A Bacteriophage Capsid Protein Provides a General Amyloid Interaction Motif (GAIM) That Binds and Remodels Misfolded Protein Assemblies
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- 作者：Rajaraman Krishnan1 ; &dagger ; ; rkrishnan@neurophage.com" class="auth_mail ; Haim Tsubery1 ; &dagger ; ; Ming Y. Proschitsky1 ; Eva Asp1 ; Michal Lulu1 ; Sharon Gilead1 ; Myra Gartner1 ; Jonathan P. Waltho2 ; 3 ; Peter J. Davis3 ; Andrea M. Hounslow3 ; Daniel A. Kirschner4 ; Hideyo Inouye4 ; David G. Myszka5 ; Jason Wright1 ; Beka Solomon6 ; Richard A. Fisher1 ; rfisher@neurophage.com" class="auth_mail
- 关键词：AD ; Alzheimer's disease ; BSA ; bovine serum albumin ; EDTA ; ethylenediaminetetraacetic acid ; HFIP ; hexafluoroisopropanol ; 1D ; one-dimensional ; MAb ; monoclonal antibody ; g3p ; gene 3 protein ; GAIM ; general amyloid interaction motif ; LCP ; luminescent conjugated polythiophene ; PTMI ; polythiophenes methyl imidazole ; PBS ; phosphate-buffered saline ; ThT ; thioflavin T ; CA ; cellulose acetate ; TROSY ; transverse relaxation optimized spectroscopy ; H/D ; hydrogen/deuterium ; RIPA ; radioimmunoprecipitation assay
- 刊名：Journal of Molecular Biology
- 出版年：26 June 2014
- 年：2014
- 卷：426
- 期：13
- 页码：2500-2519
- 全文大小：1562 K
文摘
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Phage capsid protein g3p recognizes amyloid fold.
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g3p(N1N2) binding to amyloids reflects structure function of g3p during infection.
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Recombinant bivalent g3p molecules remodel amyloids generically.
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g3p acts a general amyloid interaction motif.