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Aβ(39–42) Modulates Aβ Oligomerization but Not Fibril Formation

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Department of Chemistry and Biochemistry, University of California at Santa Barbara, Santa Barbara, California 93106, United States
Department of Physics, University of California at Santa Barbara, Santa Barbara, California 93106, United States
§ ∥ ⊥ §Department of Neurology, David Geffen School of Medicine, Brain Research Institute, and Molecular Biology Institute, University of California at Los Angeles, Los Angeles, California 90095, United States
*Phone: 805-893-2893. Fax: 805-893-8703. E-mail: [email protected]
Cite this: Biochemistry 2012, 51, 1, 108–117
Publication Date (Web):November 30, 2011
https://doi.org/10.1021/bi201520b
Copyright © 2011 American Chemical Society

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    Abstract

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    Recently, certain C-terminal fragments (CTFs) of Aβ42 have been shown to be effective inhibitors of Aβ42 toxicity. Here, we examine the interactions between the shortest CTF in the original series, Aβ(39–42), and full-length Aβ. Mass spectrometry results indicate that Aβ(39–42) binds directly to Aβ monomers and to the n = 2, 4, and 6 oligomers. The Aβ42:Aβ(39–42) complex is further probed using molecular dynamics simulations. Although the CTF was expected to bind to the hydrophobic C-terminus of Aβ42, the simulations show that Aβ(39–42) binds at several locations on Aβ42, including the C-terminus, other hydrophobic regions, and preferentially in the N-terminus. Ion mobility–mass spectrometry (IM-MS) and electron microscopy experiments indicate that Aβ(39–42) disrupts the early assembly of full-length Aβ. Specifically, the ion-mobility results show that Aβ(39–42) prevents the formation of large decamer/dodecamer Aβ42 species and, moreover, can remove these structures from solution. At the same time, thioflavin T fluorescence and electron microscopy results show that the CTF does not inhibit fibril formation, lending strong support to the hypothesis that oligomers and not amyloid fibrils are the Aβ form responsible for toxicity. The results emphasize the role of small, soluble assemblies in Aβ-induced toxicity and suggest that Aβ(39–42) inhibits Aβ-induced toxicity by a unique mechanism, modulating early assembly into nontoxic hetero-oligomers, without preventing fibril formation.

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    Additional ion mobility data of Aβ:CTF mixtures, starting structures for the MD simulations, and representative structures of the Aβ:CTF complexes from the most populated structural families. This material is available free of charge via the Internet at http://pubs.acs.org.

