메뉴 건너뛰기




Volumn 118, Issue 37, 2014, Pages 21630-21638

Inhibition of amyloid fibril growth by nanoparticle coated with histidine-based polymer

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; FUNCTIONAL GROUPS; GLYCOPROTEINS; NANOPARTICLES; PLASTIC COATINGS; SURFACE CHEMISTRY;

EID: 84920279852     PISSN: 19327447     EISSN: 19327455     Source Type: Journal    
DOI: 10.1021/jp505613g     Document Type: Article
Times cited : (71)

References (46)
  • 1
    • 0033600274 scopus 로고    scopus 로고
    • Translating Cell Biology into Therapeutic Advances in Alzheimers Disease
    • Selkoe, D. J. Translating Cell Biology into Therapeutic Advances in Alzheimers Disease Nature 1999, 399, A23-A31
    • (1999) Nature , vol.399 , pp. 23-A31
    • Selkoe, D.J.1
  • 2
    • 0347987853 scopus 로고    scopus 로고
    • Folding Proteins in Fatal Ways
    • Selkoe, D. J. Folding Proteins in Fatal Ways Nature 2003, 426, 900-904
    • (2003) Nature , vol.426 , pp. 900-904
    • Selkoe, D.J.1
  • 3
    • 0242289453 scopus 로고    scopus 로고
    • Recent Advances in Understanding the Pathogenesis of Polyglutamine Diseases: Involvement of Molecular Chaperones and Ubiquitin-Proteasome Pathway
    • Jana, N. R.; Nukina, N. Recent Advances in Understanding the Pathogenesis of Polyglutamine Diseases: Involvement of Molecular Chaperones and Ubiquitin-Proteasome Pathway J. Chem. Neuroanat. 2003, 26, 95-101
    • (2003) J. Chem. Neuroanat. , vol.26 , pp. 95-101
    • Jana, N.R.1    Nukina, N.2
  • 4
    • 33749841522 scopus 로고    scopus 로고
    • The Aggregation and Fibrillation of α-Synuclein
    • Fink, A. L. The Aggregation and Fibrillation of α-Synuclein Acc. Chem. Res. 2006, 39, 628-634
    • (2006) Acc. Chem. Res. , vol.39 , pp. 628-634
    • Fink, A.L.1
  • 5
    • 33749836310 scopus 로고    scopus 로고
    • Direct Observation of Amyloid Fibril Growth, Propagation, and Adaptation
    • Ban, T.; Yamaguchi, K.; Goto, Y. Direct Observation of Amyloid Fibril Growth, Propagation, and Adaptation Acc. Chem. Res. 2006, 39, 663-670
    • (2006) Acc. Chem. Res. , vol.39 , pp. 663-670
    • Ban, T.1    Yamaguchi, K.2    Goto, Y.3
  • 7
    • 33750510024 scopus 로고    scopus 로고
    • Alzheimer 100-Highlights in the History of Alzheimer Research
    • Jellinger, K. A. Alzheimer 100-Highlights in the History of Alzheimer Research J. Neural Transm. 2006, 113, 1603-1623
    • (2006) J. Neural Transm. , vol.113 , pp. 1603-1623
    • Jellinger, K.A.1
  • 8
    • 65649133114 scopus 로고    scopus 로고
    • Amyloid Fibrils: Abnormal Protein Assembly
    • Rambaran, R. N.; Serpell, L. C. Amyloid Fibrils: Abnormal Protein Assembly Prion 2008, 2, 112-117
    • (2008) Prion , vol.2 , pp. 112-117
    • Rambaran, R.N.1    Serpell, L.C.2
  • 9
    • 1542364225 scopus 로고    scopus 로고
    • Curcumin has Potent Anti-amyloidogenic Effects for Alzheimers β-Amyloid Fibrils in Vitro
    • Ono, K.; Hasegawa, K.; Naiki, H.; Yamada, M. Curcumin has Potent Anti-amyloidogenic Effects for Alzheimers β-Amyloid Fibrils in Vitro J. Neurosci. Res. 2004, 75, 742-750
    • (2004) J. Neurosci. Res. , vol.75 , pp. 742-750
    • Ono, K.1    Hasegawa, K.2    Naiki, H.3    Yamada, M.4
  • 11
