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Volumn 9, Issue 2, 2015, Pages 1829-1836

Inhibition of the enhancement of infection of human immunodeficiency virus by semen-derived enhancer of virus infection using amyloid-targeting polymeric nanoparticles

Author keywords

acrylate; HIV; nanoparticles; polymer; SEVI; steric inhibition

Indexed keywords

BINDING ENERGY; GLYCOPROTEINS; MOLECULES; NANOPARTICLES; NANOSTRUCTURED MATERIALS; OLIGOMERS; POLYMERS; PROTEINS; SYNTHESIS (CHEMICAL); VIRUSES;

EID: 84923527033     PISSN: 19360851     EISSN: 1936086X     Source Type: Journal    
DOI: 10.1021/nn5067254     Document Type: Article
Times cited : (20)

References (36)
  • 4
    • 84856939995 scopus 로고    scopus 로고
    • Naturally Occurring Fragments from Two Distinct Regions of the Prostatic Acid Phosphatase Form Amyloidogenic Enhancers of HIV Infection
    • Arnold, F.; Schnell, J.; Zirafi, O.; Stürzel, C.; Meier, C.; Weil, T.; Ständker, L.; Forssmann, W.-G.; Roan, N. R.; Greene, W. C. Naturally Occurring Fragments from Two Distinct Regions of the Prostatic Acid Phosphatase Form Amyloidogenic Enhancers of HIV Infection J. Virol. 2012, 86, 1244-1249
    • (2012) J. Virol. , vol.86 , pp. 1244-1249
    • Arnold, F.1    Schnell, J.2    Zirafi, O.3    Stürzel, C.4    Meier, C.5    Weil, T.6    Ständker, L.7    Forssmann, W.-G.8    Roan, N.R.9    Greene, W.C.10
  • 7
    • 79953855831 scopus 로고    scopus 로고
    • Enhancement of HIV-1 Infectivity by Simple, Self-Assembling Modular Peptides
    • Easterhoff, D.; DiMaio, J. T. M.; Doran, T. M.; Dewhurst, S.; Nilsson, B. L. Enhancement of HIV-1 Infectivity by Simple, Self-Assembling Modular Peptides Biophys. J. 2011, 100, 1325-1334
    • (2011) Biophys. J. , vol.100 , pp. 1325-1334
    • Easterhoff, D.1    Dimaio, J.T.M.2    Doran, T.M.3    Dewhurst, S.4    Nilsson, B.L.5
  • 8
    • 84897557502 scopus 로고    scopus 로고
    • The Surprising Role of Amyloid Fibrils in HIV Infection
    • Castellano, L. M.; Shorter, J. The Surprising Role of Amyloid Fibrils in HIV Infection Biology. 2012, 1, 58-80
    • (2012) Biology. , vol.1 , pp. 58-80
    • Castellano, L.M.1    Shorter, J.2
  • 9
    • 76249097321 scopus 로고    scopus 로고
    • Aminoquinoline Surfen Inhibits the Action of SEVI (Semen-Derived Enhancer of Viral Infection)
    • Roan, N. R.; Sowinski, S.; Münch, J.; Kirchhoff, F.; Greene, W. C. Aminoquinoline Surfen Inhibits the Action of SEVI (Semen-Derived Enhancer of Viral Infection) J. Biol. Chem. 2010, 285, 1861-1869
    • (2010) J. Biol. Chem. , vol.285 , pp. 1861-1869
    • Roan, N.R.1    Sowinski, S.2    Münch, J.3    Kirchhoff, F.4    Greene, W.C.5
  • 10
    • 67049115575 scopus 로고    scopus 로고
    • The Main Green Tea Polyphenol Epigallocatechin-3-Gallate Counteracts Semen-Mediated Enhancement of HIV Infection
    • Hauber, I.; Hohenberg, H.; Holstermann, B.; Hunstein, W.; Hauber, J. The Main Green Tea Polyphenol Epigallocatechin-3-Gallate Counteracts Semen-Mediated Enhancement of HIV Infection Proc. Natl. Acad. Sci. U.S.A. 2009, 106, 9033-9038
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 9033-9038
    • Hauber, I.1    Hohenberg, H.2    Holstermann, B.3    Hunstein, W.4    Hauber, J.5
