Binding of amyloid beta-peptide to ganglioside micelles is dependent on histidine-13.

The Biochemical Journal
Mike P WilliamsonTetsuo Asakura

Abstract

Amyloid beta-peptide (Abeta) is a major component of plaques in Alzheimer's disease, and formation of senile plaques has been suggested to originate from regions of neuronal membrane rich in gangliosides. Here we demonstrate using NMR on 15N-labelled Abeta-(1-40) and Abeta-(1-42) that the interaction with ganglioside G(M1) micelles is localized to the N-terminal region of the peptide, particularly residues His13 to Leu17, which become more helical when bound. The key interaction is with His13, which undergoes a G(M1)-specific conformational change. The sialic acid residue of the ganglioside headgroup is important for determining the nature of the conformational change. The isolated pentasaccharide headgroup of G(M1) is not bound, suggesting the need for a polyanionic surface. Binding to heparin confirms this suggestion, since binding is of similar affinity but does not produce the same conformational changes in the peptide. A comparison of Abeta-(1-40) and Abeta-(1-42) indicates that binding to G(M1) micelles is not related to oligomerization, which occurs at the C-terminal end. These results imply that binding to ganglioside micelles causes a transition from random coil to alpha-helix in the N-terminal region, leaving the C-te...Continue Reading

References

Aug 15, 1990·Biopolymers·M P Williamson
Jan 1, 1989·Annual Review of Neuroscience·D J Selkoe
Jan 1, 1986·Proceedings of the National Academy of Sciences of the United States of America·D A KirschnerD J Selkoe
Oct 1, 1984·Journal of Neurochemistry·I KraĉunA Stavljenić
Jan 23, 1995·Behavioural Brain Research·Y Nagai
Sep 1, 1993·Proteins·Y BaiS W Englander
Dec 1, 1993·Journal of Neurochemistry·K R BrundenR C Frederickson
Mar 21, 1998·The Journal of Biological Chemistry·J McLaurinA Chakrabartty
Aug 15, 2000·Journal of Structural Biology·S ZhangJ P Lee
Aug 30, 2000·The Journal of Biological Chemistry·T H HuangA Chakrabartty
Oct 13, 2000·European Journal of Biochemistry·J McLaurin, P E Fraser
May 10, 2001·Proceedings of the National Academy of Sciences of the United States of America·B Wolozin
May 23, 2001·Archives of Biochemistry and Biophysics·T ArigaT Miyatake
Mar 7, 2002·Journal of Agricultural and Food Chemistry·Adrian J CharltonMichael P Williamson
Aug 28, 2002·Biochemical Society Transactions·D M WalshD J Selkoe
Mar 28, 2003·Biochemical and Biophysical Research Communications·Atsuko KakioKatsumi Matsuzaki
Oct 15, 2003·Journal of Molecular Biology·Jonathan MorrisonDavid Neuhaus
Jun 17, 2004·Journal of Neurochemistry·Naoki YamamotoKatsuhiko Yanagisawa
Dec 21, 2004·Nature Neuroscience·James P ClearyKaren H Ashe
Jan 26, 2005·The Journal of Clinical Investigation·Robert P BrendzaDavid M Holtzman
Feb 15, 2005·Biochemical and Biophysical Research Communications·Masaki WakabayashiKatsumi Matsuzaki
Apr 27, 2005·Proceedings of the National Academy of Sciences of the United States of America·Gerald P GellermannMarcus Fändrich
Aug 13, 2005·Journal of Molecular Biology·Claire GoldsburyShirley A Müller

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Citations

Nov 1, 2008·Cell Biochemistry and Biophysics·Roberth ByströmGerhard Gröbner
Jul 26, 2007·Biochemistry·Christine O SallumAndrei T Alexandrescu
Aug 4, 2012·ACS Chemical Neuroscience·Sharmistha SinhaGal Bitan
Jul 21, 2010·Alzheimer's Research & Therapy·Kerensa BroersenJoost Schymkowitz
Mar 13, 2008·Journal of Lipid Research·Toshio ArigaRobert K Yu
Feb 15, 2011·International Journal of Alzheimer's Disease·Maho Yagi-UtsumiKoichi Kato
Nov 10, 2013·Advances in Colloid and Interface Science·Annalisa ReliniAlessandra Gliozzi
Mar 6, 2012·Science China. Chemistry·Bin SunXuefei Huang
Dec 23, 2015·International Journal of Molecular Sciences·Ian James Martins
Jan 14, 2009·Chemistry and Physics of Lipids·Yasumoto NakazawaTetsuo Asakura
Sep 10, 2015·Biological Chemistry·Yanhui XiangGuanghou Shui
Jan 11, 2011·Journal of Neurochemistry·Katsuhiko Yanagisawa
Mar 30, 2016·Journal of Molecular Modeling·Juho LeeArt E Cho
Jan 29, 2011·International Journal of Alzheimer's Disease·Toshio ArigaRobert K Yu
Apr 24, 2015·Glycoconjugate Journal·Katsuhiko Yanagisawa
May 9, 2016·Journal of Biological Physics·Matjaž ŽganecBrigita Urbanc
May 12, 2007·Journal of Neuroscience Research·Gerald P GellermannStephan Diekmann
May 7, 2009·Biotechnology and Bioengineering·Irina RamosTheresa A Good
Oct 1, 2010·Protein Science : a Publication of the Protein Society·Ben KeshetTheresa A Good
May 3, 2019·Scientific Reports·Yuhei TachiHisashi Okumura
Jun 3, 2016·The Journal of Biological Chemistry·Nasrollah Rezaei-GhalehMarkus Zweckstetter
Feb 2, 2018·Chemical & Pharmaceutical Bulletin·Majid VahedTyuji Hoshino
Jun 23, 2020·Protein Science : a Publication of the Protein Society·Jacques FantiniNouara Yahi
Feb 27, 2020·International Journal of Molecular Sciences·Yu-Chia KaoKuen-Jer Tsai
Mar 17, 2020·Journal of Alzheimer's Disease : JAD·Ariel J Kuhn, Jevgenij Raskatov
Oct 30, 2020·Frontiers in Neuroscience·Simonetta SipioneVaibhavi Kadam
Feb 19, 2021·Journal of the American Chemical Society·Debabrata MaityAndrew D Hamilton
Mar 7, 2021·Chemistry and Physics of Lipids·Sara García-ViñualesDanilo Milardi
Oct 1, 2020·Scientific Reports·Valentina GrecoEnrico Rizzarelli

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