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
  • [21] Isolated Amyloid-β(1-42) Protofibrils, But Not Isolated Fibrils, Are Robust Stimulators of Microglia
    Paranjape, Geeta S.
    Gouwens, Lisa K.
    Osborn, David C.
    Nichols, Michael R.
    ACS CHEMICAL NEUROSCIENCE, 2012, 3 (04): : 302 - 311
  • [22] Menadione sodium bisulfite inhibits the toxic aggregation of amyloid-β(1-42)
    Zhang, Yu
    Zhao, Yudan
    Wang, Zhuoyi
    Gong, Hao
    Ma, Liang
    Sun, Dongsheng
    Yang, Chen
    Li, Yang
    Cheng, Biao
    Petersen, Robert B.
    Jiang, Fengchao
    Liu, Gongping
    Huang, Kun
    BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS, 2018, 1862 (10): : 2226 - 2235
  • [23] α-synuclein induced synapse damage is enhanced by amyloid-β1-42
    Bate, Clive
    Gentleman, Steve
    Williams, Alun
    MOLECULAR NEURODEGENERATION, 2010, 5
  • [24] Ganglioside-mediated aggregation of amyloid β-proteins (Aβ): comparison between Aβ-(1-42) and Aβ-(1-40)
    Ogawa, Mariko
    Tsukuda, Miho
    Yamaguchi, Takahiro
    Ikeda, Keisuke
    Okada, Takuma
    Yano, Yoshiaki
    Hoshino, Masaru
    Matsuzaki, Katsumi
    JOURNAL OF NEUROCHEMISTRY, 2011, 116 (05) : 851 - 857
  • [25] Molecular Integrative Study on Inhibitory Effects of Pentapeptides on Polymerization and Cell Toxicity of Amyloid-β Peptide (1-42)
    Ye, Lianmeng
    Ajuyo, Nuela Manka'a Che
    Wu, Zhongyun
    Yuan, Nan
    Xiao, Zhengpan
    Gu, Wenyu
    Zhao, Jiazheng
    Pei, Yechun
    Min, Yi
    Wang, Dayong
    CURRENT ISSUES IN MOLECULAR BIOLOGY, 2024, 46 (09) : 10160 - 10179
  • [26] Preparation and characterization of lipid-based nanoparticles binding with high affinity amyloid-β1-42 peptide
    Re, Francesca
    Gobbi, Marco
    Salmona, Mario
    Gasco, Paolo
    Cazzaniga, Emanuela
    Moore, Susan
    JOURNAL OF BIOTECHNOLOGY, 2010, 150 : S27 - S27
  • [27] Chemical modifications of amyloid-β(1-42) have a significant impact on the repertoire of brain amyloid-β(1-42) binding proteins
    Medvedev, Alexei E.
    Buneeva, Olga A.
    Kopylov, Arthur T.
    Mitkevich, Vladimir A.
    Kozin, Sergey A.
    Zgoda, Victor G.
    Makarov, Alexander A.
    BIOCHIMIE, 2016, 128 : 55 - 58
  • [28] Effect of Ovocystatin on Amyloid β 1-42 Aggregation-In Vitro Studies
    Stanczykiewicz, Bartlomiej
    Goszczynski, Tomasz M.
    Migdal, Pawel
    Piksa, Marta
    Pawlik, Krzysztof
    Gburek, Jakub
    Golab, Krzysztof
    Konopska, Boguslawa
    Zablocka, Agnieszka
    INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, 2023, 24 (06)
  • [29] Diverse Ecdysterones Show Different Effects on Amyloid-β42 Aggregation but All Uniformly Inhibit Amyloid-β42-Induced Cytotoxicity
    Yang, Shi-Gao
    Zhang, Xi
    Sun, Xiao-Sia
    Ling, Tie-Jun
    Feng, Ying
    Du, Xue-Ying
    Zhao, Min
    Yang, Yang
    Xue, Di
    Wang, Li
    Liu, Rui-Tian
    JOURNAL OF ALZHEIMERS DISEASE, 2010, 22 (01) : 107 - 117
  • [30] Amyloid Fibril Formation of Arctic Amyloid-β 1-42 Peptide is Efficiently Inhibited by the BRICHOS Domain
    Zhong, Xueying
    Kumar, Rakesh
    Wang, Yu
    Biverstal, Henrik
    Jegerschoeld, Caroline Ingeborg
    Koeck, Philip J. B.
    Johansson, Jan
    Abelein, Axel
    Chen, Gefei
    ACS CHEMICAL BIOLOGY, 2022, 17 (08) : 2201 - 2211
12345