • (2010) Curr. Med. Chem. , vol.17 , pp. 198-212
    • De Kimpe, L.1    Scheper, W.2
  • 13
    • 77749336627 scopus 로고    scopus 로고
    • Amyloid-Beta Aggregates Cause Alterations of Astrocytic Metabolic Phenotype: Impact on Neuronal Viability
    • Allaman, I.; Gavillet, M.; Belanger, M.; Laroche, T.; Viertl, D.; Lashuel, H. A.; Magistretti, P. J. Amyloid-Beta Aggregates Cause Alterations of Astrocytic Metabolic Phenotype: Impact on Neuronal Viability J. Neurosci. 2010, 30, 3326-3338
    • (2010) J. Neurosci. , vol.30 , pp. 3326-3338
    • Allaman, I.1    Gavillet, M.2    Belanger, M.3    Laroche, T.4    Viertl, D.5    Lashuel, H.A.6    Magistretti, P.J.7
  • 16
    • 79952810857 scopus 로고    scopus 로고
    • Amyloid-Beta Protein Oligomer at Low Nanomolar Concentrations Activates Microglia and Induces Microglial Neurotoxicity
    • Maezawa, I.; Zimin, P. I.; Wulff, H.; Jin, L. W. Amyloid-Beta Protein Oligomer at Low Nanomolar Concentrations Activates Microglia and Induces Microglial Neurotoxicity J. Biol. Chem. 2011, 286, 3693-3706
    • (2011) J. Biol. Chem. , vol.286 , pp. 3693-3706
    • Maezawa, I.1    Zimin, P.I.2    Wulff, H.3    Jin, L.W.4
  • 18
    • 84858112545 scopus 로고    scopus 로고
    • Therapeutic Albumin Binding to Remove Amyloid-Beta
    • Costa, M.; Ortiz, A. M.; Jorquera, J. I. Therapeutic Albumin Binding to Remove Amyloid-Beta J. Alzheimers Dis. 2012, 29, 159-170
    • (2012) J. Alzheimers Dis. , vol.29 , pp. 159-170
    • Costa, M.1    Ortiz, A.M.2    Jorquera, J.I.3
  • 19
    • 79958204688 scopus 로고    scopus 로고
    • Inhibition of Aggregation of Amyloid Peptides by Beta-Sheet Breaker Peptides and Their Binding Affinity
    • Viet, M. H.; Ngo, S. T.; Lam, N. S.; Li, M. S. Inhibition of Aggregation of Amyloid Peptides by Beta-Sheet Breaker Peptides and Their Binding Affinity J. Phys. Chem. B 2011, 115, 7433-7446
    • (2011) J. Phys. Chem. B , vol.115 , pp. 7433-7446
    • Viet, M.H.1    Ngo, S.T.2    Lam, N.S.3    Li, M.S.4
  • 20
    • 0018387102 scopus 로고
    • Polycyanoacrylate nanocapsules as potential lysosomotropic carriers: Preparation, morphological and sorptive properties
    • Couvreur, P.; Kante, B.; Roland, M.; Guiot, P.; Bauduin, P.; Speiser, P. Polycyanoacrylate Nanocapsules as Potential Lysosomotropic Carriers: Preparation, Morphological and Sorptive Properties J. Pharm. Pharmacol. 1979, 31, 331-332 (Pubitemid 9207599)
    • (1979) Journal of Pharmacy and Pharmacology , vol.31 , Issue.5 , pp. 331-332
    • Couvreur, P.1    Kante, B.2    Roland, M.3
  • 21
    • 0037466349 scopus 로고    scopus 로고
    • Poly(alkylcyanoacrylates) as biodegradable materials for biomedical applications
    • DOI 10.1016/S0169-409X(03)00041-3
    • Vauthier, C.; Dubernet, C.; Fattal, E.; Pinto-Alphandary, H.; Couvreur, P. Poly(alkylcyanoacrylates) as Biodegradable Materials for Biomedical Applications Adv. Drug Delivery Rev. 2003, 55, 519-548 (Pubitemid 36423302)