  • 13
    • 84866528327 scopus 로고    scopus 로고
    • Inhibition of Semen-Derived Enhancer of Virus Infection (SEVI) Fibrillogenesis by Zinc and Copper
    • Sheftic, S. R.; Snell, J. M.; Jha, S.; Alexandrescu, A. T. Inhibition of Semen-Derived Enhancer of Virus Infection (SEVI) Fibrillogenesis by Zinc and Copper Eur. Biophys. J. 2012, 41, 695-704
    • (2012) Eur. Biophys. J. , vol.41 , pp. 695-704
    • Sheftic, S.R.1    Snell, J.M.2    Jha, S.3    Alexandrescu, A.T.4
  • 14
    • 79952599026 scopus 로고    scopus 로고
    • Blocking Semen-Mediated Enhancement of HIV Infection by Amyloid-Binding Small Molecules
    • Kirchhoff, F.; Munch, J. Blocking Semen-Mediated Enhancement of HIV Infection by Amyloid-Binding Small Molecules Future Virol. 2011, 6, 183-186
    • (2011) Future Virol. , vol.6 , pp. 183-186
    • Kirchhoff, F.1    Munch, J.2
  • 15
    • 30344461610 scopus 로고    scopus 로고
    • Inhibiting Protein-Amyloid Interactions with Small Molecules: A Surface Chemistry Approach
    • Inbar, P.; Yang, J. Inhibiting Protein-Amyloid Interactions with Small Molecules: A Surface Chemistry Approach Bioorg. Med. Chem. Lett. 2006, 16, 1076-1079
    • (2006) Bioorg. Med. Chem. Lett. , vol.16 , pp. 1076-1079
    • Inbar, P.1    Yang, J.2
  • 16
    • 33749675670 scopus 로고    scopus 로고
    • Oligo(ethylene glycol) Derivatives of Thioflavin T as Inhibitors of Protein-Amyloid Interactions
    • Inbar, P.; Li, C. Q.; Takayama, S. A.; Bautista, M. R.; Yang, J. Oligo(ethylene glycol) Derivatives of Thioflavin T as Inhibitors of Protein-Amyloid Interactions ChemBioChem 2006, 7, 1563-1566
    • (2006) ChemBioChem , vol.7 , pp. 1563-1566
    • Inbar, P.1    Li, C.Q.2    Takayama, S.A.3    Bautista, M.R.4    Yang, J.5
  • 17
    • 42949139843 scopus 로고    scopus 로고
    • Assay to Screen for Molecules That Associate with Alzheimer's Related β-Amyloid Fibrils
    • Inbar, P.; Bautista, M. R.; Takayama, S. A.; Yang, J. Assay To Screen for Molecules That Associate with Alzheimer's Related β-Amyloid Fibrils Anal. Chem. 2008, 80, 3502-3506
    • (2008) Anal. Chem. , vol.80 , pp. 3502-3506
    • Inbar, P.1    Bautista, M.R.2    Takayama, S.A.3    Yang, J.4
  • 18
    • 84863057042 scopus 로고    scopus 로고
    • Enzyme-Linked Immunosorbent Assay-Based Method to Quantify the Association of Small Molecules with Aggregated Amyloid Peptides
    • Capule, C. C.; Yang, J. Enzyme-Linked Immunosorbent Assay-Based Method to Quantify the Association of Small Molecules with Aggregated Amyloid Peptides Anal. Chem. 2012, 84, 1786-1791
    • (2012) Anal. Chem. , vol.84 , pp. 1786-1791
    • Capule, C.C.1    Yang, J.2
  • 19
    • 78649820608 scopus 로고    scopus 로고
    • Inhibitors of Catalase-Amyloid Interactions Protect Cells from Beta-Amyloid-Induced Oxidative Stress and Toxicity
    • Habib, L. K.; Lee, M. T. C.; Yang, J. Inhibitors of Catalase-Amyloid Interactions Protect Cells from Beta-Amyloid-Induced Oxidative Stress and Toxicity J. Biol. Chem. 2010, 285, 38933-38943
    • (2010) J. Biol. Chem. , vol.285 , pp. 38933-38943
    • Habib, L.K.1    Lee, M.T.C.2    Yang, J.3
  • 20
    • 78149248966 scopus 로고    scopus 로고