    • 34547451145 scopus 로고    scopus 로고
    • Curcumin Labels Amyloid Pathology in Vivo, Disrupts Existing Plaques, and Partially Restores Distorted Neurites in an Alzheimer Mouse Model
    • Garcia-Alloza, M.; Borrelli, L. A.; Rozkalne, A.; Hyman, B. T.; Bacskai, B. J. Curcumin Labels Amyloid Pathology in Vivo, Disrupts Existing Plaques, and Partially Restores Distorted Neurites in an Alzheimer Mouse Model J. Neurochem. 2007, 102, 1095-1104
    • (2007) J. Neurochem. , vol.102 , pp. 1095-1104
    • Garcia-Alloza, M.1    Borrelli, L.A.2    Rozkalne, A.3    Hyman, B.T.4    Bacskai, B.J.5
  • 12
    • 48849104834 scopus 로고    scopus 로고
    • Molecules that Target β-Amyloid
    • Stains, C. I.; Mondal, K.; Ghosh, I. Molecules that Target β-Amyloid ChemMedChem. 2007, 2, 1674-1692
    • (2007) ChemMedChem. , vol.2 , pp. 1674-1692
    • Stains, C.I.1    Mondal, K.2    Ghosh, I.3
  • 13
    • 39649124929 scopus 로고    scopus 로고
    • Designing Peptide Inhibitors for Oligomerization and Toxicity of Alzheimers β-Amyloid Peptide
    • Austen, B. M.; Paleologou, K. E.; Ali, S. A. E.; Qureshi, M. M.; Allsop, D.; El-Agnaf, O. M. A. Designing Peptide Inhibitors for Oligomerization and Toxicity of Alzheimers β-Amyloid Peptide Biochemistry 2008, 47, 1984-1992
    • (2008) Biochemistry , vol.47 , pp. 1984-1992
    • Austen, B.M.1    Paleologou, K.E.2    Ali, S.A.E.3    Qureshi, M.M.4    Allsop, D.5    El-Agnaf, O.M.A.6
  • 14
    • 61849111130 scopus 로고    scopus 로고
    • Cognitive-Performance Recovery of Alzheimers Disease Model Mice by Modulation of Early Soluble Amyloidal Assemblies
    • Frydman-Marom, A.; Rechter, M.; Shefler, I.; Bram, Y.; Shalev, D. E.; Gazit, E. Cognitive-Performance Recovery of Alzheimers Disease Model Mice by Modulation of Early Soluble Amyloidal Assemblies Angew. Chem., Int. Ed. 2009, 48, 1981-1986
    • (2009) Angew. Chem., Int. Ed. , vol.48 , pp. 1981-1986
    • Frydman-Marom, A.1    Rechter, M.2    Shefler, I.3    Bram, Y.4    Shalev, D.E.5    Gazit, E.6
  • 15
    • 38949216069 scopus 로고    scopus 로고
    • Effect of Trehalose on W7FW14F Apomyoglobin and Insulin Fibrillization: New Insight into Inhibition Activity
    • Vilasi, S.; Iannuzzi, C.; Portaccio, M.; Irace, G.; Sirangelo, I. Effect of Trehalose on W7FW14F Apomyoglobin and Insulin Fibrillization: New Insight into Inhibition Activity Biochemistry 2008, 47, 1789-1796
    • (2008) Biochemistry , vol.47 , pp. 1789-1796
    • Vilasi, S.1    Iannuzzi, C.2    Portaccio, M.3    Irace, G.4    Sirangelo, I.5
  • 16
    • 84861899099 scopus 로고    scopus 로고
    • Trehalose Inhibits Fibrillation of A53T Mutant α-Synuclein and Disaggregates Existing Fibrils
    • Yu, W.-B.; Jiang, T.; Lan, D.-M.; Lu, J.-H.; Yue, Z.-Y.; Wang, J.; Zhou, P. Trehalose Inhibits Fibrillation of A53T Mutant α-Synuclein and Disaggregates Existing Fibrils Arch. Biochem. Biophys. 2012, 523, 144-150
    • (2012) Arch. Biochem. Biophys. , vol.523 , pp. 144-150
    • Yu, W.-B.1    Jiang, T.2    Lan, D.-M.3    Lu, J.-H.4    Yue, Z.-Y.5    Wang, J.6    Zhou, P.7
  • 17
    • 38349130550 scopus 로고    scopus 로고
    • Synthesis of Monofunctional Curcumin Derivatives, Clicked Curcumin Dimer, and a PAMAM Dendrimer Curcumin Conjugate for Therapeutic Applications