    • (2003) Advanced Drug Delivery Reviews , vol.55 , Issue.4 , pp. 519-548
    • Vauthier, C.1    Dubernet, C.2    Fattal, E.3    Pinto-Alphandary, H.4    Couvreur, P.5
  • 22
    • 81355149640 scopus 로고    scopus 로고
    • Nanotechnology for Therapy and Imaging of Liver Diseases
    • Reddy, L. H.; Couvreur, P. Nanotechnology for Therapy and Imaging of Liver Diseases J. Hepatol. 2011, 55, 1461-1466
    • (2011) J. Hepatol. , vol.55 , pp. 1461-1466
    • Reddy, L.H.1    Couvreur, P.2
  • 23
    • 77957971079 scopus 로고    scopus 로고
    • Nanotechnology. Nanoparticle Trojan Horses Gallop from the Lab into the Clinic
    • Service, R. F. Nanotechnology. Nanoparticle Trojan Horses Gallop from the Lab into the Clinic Science 2010, 330, 314-315
    • (2010) Science , vol.330 , pp. 314-315
    • Service, R.F.1
  • 24
    • 33947630376 scopus 로고    scopus 로고
    • Translocation of poly(ethylene glycol-co-hexadecyl)cyanoacrylate nanoparticles into rat brain endothelial cells: Role of apolipoproteins on receptor-medicted endocytosis
    • DOI 10.1021/bm060711a
    • Kim, H. R.; Andrieux, K.; Gil, S.; Taverna, M.; Chacun, H.; Desmaele, D.; Taran, F.; Georgin, D.; Couvreur, P. Translocation of Poly(ethylene glycol- co -hexadecyl)cyanoacrylate Nanoparticles into Rat Brain Endothelial Cells: Role of Apolipoproteins in Receptor-Mediated Endocytosis Biomacromolecules 2007, 8, 793-799 (Pubitemid 46488459)
    • (2007) Biomacromolecules , vol.8 , Issue.3 , pp. 793-799
    • Kim, H.R.1    Andrieux, K.2    Gil, S.3    Taverna, M.4    Chacun, H.5    Desmaele, D.6    Taran, F.7    Georgin, D.8    Couvreur, P.9
  • 25
    • 0033168385 scopus 로고    scopus 로고
    • Visualization of in vitro protein-rejecting properties of PEGylated stealth® polycyanoacrylate nanoparticles
    • DOI 10.1016/S0142-9612(99)00021-6, PII S0142961299000216
    • Peracchia, M. T.; Harnisch, S.; Pinto-Alphandary, H.; Gulik, A.; Dedieu, J. C.; Desmaele, D.; d'Angelo, J.; Muller, R. H.; Couvreur, P. Visualization of In Vitro Protein-Rejecting Properties of PEGylated Stealth Polycyanoacrylate Nanoparticles Biomaterials 1999, 20, 1269-1275 (Pubitemid 29281378)
    • (1999) Biomaterials , vol.20 , Issue.14 , pp. 1269-1275
    • Peracchia, M.T.1    Harnisch, S.2    Pinto-Alphandary, H.3    Gulik, A.4    Dedieu, J.C.5    Desmaele, D.6    D'Angelo, J.7    Muller, R.H.8    Couvreur, P.9
  • 26
    • 77950351203 scopus 로고    scopus 로고
    • Design of Fluorescently Tagged Poly(alkyl cyanoacrylate) Nanoparticles for Human Brain Endothelial Cell Imaging
    • Brambilla, D.; Nicolas, J.; Le Droumaguet, B.; Andrieux, K.; Marsaud, V.; Couraud, P. O.; Couvreur, P. Design of Fluorescently Tagged Poly(alkyl cyanoacrylate) Nanoparticles for Human Brain Endothelial Cell Imaging Chem. Commun. 2010, 46, 2602-2604
    • (2010) Chem. Commun. , vol.46 , pp. 2602-2604