    • Amyloid-Binding Small Molecules Efficiently Block SEVI (Semen-Derived Enhancer of Virus Infection)- and Semen-Mediated Enhancement of HIV-1 Infection
    • Olsen, J. S.; Brown, C.; Capule, C. C.; Rubinshtein, M.; Doran, T. M.; Srivastava, R. K.; Feng, C.; Nilsson, B. L.; Yang, J.; Dewhurst, S. Amyloid-Binding Small Molecules Efficiently Block SEVI (Semen-Derived Enhancer of Virus Infection)- and Semen-Mediated Enhancement of HIV-1 Infection J. Biol. Chem. 2010, 285, 35488-35496
    • (2010) J. Biol. Chem. , vol.285 , pp. 35488-35496
    • Olsen, J.S.1    Brown, C.2    Capule, C.C.3    Rubinshtein, M.4    Doran, T.M.5    Srivastava, R.K.6    Feng, C.7    Nilsson, B.L.8    Yang, J.9    Dewhurst, S.10
  • 21
    • 84862907885 scopus 로고    scopus 로고
    • Oligovalent Amyloid-Binding Agents Reduce SEVI-Mediated Enhancement of HIV-1 Infection
    • Capule, C. C.; Brown, C.; Olsen, J. S.; Dewhurst, S.; Yang, J. Oligovalent Amyloid-Binding Agents Reduce SEVI-Mediated Enhancement of HIV-1 Infection J. Am. Chem. Soc. 2012, 134, 905-908
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 905-908
    • Capule, C.C.1    Brown, C.2    Olsen, J.S.3    Dewhurst, S.4    Yang, J.5
  • 22
    • 0037388765 scopus 로고    scopus 로고
    • Structural Organization of Authentic, Mature HIV-1 Virions and Cores
    • Briggs, J. A. G.; Wilk, T.; Welker, R.; Kra, H.-G.; Fuller, S. D. Structural Organization of Authentic, Mature HIV-1 Virions and Cores EMBO J. 2003, 22, 1707-1715
    • (2003) EMBO J. , vol.22 , pp. 1707-1715
    • Briggs, J.A.G.1    Wilk, T.2    Welker, R.3    Kra, H.-G.4    Fuller, S.D.5
  • 23
    • 0029994114 scopus 로고    scopus 로고
    • Polyacrylamides Bearing Pendant α-Sialoside Groups Strongly Inhibit Agglutination of Erythrocytes by Influenza Virus: The Strong Inhibition Reflects Enhanced Binding through Cooperative Polyvalent Interactions
    • Sigal, G. B.; Mammen, M.; Dahmann, G.; Whitesides, G. M. Polyacrylamides Bearing Pendant α-Sialoside Groups Strongly Inhibit Agglutination of Erythrocytes by Influenza Virus: The Strong Inhibition Reflects Enhanced Binding through Cooperative Polyvalent Interactions J. Am. Chem. Soc. 1996, 118, 3789-3800
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 3789-3800
    • Sigal, G.B.1    Mammen, M.2    Dahmann, G.3    Whitesides, G.M.4
  • 24
    • 0028366108 scopus 로고
    • Poly(Alkylcyanoacrylate) Nanocapsules: Physicochemical Characterization and Mechanism of Formation
    • Chouinard, F.; Buczkowski, S.; Lenaerts, V. Poly(Alkylcyanoacrylate) Nanocapsules: Physicochemical Characterization and Mechanism of Formation Pharm. Res. 1994, 11, 869-874
    • (1994) Pharm. Res. , vol.11 , pp. 869-874
    • Chouinard, F.1    Buczkowski, S.2    Lenaerts, V.3
  • 25
    • 44749087481 scopus 로고    scopus 로고
    • Design and Production of Nanoparticles Formulated from Nano-Emulsion Templates-A Review
    • Anton, N.; Benoit, J.-P.; Saulnier, P. Design and Production of Nanoparticles Formulated from Nano-Emulsion Templates-A Review J. Controlled Release 2008, 128, 185-199
    • (2008) J. Controlled Release , vol.128 , pp. 185-199
    • Anton, N.1    Benoit, J.-P.2    Saulnier, P.3
  • 27
    • 0026417546 scopus 로고
    • A Kinetic Investigation of Butyl Acrylate Polymerization