    • Shi, W.; Dolai, S.; Rizk, S.; Hussain, A.; Tariq, H.; Averick, S.; LAmoreaux, W.; Idrissi, A. E.; Banerjee, P.; Raja, K. Synthesis of Monofunctional Curcumin Derivatives, Clicked Curcumin Dimer, and a PAMAM Dendrimer Curcumin Conjugate for Therapeutic Applications Org. Lett. 2007, 9, 5461-5464
    • (2007) Org. Lett. , vol.9 , pp. 5461-5464
    • Shi, W.1    Dolai, S.2    Rizk, S.3    Hussain, A.4    Tariq, H.5    Averick, S.6    Lamoreaux, W.7    Idrissi, A.E.8    Banerjee, P.9    Raja, K.10
  • 18
    • 48449085158 scopus 로고    scopus 로고
    • Inhibition of Alzheimer Amyloid-β Aggregation by Polyvalent Trehalose
    • Miura, Y.; You, C.; Ohnishi, R. Inhibition of Alzheimer Amyloid-β Aggregation by Polyvalent Trehalose Sci. Technol. Adv. Mater. 2008, 9, 024407-024413
    • (2008) Sci. Technol. Adv. Mater. , vol.9 , pp. 024407-024413
    • Miura, Y.1    You, C.2    Ohnishi, R.3
  • 19
    • 79960300049 scopus 로고    scopus 로고
    • A Specific Inhibitory Effect of Multivalent Trehalose toward Aβ (1-40) Aggregation
    • Wada, M.; Miyazawa, Y.; Miura, Y. A Specific Inhibitory Effect of Multivalent Trehalose toward Aβ (1-40) Aggregation Polym. Chem. 2011, 2, 1822-1830
    • (2011) Polym. Chem. , vol.2 , pp. 1822-1830
    • Wada, M.1    Miyazawa, Y.2    Miura, Y.3
  • 21
    • 70350348150 scopus 로고    scopus 로고
    • Inhibition of Beta (1-40) Amyloid Fibrillation with N -acetyl- l -cysteine Capped Quantum Dots
    • Xiao, L.; Zhao, D.; Chan, W.-H.; Choi, M. M. F.; Li, H.-W. Inhibition of Beta (1-40) Amyloid Fibrillation with N -acetyl- l -cysteine Capped Quantum Dots Biomaterials 2010, 31, 91-98
    • (2010) Biomaterials , vol.31 , pp. 91-98
    • Xiao, L.1    Zhao, D.2    Chan, W.-H.3    Choi, M.M.F.4    Li, H.-W.5
  • 22
    • 77951681963 scopus 로고    scopus 로고
    • Dual Effect of Amino Modified Polystyrene Nanoparticles on Amyloid-β Protein Fibrillation
    • Cabaleiro-Lago, C.; Quinlan-Pluck, F.; Lynch, I.; Dawson, K. A.; Linse, S. Dual Effect of Amino Modified Polystyrene Nanoparticles on Amyloid-β Protein Fibrillation ACS Chem. Neurosci. 2010, 1, 279-287
    • (2010) ACS Chem. Neurosci. , vol.1 , pp. 279-287
    • Cabaleiro-Lago, C.1    Quinlan-Pluck, F.2    Lynch, I.3    Dawson, K.A.4    Linse, S.5
  • 23
    • 80051581351 scopus 로고    scopus 로고
    • Acceleration and Inhibition of Amyloid-β Fibril Formation by Peptide-Conjugated Fluorescent-Maghemite Nanoparticles
    • Skaat, H.; Shafir, G.; Margel, S. Acceleration and Inhibition of Amyloid-β Fibril Formation by Peptide-Conjugated Fluorescent-Maghemite Nanoparticles J. Nanopart. Res. 2011, 13, 3521-3534
    • (2011) J. Nanopart. Res. , vol.13 , pp. 3521-3534
    • Skaat, H.1    Shafir, G.2    Margel, S.3
  • 24
    • 80052946027 scopus 로고    scopus 로고
    • Surface-Modified Protein Microspheres Capture Amyloid-β and Inhibit its Aggregation and Toxicity
    • Richman, M.; Wilk, S.; Skirtenko, N.; Perelman, A.; Rahimipour, S. Surface-Modified Protein Microspheres Capture Amyloid-β and Inhibit its Aggregation and Toxicity Chem.-Eur. J. 2011, 17, 11171-11177
    • (2011) Chem.-Eur. J. , vol.17 , pp. 11171-11177