    • Brambilla, D.1    Nicolas, J.2    Le Droumaguet, B.3    Andrieux, K.4    Marsaud, V.5    Couraud, P.O.6    Couvreur, P.7
  • 27
    • 78650336764 scopus 로고    scopus 로고
    • New Method Based on Capillary Electrophoresis with Laser-Induced Fluorescence Detection (CE-LIF) to Monitor Interaction between Nanoparticles and the Amyloid-Beta Peptide
    • Brambilla, D.; Verpillot, R.; Taverna, M.; De Kimpe, L.; Le Droumaguet, B.; Nicolas, J.; Canovi, M.; Gobbi, M.; Mantegazza, F.; Salmona, M. et al. New Method Based on Capillary Electrophoresis with Laser-Induced Fluorescence Detection (CE-LIF) To Monitor Interaction between Nanoparticles and the Amyloid-Beta Peptide Anal. Chem. 2010, 82, 10083-10089
    • (2010) Anal. Chem. , vol.82 , pp. 10083-10089
    • Brambilla, D.1    Verpillot, R.2    Taverna, M.3    De Kimpe, L.4    Le Droumaguet, B.5    Nicolas, J.6    Canovi, M.7    Gobbi, M.8    Mantegazza, F.9    Salmona, M.10
  • 31
    • 0343191443 scopus 로고    scopus 로고
    • 'Stealth' corona-core nanoparticles surface modified by polyethylene glycol (PEG): Influences of the corona (PEG chain length and surface density) and of the core composition on phagocytic uptake and plasma protein adsorption
    • DOI 10.1016/S0927-7765(99)00156-3, PII S0927776599001563
    • Gref, R.; Luck, M.; Quellec, P.; Marchand, M.; Dellacherie, E.; Harnisch, S.; Blunk, T.; Muller, R. H. 'Stealth' Corona-Core Nanoparticles Surface Modified by Polyethylene Glycol (PEG): Influences of the Corona (PEG Chain Length and Surface Density) and of the Core Composition on Phagocytic Uptake and Plasma Protein Adsorption Colloids Surf., B 2000, 18, 301-313 (Pubitemid 30479870)
    • (2000) Colloids and Surfaces B: Biointerfaces , vol.18 , Issue.3-4 , pp. 301-313
    • Gref, R.1    Luck, M.2    Quellec, P.3    Marchand, M.4    Dellacherie, E.5    Harnisch, S.6    Blunk, T.7    Muller, R.H.8
  • 33
    • 75749092650 scopus 로고    scopus 로고
    • Facile Disassembly of Amyloid Fibrils Using Gemini Surfactant Micelles
    • Han, Y.; He, C.; Cao, M.; Huang, X.; Wang, Y.; Li, Z. Facile Disassembly of Amyloid Fibrils Using Gemini Surfactant Micelles Langmuir 2010, 26, 1583-1587
    • (2010) Langmuir , vol.26 , pp. 1583-1587
    • Han, Y.1    He, C.2    Cao, M.3    Huang, X.4    Wang, Y.5    Li, Z.6
  • 34
    • 34447333696 scopus 로고    scopus 로고
    • Analytical method for β-amyloid fibrils using CE-laser induced fluorescence and its application to screening for inhibitors of β-amyloid protein aggregation
    • DOI 10.1021/ac0701482
    • Kato, M.; Kinoshita, H.; Enokita, M.; Hori, Y.; Hashimoto, T.; Iwatsubo, T.; Toyo'oka, T. Analytical Method for Beta-Amyloid Fibrils Using CE-Laser Induced Fluorescence and Its Application to Screening for Inhibitors of Beta-Amyloid Protein Aggregation Anal. Chem. 2007, 79, 4887-4891 (Pubitemid 47051441)
    • (2007) Analytical Chemistry , vol.79 , Issue.13 , pp. 4887-4891