    • Dube, M. A.; Rilling, K.; Penlidis, A. A Kinetic Investigation of Butyl Acrylate Polymerization J. Appl. Polym. Sci. 1991, 43, 2137-2145
    • (1991) J. Appl. Polym. Sci. , vol.43 , pp. 2137-2145
    • Dube, M.A.1    Rilling, K.2    Penlidis, A.3
  • 28
    • 55349119903 scopus 로고    scopus 로고
    • Preparation of Carmustine-loaded PLA Ultrasmall-nanoparticles by Adjusting Micellar Behavior of Surfactants
    • Yan, C.; Yuan, X.; Kang, C.; Zhao, Y.-H.; Liu, J.; Guo, Y.; Lu, J.; Pu, P.; Sheng, J. Preparation of Carmustine-loaded PLA Ultrasmall-nanoparticles by Adjusting Micellar Behavior of Surfactants J. Appl. Polym. Sci. 2008, 110, 2446-2452
    • (2008) J. Appl. Polym. Sci. , vol.110 , pp. 2446-2452
    • Yan, C.1    Yuan, X.2    Kang, C.3    Zhao, Y.-H.4    Liu, J.5    Guo, Y.6    Lu, J.7    Pu, P.8    Sheng, J.9
  • 30
    • 54249083926 scopus 로고    scopus 로고
    • A Comparison of Atomic Force Microscopy (AFM) and Dynamic Light Scattering (DLS) Methods to Characterize Nanoparticle Size Distributions
    • Hoo, C. M.; Starostin, N.; West, P.; Mecartney, M. L. A Comparison of Atomic Force Microscopy (AFM) and Dynamic Light Scattering (DLS) Methods to Characterize Nanoparticle Size Distributions J. Nanoparticle Res. 2008, 10, 89-96
    • (2008) J. Nanoparticle Res. , vol.10 , pp. 89-96
    • Hoo, C.M.1    Starostin, N.2    West, P.3    Mecartney, M.L.4
  • 31
    • 0026647722 scopus 로고
    • Alkylcyanoacrylate Drug Carriers: I. Physicochemical Characterization of Nanoparticles with Different Alkyl Chain Length
    • Muller, R. H.; Lherm, C.; Herbort, J.; Blunk, T.; Couvreur, P. Alkylcyanoacrylate Drug Carriers: I. Physicochemical Characterization of Nanoparticles with Different Alkyl Chain Length Int. J. Pharm. 1992, 84, 1-11
    • (1992) Int. J. Pharm. , vol.84 , pp. 1-11
    • Muller, R.H.1    Lherm, C.2    Herbort, J.3    Blunk, T.4    Couvreur, P.5
  • 33
    • 84866704372 scopus 로고    scopus 로고
    • Biocompatible Polymeric Nanoparticles Degrade and Release Cargo in Response to Biologically Relevant Levels of Hydrogen Peroxide
    • De Gracia Lux, C.; Joshi-Barr, S.; Nguyen, T.; Mahmoud, E.; Schopf, E.; Fomina, N.; Almutairi, A. Biocompatible Polymeric Nanoparticles Degrade and Release Cargo in Response to Biologically Relevant Levels of Hydrogen Peroxide J. Am. Chem. Soc. 2012, 134, 15758-15764
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 15758-15764
    • De Gracia Lux, C.1    Joshi-Barr, S.2    Nguyen, T.3    Mahmoud, E.4    Schopf, E.5    Fomina, N.6    Almutairi, A.7
  • 35
    • 84923524731 scopus 로고    scopus 로고
    • Delivery of Polymeric Nanoparticles to Target Vascular Diseases
    • Agyare, E.; Kandimalla, K. Delivery of Polymeric Nanoparticles to Target Vascular Diseases Biomol. Res. Ther. 2014, S1:001, 1-11
    • (2014) Biomol. Res. Ther. , vol.1001 , pp. 1-11
    • Agyare, E.1    Kandimalla, K.2
  • 36
    • 3343003514 scopus 로고    scopus 로고
    • Techniques to Study Amyloid Fibril Formation in Vitro
    • Nilsson, M. R. Techniques to Study Amyloid Fibril Formation in Vitro Methods 2004, 34, 151-160
    • (2004) Methods , vol.34 , pp. 151-160
    • Nilsson, M.R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.