Randomization of Amyloid-β-Peptide(1-42) Conformation by Sulfonated and Sulfated Nanoparticles Reduces Aggregation and Cytotoxicity

被引：29
|
作者：
Saraiva, Ana M. [1 ,2 ]
Cardoso, Isabel [3 ,4 ]
Saraiva, Maria Joao [3 ]
Tauer, Klaus [1 ]
Pereira, M. Carmo [2 ]
Coelho, Manuel A. N. [2 ]
Moehwald, Helmuth [1 ]
Brezesinski, Gerald [1 ]
机构：
[1] Max Planck Inst Colloids & Interfaces, D-14476 Potsdam, Germany
[2] Univ Porto, LEPAE, Dept Engn Quim, Fac Engn, P-4200465 Oporto, Portugal
[3] Inst Biol Mol & Celular, Mol Neurobiol Unit, P-4150180 Oporto, Portugal
[4] Inst Politecn Porto, Escola Super Tecnol Saude Porto, P-4400330 Vila Nova De Gaia, Portugal
来源：
MACROMOLECULAR BIOSCIENCE | 2010年 / 10卷 / 10期
关键词：
amyloid-beta peptides; cytotoxicity; nanoparticles; oligomers; polystyrene; SMALL-MOLECULE INHIBITORS; CENTRAL-NERVOUS-SYSTEM; BETA-AMYLOID PEPTIDES; PROTEIN A-BETA; ALZHEIMERS-DISEASE; TEMPERATURE-DEPENDENCE; OLIGOMERS; NEUROTOXICITY; DEGENERATION; A-BETA(1-42);
D O I：
10.1002/mabi.200900448
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
The amyloid-beta peptide (A beta) plays a central role in the mechanism of Alzheimer's disease, being the main constituent of the plaque deposits found in AD brains. A beta amyloid formation and deposition are due to a conformational switching to a beta-enriched secondary structure. Our strategy to inhibit A beta aggregation involves the reconversion of A beta conformation by adsorption to nanoparticles. NPs were synthesized by sulfonation and sulfation of polystyrene, leading to microgels and latexes. Both polymeric nanostructures affect the conformation of AB inducing an unordered state. Oligomerization was delayed and cytotoxicity reduced. The proper balance between hydrophilic moieties and hydrophobic chains seems to be an essential feature of effective NPs.
引用
收藏
页码：1152 / 1163
页数：12
相关论文
共 50 条
  • [1] RRY Inhibits Amyloid-β1-42 Peptide Aggregation and Neurotoxicity
    Sun, Xicui
    Duan, Songwei
    Cao, Anna
    Villagomez, Bryan
    Lin, Runxuan
    Chen, Hongxia
    Pi, Liya
    Ren, Bin
    Chen, Rong
    Chen, Minjie
    Ying, Zhekang
    Fang, Shenyun
    Cao, Qi
    JOURNAL OF ALZHEIMERS DISEASE REPORTS, 2021, 5 (01) : 479 - 495
  • [2] Amyloid-(1-42) Aggregation Initiates Its Cellular Uptake and Cytotoxicity
    Jin, Sha
    Kedia, Niraja
    Illes-Toth, Eva
    Haralampiev, Ivan
    Prisner, Simon
    Herrmann, Andreas
    Wanker, Erich E.
    Bieschke, Jan
    JOURNAL OF BIOLOGICAL CHEMISTRY, 2016, 291 (37) : 19590 - 19606
  • [3] Aggregation of Alzheimer Amyloid β Peptide (1-42) on the Multivalent Sulfonated Sugar Interface
    Fukuda, Tomohiro
    Matsumoto, Erino
    Onogi, Shunsuke
    Miura, Yoshiko
    BIOCONJUGATE CHEMISTRY, 2010, 21 (06) : 1079 - 1086
  • [4] Nitration of amyloid-β peptide (1-42) as a protective mechanism for the amyloid-β peptide (1-42) against copper ion toxicity
    Zhao, Jie
    Gao, Wanxia
    Yang, Zhen
    Li, Hailing
    Gao, Zhonghong
    JOURNAL OF INORGANIC BIOCHEMISTRY, 2019, 190 : 15 - 23
  • [5] Controlling Amyloid-β Peptide(1-42) Oligomerization and Toxicity by Fluorinated Nanoparticles
    Saraiva, Ana M.
    Cardoso, Isabel
    Carmo Pereira, M.
    Coelho, Manuel A. N.
    Joao Saraiva, Maria
    Moehwald, Helmuth
    Brezesinski, Gerald
    CHEMBIOCHEM, 2010, 11 (13) : 1905 - 1913
  • [6] Sulfated Polysaccharides Promote the Assembly of Amyloid β1-42 Peptide into Stable Fibrils of Reduced Cytotoxicity
    Bravo, Ramona
    Arimon, Muriel
    Valle-Delgado, Juan Jose
    Garcia, Raquel
    Durany, Nuria
    Castel, Susanna
    Cruz, Montserrat
    Ventura, Salvador
    Fernandez-Busquets, Xavier
    JOURNAL OF BIOLOGICAL CHEMISTRY, 2008, 283 (47) : 32471 - 32483
  • [7] Clusterin Binding Modulates the Aggregation and Neurotoxicity of Amyloid-β(1-42)
    Kim, Yun-Mi
    Park, SuJi
    Choi, Su Yeon
    Oh, Shin Bi
    Jung, MinKyo
    Pack, Chan-Gi
    Hwang, Jung Jin
    Tak, Eunyoung
    Lee, Joo-Yong
    MOLECULAR NEUROBIOLOGY, 2022, 59 (10) : 6228 - 6244
  • [8] Lipid-based nanoparticles with high binding affinity for amyloid-β1-42 peptide
    Gobbi, Marco
    Re, Francesca
    Canovi, Mara
    Beeg, Marten
    Gregori, Maria
    Sesana, Silvia
    Sonnino, Sandro
    Brogioli, Doriano
    Musicanti, Claudia
    Gasco, Paolo
    Salmona, Mario
    Masserini, Massimo E.
    BIOMATERIALS, 2010, 31 (25) : 6519 - 6529
  • [9] In vitro fibrillization of Alzheimer's amyloid-β peptide (1-42)
    Tiiman, Ann
    Krishtal, Jekaterina
    Palumaa, Peep
    Tougu, Vello
    AIP ADVANCES, 2015, 5 (09):
  • [10] Histone H1 Favors Folding and Parallel Fibrillar Aggregation of the 1-42 Amyloid-β Peptide
    Roque, Alicia
    Sortino, Rosalba
    Ventura, Salvador
    Ponte, Inma
    Suau, Pedro
    LANGMUIR, 2015, 31 (24) : 6782 - 6790
12345