    • Kato, M.1    Kinoshita, H.2    Enokita, M.3    Hori, Y.4    Hashimoto, T.5    Iwatsubo, T.6    Toyo'Oka, T.7
  • 36
    • 79952453932 scopus 로고    scopus 로고
    • A Modified Protocol to Prepare Seed-Free Starting Solutions of Amyloid-Beta (Aβ) and Aβ from the Corresponding Depsipeptides
    • Beeg, M.; Stravalaci, M.; Bastone, A.; Salmona, M.; Gobbi, M. A Modified Protocol To Prepare Seed-Free Starting Solutions of Amyloid-Beta (Aβ) and Aβ from the Corresponding Depsipeptides Anal. Biochem. 2011, 411, 297-299
    • (2011) Anal. Biochem. , vol.411 , pp. 297-299
    • Beeg, M.1    Stravalaci, M.2    Bastone, A.3    Salmona, M.4    Gobbi, M.5
  • 37
    • 78650626543 scopus 로고    scopus 로고
    • Use of Surface Plasmon Resonance to Study the Elongation Kinetics and the Binding Properties of the Highly Amyloidogenic Aβ1-42 Peptide, Synthesized by Depsi-Peptide Technique
    • Stravalaci, M.; Beeg, M.; Salmona, M.; Gobbi, M. Use of Surface Plasmon Resonance To Study the Elongation Kinetics and the Binding Properties of the Highly Amyloidogenic Aβ1-42 Peptide, Synthesized by Depsi-Peptide Technique Biosens. Bioelectron. 2011, 26, 2772-2775
    • (2011) Biosens. Bioelectron. , vol.26 , pp. 2772-2775
    • Stravalaci, M.1    Beeg, M.2    Salmona, M.3    Gobbi, M.4
  • 40
    • 84864184647 scopus 로고    scopus 로고
    • version 5.5; Schrodinger, LLC: New York
    • Glide, version 5.5; Schrodinger, LLC: New York, 2009.
    • (2009) Glide
  • 41
    • 0029912748 scopus 로고    scopus 로고
    • Development and testing of the OPLS all-atom force field on conformational energetics and properties of organic liquids
    • DOI 10.1021/ja9621760, PII S0002786396021762
    • Jorgensen, W. L.; Maxwell, D. S.; Tirado-Rives, J. Development and Testing of the Opls All-Atom Force Field on Conformational Energetics and Properties of Organic Liquids J. Am. Chem. Soc. 1996, 118, 11225-11236 (Pubitemid 26399746)
    • (1996) Journal of the American Chemical Society , vol.118 , Issue.45 , pp. 11225-11236
    • Jorgensen, W.L.1    Maxwell, D.S.2    Tirado-Rives, J.3
  • 42
    • 0035913529 scopus 로고    scopus 로고
    • Evaluation and reparametrization of the OPLS-AA force field for proteins via comparison with accurate quantum chemical calculations on peptides
    • DOI 10.1021/jp003919d
    • Kaminski, G. A.; Friesner, R. A.; Tirado-Rives, J.; Jorgensen, W. L. Evaluation and Reparametrization of the Opls-Aa Force Field for Proteins via Comparison with Accurate Quantum Chemical Calculations on Peptides J. Phys. Chem. B 2001, 105, 6474-6487 (Pubitemid 35339015)
    • (2001) Journal of Physical Chemistry B , vol.105 , Issue.28 , pp. 6474-6487
    • Kaminski, G.A.1    Friesner, R.A.2    Tirado-Rives, J.3    Jorgensen, W.L.4
  • 43
    • 84864241609 scopus 로고    scopus 로고
    • version 9.0; Schrodinger, LLC: New York
    • MAESTRO, version 9.0; Schrodinger, LLC: New York, 2009.