    • Richman, M.1    Wilk, S.2    Skirtenko, N.3    Perelman, A.4    Rahimipour, S.5
  • 27
    • 84866097763 scopus 로고    scopus 로고
    • Engineered Polymer Nanoparticles Containing Hydrophobic Dipeptide for Inhibition of Amyloid-β Fibrillation
    • Skaat, H.; Chen, R.; Grinberg, I.; Margel, S. Engineered Polymer Nanoparticles Containing Hydrophobic Dipeptide for Inhibition of Amyloid-β Fibrillation Biomacromolecules 2012, 13, 2662-2670
    • (2012) Biomacromolecules , vol.13 , pp. 2662-2670
    • Skaat, H.1    Chen, R.2    Grinberg, I.3    Margel, S.4
  • 29
    • 84870614632 scopus 로고    scopus 로고
    • Negatively Charged Gold Nanoparticles Inhibit Alzheimers Amyloid-β Fibrillization, Induce Fibril Dissociation, and Mitigate Neurotoxicity
    • Liao, Y.-H.; Chang, Y.-J.; Yoshiike, Y.; Chang, Y.-C.; Chen, Y.-R. Negatively Charged Gold Nanoparticles Inhibit Alzheimers Amyloid-β Fibrillization, Induce Fibril Dissociation, and Mitigate Neurotoxicity Small 2012, 8, 3631-3639
    • (2012) Small , vol.8 , pp. 3631-3639
    • Liao, Y.-H.1    Chang, Y.-J.2    Yoshiike, Y.3    Chang, Y.-C.4    Chen, Y.-R.5
  • 33
    • 77953400398 scopus 로고    scopus 로고
    • Nanoparticle-Induced Folding and Fibril Formation of Coiled-Coil-Based Model Peptides
    • Wagner, S. C.; Roskamp, M.; Pallerla, M.; Araghi, R. R.; Schlecht, S.; Koksch, B. Nanoparticle-Induced Folding and Fibril Formation of Coiled-Coil-Based Model Peptides Small 2010, 6, 1321-1328
    • (2010) Small , vol.6 , pp. 1321-1328
    • Wagner, S.C.1    Roskamp, M.2    Pallerla, M.3    Araghi, R.R.4    Schlecht, S.5    Koksch, B.6
  • 35
    • 77955898208 scopus 로고    scopus 로고
    • Effects of DHLA-Capped CdSe/ZnS Quantum Dots on the Fibrillation of Human Serum Albumin
    • Vannoy, C. H.; Leblanc, R. M. Effects of DHLA-Capped CdSe/ZnS Quantum Dots on the Fibrillation of Human Serum Albumin J. Phys. Chem. B 2010, 114, 10881-10888
    • (2010) J. Phys. Chem. B , vol.114 , pp. 10881-10888
    • Vannoy, C.H.1    Leblanc, R.M.2
  • 38
    • 84900026924 scopus 로고    scopus 로고
    • Inhibition of Amyloid Fibril Growth and Dissolution of Amyloid Fibrils by Curcumin-Gold Nanoparticles
    • Palmal, S.; Maity, A. R.; Singh, B. K.; Basu, S.; Jana, N. R.; Jana, N. R. Inhibition of Amyloid Fibril Growth and Dissolution of Amyloid Fibrils by Curcumin-Gold Nanoparticles Chem.-Eur. J. 2014, 20, 6184-6191
    • (2014) Chem.-Eur. J. , vol.20 , pp. 6184-6191
    • Palmal, S.1    Maity, A.R.2    Singh, B.K.3    Basu, S.4    Jana, N.R.5    Jana, N.R.6
  • 39
    • 84875545405 scopus 로고    scopus 로고
    • Influence of the Physiochemical Properties of Superparamagnetic Iron Oxide Nanoparticles on Amyloid-β Protein Fibrillation in Solution
    • Mahmoudi, M.; Quinlan-Pluck, F.; Monopoli, M. P.; Sheibani, S.; Vali, H.; Dawson, K. A.; Lynch, I. Influence of the Physiochemical Properties of Superparamagnetic Iron Oxide Nanoparticles on Amyloid-β Protein Fibrillation in Solution ACS Chem. Neurosci. 2013, 4, 475-485
    • (2013) ACS Chem. Neurosci. , vol.4 , pp. 475-485
    • Mahmoudi, M.1    Quinlan-Pluck, F.2    Monopoli, M.P.3    Sheibani, S.4    Vali, H.5    Dawson, K.A.6    Lynch, I.7