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    11. Amy G. Wong, Chun Wu, Eleni Hannaberry, Matthew D. Watson, Joan-Emma Shea, and Daniel P. Raleigh . Analysis of the Amyloidogenic Potential of Pufferfish (Takifugu rubripes) Islet Amyloid Polypeptide Highlights the Limitations of Thioflavin-T Assays and the Difficulties in Defining Amyloidogenicity. Biochemistry 2016, 55 (3) , 510-518. https://doi.org/10.1021/acs.biochem.5b01107
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    13. Ravit Malishev, Sukhendu Nandi, Sofiya Kolusheva, Yael Levi-Kalisman, Frank-Gerrit Klärner, Thomas Schrader, Gal Bitan, and Raz Jelinek . Toxicity Inhibitors Protect Lipid Membranes from Disruption by Aβ42. ACS Chemical Neuroscience 2015, 6 (11) , 1860-1869. https://doi.org/10.1021/acschemneuro.5b00200
    14. Xueyun Zheng, Deyu Liu, Robin Roychaudhuri, David B. Teplow, and Michael T. Bowers . Amyloid β-Protein Assembly: Differential Effects of the Protective A2T Mutation and Recessive A2V Familial Alzheimer’s Disease Mutation. ACS Chemical Neuroscience 2015, 6 (10) , 1732-1740. https://doi.org/10.1021/acschemneuro.5b00171
    15. James R. Arndt, Samaneh Ghassabi Kondalaji, Megan M. Maurer, Arlo Parker, Justin Legleiter, and Stephen J. Valentine . Huntingtin N-Terminal Monomeric and Multimeric Structures Destabilized by Covalent Modification of Heteroatomic Residues. Biochemistry 2015, 54 (28) , 4285-4296. https://doi.org/10.1021/acs.biochem.5b00478
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    17. Neng Xiong, Xiao-Yan Dong, Jie Zheng, Fu-Feng Liu, and Yan Sun . Design of LVFFARK and LVFFARK-Functionalized Nanoparticles for Inhibiting Amyloid β-Protein Fibrillation and Cytotoxicity. ACS Applied Materials & Interfaces 2015, 7 (10) , 5650-5662. https://doi.org/10.1021/acsami.5b00915
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    19. Sanghyun Lee, Xueyun Zheng, Janarthanan Krishnamoorthy, Masha G. Savelieff, Hyun Min Park, Jeffrey R. Brender, Jin Hoon Kim, Jeffrey S. Derrick, Akiko Kochi, Hyuck Jin Lee, Cheal Kim, Ayyalusamy Ramamoorthy, Michael T. Bowers, and Mi Hee Lim . Rational Design of a Structural Framework with Potential Use to Develop Chemical Reagents That Target and Modulate Multiple Facets of Alzheimer’s Disease. Journal of the American Chemical Society 2014, 136 (1) , 299-310. https://doi.org/10.1021/ja409801p
    20. Christian Bleiholder, Thanh D. Do, Chun Wu, Nicholas J. Economou, Summer S. Bernstein, Steven K. Buratto, Joan-Emma Shea, and Michael T. Bowers . Ion Mobility Spectrometry Reveals the Mechanism of Amyloid Formation of Aβ(25–35) and Its Modulation by Inhibitors at the Molecular Level: Epigallocatechin Gallate and Scyllo-inositol. Journal of the American Chemical Society 2013, 135 (45) , 16926-16937. https://doi.org/10.1021/ja406197f
    21. Jeppe T. Pedersen and Niels H. H. Heegaard . Analysis of Protein Aggregation in Neurodegenerative Disease. Analytical Chemistry 2013, 85 (9) , 4215-4227. https://doi.org/10.1021/ac400023c
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    23. Carlos Gutierrez-Merino. Brain Hydrophobic Peptides Antagonists of Neurotoxic Amyloid β Peptide Monomers/Oligomers–Protein Interactions. International Journal of Molecular Sciences 2023, 24 (18) , 13846. https://doi.org/10.3390/ijms241813846
    24. Hedieh Shahpasand-Kroner, Ibrar Siddique, Ravinder Malik, Gabriel R. Linares, Magdalena I. Ivanova, Justin Ichida, Tatjana Weil, Jan Münch, Elsa Sanchez-Garcia, Frank-Gerrit Klärner, Thomas Schrader, Gal Bitan, . Molecular Tweezers: Supramolecular Hosts with Broad-Spectrum Biological Applications. Pharmacological Reviews 2023, 75 (2) , 263-308. https://doi.org/10.1124/pharmrev.122.000654
    25. Wesley J. Wagner, Michael L. Gross. Using mass spectrometry‐based methods to understand amyloid formation and inhibition of alpha‐synuclein and amyloid beta. Mass Spectrometry Reviews 2022, https://doi.org/10.1002/mas.21814
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    27. Adeola Shobo, Alexander Röntgen, Mark A. Hancock, Gerhard Multhaup. Biophysical characterization as a tool to predict amyloidogenic and toxic properties of amyloid‐β42 peptides. FEBS Letters 2022, 596 (11) , 1401-1411. https://doi.org/10.1002/1873-3468.14358
    28. Martyna M. Matuszyk, Claire J. Garwood, Laura Ferraiuolo, Julie E. Simpson, Rosemary A. Staniforth, Stephen B. Wharton. Biological and methodological complexities of beta‐amyloid peptide: Implications for Alzheimer’s disease research. Journal of Neurochemistry 2022, 160 (4) , 434-453. https://doi.org/10.1111/jnc.15538
    29. Faisal Abedin, Nabin Kandel, Suren A. Tatulian. Effects of Aβ-derived peptide fragments on fibrillogenesis of Aβ. Scientific Reports 2021, 11 (1) https://doi.org/10.1038/s41598-021-98644-y
    30. Akshay Kapadia, Krishna K. Sharma, Indresh Kumar Maurya, Varinder Singh, Madhu Khullar, Rahul Jain. Structural and mechanistic insights into the inhibition of amyloid-β aggregation by Aβ39-42 fragment derived synthetic peptides. European Journal of Medicinal Chemistry 2021, 212 , 113126. https://doi.org/10.1016/j.ejmech.2020.113126