    • (2009) MAESTRO
  • 50
    • 33646940952 scopus 로고
    • Numerical Integration of the Cartesian Equations of Motion of a System with Constraints; Molecular Dynamics of n -Alkanes
    • Ryckaert, J. P.; Ciccotti, G.; Berendsen, H. J. C. Numerical Integration of the Cartesian Equations of Motion of a System with Constraints; Molecular Dynamics of n -Alkanes J. Comput. Phys. 1977, 23, 327-341
    • (1977) J. Comput. Phys. , vol.23 , pp. 327-341
    • Ryckaert, J.P.1    Ciccotti, G.2    Berendsen, H.J.C.3
  • 52
    • 0020997912 scopus 로고
    • Dictionary of Protein Secondary Structure: Pattern Recognition of Hydrogen-Bonded and Geometrical Features
    • Kabsch, W.; Sander, C. Dictionary of Protein Secondary Structure: Pattern Recognition of Hydrogen-Bonded and Geometrical Features Biopolymers 1983, 22, 2577-2637
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 53
    • 54849408545 scopus 로고    scopus 로고
    • Poly(ethylene glycol)S Generate Complement Activation Products in Human Serum through Increased Alternative Pathway Turnover and a Masp-2-Dependent Process
    • Hamad, I.; Hunter, A. C.; Szebeni, J.; Moghimi, S. M. Poly(ethylene glycol)S Generate Complement Activation Products in Human Serum through Increased Alternative Pathway Turnover and a Masp-2-Dependent Process Mol. Immunol. 2008, 46, 225-232
    • (2008) Mol. Immunol. , vol.46 , pp. 225-232
    • Hamad, I.1    Hunter, A.C.2    Szebeni, J.3    Moghimi, S.M.4
  • 54
    • 78649538085 scopus 로고    scopus 로고
    • Distinct Polymer Architecture Mediates Switching of Complement Activation Pathways at the Nanosphere-Serum Interface: Implications for Stealth Nanoparticle Engineering
    • Moghimi, S. M.; Hamad, I.; Al-Hanbali, O.; Hunter, A. C.; Rutt, K. J.; Andresen, T. L. Distinct Polymer Architecture Mediates Switching of Complement Activation Pathways at the Nanosphere-Serum Interface: Implications for Stealth Nanoparticle Engineering ACS Nano 2010, 4, 6629-6638
    • (2010) ACS Nano , vol.4 , pp. 6629-6638
    • Moghimi, S.M.1    Hamad, I.2    Al-Hanbali, O.3    Hunter, A.C.4    Rutt, K.J.5    Andresen, T.L.6
  • 55
    • 33845639957 scopus 로고    scopus 로고
    • Methylation of the Phosphate Oxygen Moiety of Phospholipid- Methoxy(polyethylene glycol) Conjugate Prevents PEGylated Liposome-Mediated Complement Activation and Anaphylatoxin Production
    • Moghimi, S. M.; Hamad, I.; Andresen, T. L.; Jorgensen, K.; Szebeni, J. Methylation of the Phosphate Oxygen Moiety of Phospholipid-Methoxy(polyethylene glycol) Conjugate Prevents PEGylated Liposome-Mediated Complement Activation and Anaphylatoxin Production FASEB J. 2006, 20, 2591-2593
    • (2006) FASEB J. , vol.20 , pp. 2591-2593
    • Moghimi, S.M.1    Hamad, I.2    Andresen, T.L.3    Jorgensen, K.4    Szebeni, J.5
  • 56
    • 0031281885 scopus 로고    scopus 로고
    • Kinetics of Blood Component Adsorption on Poly(d, l -lactic acid) Nanoparticles: Evidence of Complement C3 Component Involvement
    • Allemann, E.; Gravel, P.; Leroux, J. C.; Balant, L.; Gurny, R. Kinetics of Blood Component Adsorption on Poly(d, l -lactic acid) Nanoparticles: Evidence of Complement C3 Component Involvement J. Biomed. Mater. Res. 1997, 37, 229-334
    • (1997) J. Biomed. Mater. Res. , vol.37 , pp. 229-334
    • Allemann, E.1    Gravel, P.2    Leroux, J.C.3    Balant, L.4    Gurny, R.5


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