Small-molecule conversion of toxic oligomers to nontoxic β-sheet–rich amyloid fibrils

被引:0
|
作者
Jan Bieschke
Martin Herbst
Thomas Wiglenda
Ralf P Friedrich
Annett Boeddrich
Franziska Schiele
Daniela Kleckers
Juan Miguel Lopez del Amo
Björn A Grüning
Qinwen Wang
Michael R Schmidt
Rudi Lurz
Roger Anwyl
Sigrid Schnoegl
Marcus Fändrich
Ronald F Frank
Bernd Reif
Stefan Günther
Dominic M Walsh
Erich E Wanker
机构
[1] Neuroproteomics,Department of Neurology
[2] Max Delbrueck Center for Molecular Medicine,Department of Physiology
[3] Charité-Universitätsmedizin Berlin,Department of Chemistry
[4] Helmholtz Centre for Infection Research,undefined
[5] Institute of Pharmaceutical Sciences,undefined
[6] Albert-Ludwigs-University Freiburg,undefined
[7] School of Medicine,undefined
[8] Trinity College,undefined
[9] Max Planck Institute for Molecular Genetics,undefined
[10] Max Planck Research Unit for Enzymology of Protein Folding,undefined
[11] Helmholtz Center for Infection Research,undefined
[12] Technical University Munich,undefined
[13] Laboratory for Neurodegenerative Research,undefined
[14] The Conway Institute for Biomolecular and Biomedical Research,undefined
[15] University College Dublin,undefined
[16] Present addresses: Department of Biomedical Engineering,undefined
[17] Washington University in St. Louis,undefined
[18] St. Louis,undefined
[19] Missouri,undefined
[20] USA (J.B.) and Department of Physiology and Pharmacology,undefined
[21] Medical School,undefined
[22] Ningbo University,undefined
[23] Ningbo,undefined
[24] China (Q.W.).,undefined
来源
Nature Chemical Biology | 2012年 / 8卷
关键词
D O I
暂无
中图分类号
学科分类号
摘要
An orcein-related small molecule can drive polymerization of amyloid-β, implicated in Alzheimer's disease, without remodeling oligomeric or fibril forms but by stabilizing a seeding-competent protofilament state and shortening the lag phase of spontaneous polymerization.[graphic not available: see fulltext]
引用
收藏
页码:93 / 101
页数:8
相关论文
共 50 条
  • [1] Small-molecule conversion of toxic oligomers to nontoxic β-sheet-rich amyloid fibrils
    Bieschke, Jan
    Herbst, Martin
    Wiglenda, Thomas
    Friedrich, Ralf P.
    Boeddrich, Annett
    Schiele, Franziska
    Kleckers, Daniela
    del Amo, Juan Miguel Lopez
    Gruening, Bjoern A.
    Wang, Qinwen
    Schmidt, Michael R.
    Lurz, Rudi
    Anwyl, Roger
    Schnoegl, Sigrid
    Faendrich, Marcus
    Frank, Ronald F.
    Reif, Bernd
    Guenther, Stefan
    Walsh, Dominic M.
    Wanker, Erich E.
    NATURE CHEMICAL BIOLOGY, 2012, 8 (01) : 93 - 101
  • [2] Small Molecule Induced Conversion of Toxic Oligomers to Non-Toxic Beta-Sheet-Rich Amyloid Fibrils
    Bieschke, Jan
    BIOPHYSICAL JOURNAL, 2012, 102 (03) : 454A - 455A
  • [3] Spectroscopic Signature for Stable β-Amyloid Fibrils versus β-Sheet-Rich Oligomers
    Lomont, Justin P.
    Rich, Kacie L.
    Maj, Michal
    Ho, Jia-Jung
    Ostrander, Joshua S.
    Zanni, Martin T.
    JOURNAL OF PHYSICAL CHEMISTRY B, 2018, 122 (01): : 144 - 153
  • [4] Toxic species in amyloid disorders: Oligomers or mature fibrils
    Verma, Meenakshi
    Vats, Abhishek
    Taneja, Vibha
    ANNALS OF INDIAN ACADEMY OF NEUROLOGY, 2015, 18 (02) : 138 - 145
  • [5] Conversion of non-fibrillar β-sheet oligomers into amyloid fibrils in Alzheimer's disease amyloid peptide aggregation
    Benseny-Cases, Nuria
    Cocera, Mercedes
    Cladera, Josep
    BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2007, 361 (04) : 916 - 921
  • [6] Amyloid-β forms fibrils by nucleated conformational conversion of oligomers
    Lee J.
    Culyba E.K.
    Powers E.T.
    Kelly J.W.
    Nature Chemical Biology, 2011, 7 (9) : 602 - 609
  • [7] Shaking Alone Induces De Novo Conversion of Recombinant Prion Proteins to β-Sheet Rich Oligomers and Fibrils
    Ladner-Keay, Carol L.
    Griffith, Bethany J.
    Wishart, David S.
    PLOS ONE, 2014, 9 (06):
  • [8] Amyloid-β forms fibrils by nucleated conformational conversion of oligomers
    Lee, Jiyong
    Culyba, Elizabeth K.
    Powers, Evan T.
    Kelly, Jeffery W.
    NATURE CHEMICAL BIOLOGY, 2011, 7 (09) : 602 - 609
  • [9] Probing small molecule binding to amyloid fibrils
    Buell, Alexander K.
    Esbjoerner, Elin K.
    Riss, Patrick J.
    White, Duncan A.
    Aigbirhio, Franklin I.
    Toth, Gergely
    Welland, Mark E.
    Dobson, Christopher M.
    Knowles, Tuomas P. J.
    PHYSICAL CHEMISTRY CHEMICAL PHYSICS, 2011, 13 (45) : 20044 - 20052
  • [10] Inhibition by small-molecule ligands of formation of amyloid fibrils of an immunoglobulin light chain variable domain
    Brumshtein, Boris
    Esswein, Shannon R.
    Salwinski, Lukasz
    Phillips, Martin L.
    Ly, Alan T.
    Cascio, Duilio
    Sawaya, Michael R.
    Eisenberg, David S.
    ELIFE, 2015, 4