  • 40
    • 84876523375 scopus 로고    scopus 로고
    • Glyconanoparticle Aided Detection of β-Amyloid by Magnetic Resonance Imaging and Attenuation of β-Amyloid Induced Cytotoxicity
    • Kouyoumdjian, H.; Zhu, D. C.; El-Dakdouki, M. H.; Lorenz, K.; Chen, J.; Li, W.; Huang, X. Glyconanoparticle Aided Detection of β-Amyloid by Magnetic Resonance Imaging and Attenuation of β-Amyloid Induced Cytotoxicity ACS Chem. Neur. Sci. 2013, 4, 575-584
    • (2013) ACS Chem. Neur. Sci. , vol.4 , pp. 575-584
    • Kouyoumdjian, H.1    Zhu, D.C.2    El-Dakdouki, M.H.3    Lorenz, K.4    Chen, J.5    Li, W.6    Huang, X.7
  • 41
    • 78650335230 scopus 로고    scopus 로고
    • Design and Development of Quantum Dots and Other Nanoparticles based Cellular Imaging Probe
    • Jana, N. R. Design and Development of Quantum Dots and Other Nanoparticles based Cellular Imaging Probe Phys. Chem. Chem. Phys. 2011, 13, 385-396
    • (2011) Phys. Chem. Chem. Phys. , vol.13 , pp. 385-396
    • Jana, N.R.1
  • 42
    • 0345306316 scopus 로고    scopus 로고
    • Single-Phase and Gram-Scale Routes toward Nearly Monodisperse Au and Other Noble Metal Nanocrystals
    • Jana, N. R.; Peng, X. Single-Phase and Gram-Scale Routes toward Nearly Monodisperse Au and Other Noble Metal Nanocrystals J. Am. Chem. Soc. 2003, 125, 14280-14281
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 14280-14281
    • Jana, N.R.1    Peng, X.2
  • 43
    • 73849123114 scopus 로고    scopus 로고
    • Imidazole Based Biocompatible Polymer Coating in Deriving <25 nm Functional Nanoparticle Probe for Cellular Imaging and Detection
    • Jana, N. R.; Patra, P. K.; Saha, A.; Basiruddin, S.; Pradhan, N. Imidazole Based Biocompatible Polymer Coating in Deriving <25 nm Functional Nanoparticle Probe for Cellular Imaging and Detection J. Phys. Chem. C 2009, 113, 21484-21492
    • (2009) J. Phys. Chem. C , vol.113 , pp. 21484-21492
    • Jana, N.R.1    Patra, P.K.2    Saha, A.3    Basiruddin, S.4    Pradhan, N.5
  • 44
    • 70449591841 scopus 로고    scopus 로고
    • Functionalized Plasmonic-Fluorescent Nanoparticles for Imaging and Detection
    • Saha, A.; Basiruddin, S.; Sarkar, R.; Pradhan, N.; Jana, N. R. Functionalized Plasmonic-Fluorescent Nanoparticles for Imaging and Detection J. Phys. Chem. C 2009, 113, 18492-18498
    • (2009) J. Phys. Chem. C , vol.113 , pp. 18492-18498
    • Saha, A.1    Basiruddin, S.2    Sarkar, R.3    Pradhan, N.4    Jana, N.R.5
  • 45
    • 0032849874 scopus 로고    scopus 로고
    • Quantification of Beta-Sheet Amyloid Fibril Structures with Thioflavin T
    • LeVin, H., III Quantification of Beta-Sheet Amyloid Fibril Structures with Thioflavin T Methods Enzymol. 1999, 309, 274-284
    • (1999) Methods Enzymol. , vol.309 , pp. 274-284
    • Levin, H.1
  • 46
    • 77952320068 scopus 로고    scopus 로고
    • Molecular Mechanism of Thioflavin-T Binding to Amyloid Fibrils
    • Biancalana, M.; Koide, S. Molecular Mechanism of Thioflavin-T Binding to Amyloid Fibrils Biochim. Biophys. Acta 1999, 1804, 1405-1412
    • (1999) Biochim. Biophys. Acta , vol.1804 , pp. 1405-1412
    • Biancalana, M.1    Koide, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.