    31. Ke Wang, Liu Na, Mojie Duan. The Pathogenesis Mechanism, Structure Properties, Potential Drugs and Therapeutic Nanoparticles against the Small Oligomers of Amyloid-β. Current Topics in Medicinal Chemistry 2021, 21 (2) , 151-167. https://doi.org/10.2174/1568026620666200916123000
    32. Sarita Tripathi, Samridhi Pathak, Avinash Kale. Nanoparticles as Artificial Chaperons Suppressing Protein Aggregation: Remedy in Neurodegenerative Diseases. 2021, 311-338. https://doi.org/10.1007/978-3-030-61985-5_12
    33. Emma E. Cawood, Theodoros K. Karamanos, Andrew J. Wilson, Sheena E. Radford. Visualizing and trapping transient oligomers in amyloid assembly pathways. Biophysical Chemistry 2021, 268 , 106505. https://doi.org/10.1016/j.bpc.2020.106505
    34. Yanxian Zhang, Baiping Ren, Dong Zhang, Yonglan Liu, Mingzhen Zhang, Chao Zhao, Jie Zheng. Design principles and fundamental understanding of biosensors for amyloid-β detection. Journal of Materials Chemistry B 2020, 8 (29) , 6179-6196. https://doi.org/10.1039/D0TB00344A
    35. Akshay Kapadia, Aesan Patel, Krishna K. Sharma, Indresh Kumar Maurya, Varinder Singh, Madhu Khullar, Rahul Jain. Effect of C-terminus amidation of Aβ 39–42 fragment derived peptides as potential inhibitors of Aβ aggregation. RSC Advances 2020, 10 (45) , 27137-27151. https://doi.org/10.1039/D0RA04788K
    36. Nicolo Tonali, Veronica I. Dodero, Julia Kaffy, Loreen Hericks, Sandrine Ongeri, Norbert Sewald. Real‐Time BODIPY‐Binding Assay To Screen Inhibitors of the Early Oligomerization Process of Aβ1–42 Peptide. ChemBioChem 2020, 21 (8) , 1129-1135. https://doi.org/10.1002/cbic.201900652
    37. Serena Lazzaro, Nina Ogrinc, Lieke Lamont, Graziella Vecchio, Giuseppe Pappalardo, Ron M. A. Heeren. Ion mobility spectrometry combined with multivariate statistical analysis: revealing the effects of a drug candidate for Alzheimer’s disease on Aβ1-40 peptide early assembly. Analytical and Bioanalytical Chemistry 2019, 411 (24) , 6353-6363. https://doi.org/10.1007/s00216-019-02030-7
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    39. Huan Zhang, Xiaoyan Dong, Fufeng Liu, Jie Zheng, Yan Sun. Ac-LVFFARK-NH 2 conjugation to β-cyclodextrin exhibits significantly enhanced performance on inhibiting amyloid β-protein fibrillogenesis and cytotoxicity. Biophysical Chemistry 2018, 235 , 40-47. https://doi.org/10.1016/j.bpc.2018.02.002
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    41. Eric Y. Hayden, Kimberly K. Hoi, Jasmine Lopez, Mohammed Inayathullah, Margaret M. Condron, David B. Teplow. Identification of key regions and residues controlling Aβ folding and assembly. Scientific Reports 2017, 7 (1) https://doi.org/10.1038/s41598-017-10845-6
    42. Daniel J. Adams, Travis G. Nemkov, John P. Mayer, William M. Old, Michael H. B. Stowell, . Identification of the primary peptide contaminant that inhibits fibrillation and toxicity in synthetic amyloid-β42. PLOS ONE 2017, 12 (8) , e0182804. https://doi.org/10.1371/journal.pone.0182804
    43. Brigita Urbanc. Flexible N‐Termini of Amyloid β‐Protein Oligomers: A Link between Structure and Activity?. Israel Journal of Chemistry 2017, 57 (7-8) , 651-664. https://doi.org/10.1002/ijch.201600097
    44. Dimitri Brinet, François Gaie-Levrel, Vincent Delatour, Julia Kaffy, Sandrine Ongeri, Myriam Taverna. In vitro monitoring of amyloid β-peptide oligomerization by Electrospray differential mobility analysis: An alternative tool to evaluate Alzheimer's disease drug candidates. Talanta 2017, 165 , 84-91. https://doi.org/10.1016/j.talanta.2016.12.011
    45. Neng Xiong, Yanjiao Zhao, Xiaoyan Dong, Jie Zheng, Yan Sun. Design of a Molecular Hybrid of Dual Peptide Inhibitors Coupled on AuNPs for Enhanced Inhibition of Amyloid β‐Protein Aggregation and Cytotoxicity. Small 2017, 13 (13) https://doi.org/10.1002/smll.201601666
    46. Xu Han, Jiyong Park, Wei Wu, Andres Malagon, Lingyu Wang, Edgar Vargas, Athula Wikramanayake, K. N. Houk, Roger M. Leblanc. A resorcinarene for inhibition of Aβ fibrillation. Chemical Science 2017, 8 (3) , 2003-2009. https://doi.org/10.1039/C6SC04854D
    47. Jing Liu, Bin Yang, Jun Ke, Wenjia Li, Wen-Chen Suen. Antibody-Based Drugs and Approaches Against Amyloid-β Species for Alzheimer’s Disease Immunotherapy. Drugs & Aging 2016, 33 (10) , 685-697. https://doi.org/10.1007/s40266-016-0406-x
    48. F. Rahimi, H. Li, S. Sinha, G. Bitan. Modulators of Amyloid β-Protein (Aβ) Self-Assembly. 2016, 97-191. https://doi.org/10.1016/B978-0-12-802173-6.00006-X
    49. Prabir Khatua, Jaya C. Jose, Neelanjana Sengupta, Sanjoy Bandyopadhyay. Conformational features of the Aβ 42 peptide monomer and its interaction with the surrounding solvent. Physical Chemistry Chemical Physics 2016, 18 (43) , 30144-30159. https://doi.org/10.1039/C6CP04925G
    50. Javed Masood Khan, Mohd Shahnawaz Khan, Mohd Sajid Ali, Nasser Abdulatif Al-Shabib, Rizwan Hasan Khan. Cetyltrimethylammonium bromide (CTAB) promote amyloid fibril formation in carbohydrate binding protein (concanavalin A) at physiological pH. RSC Advances 2016, 6 (44) , 38100-38111. https://doi.org/10.1039/C6RA03707K
    51. Rosa Pujol-Pina, Sílvia Vilaprinyó-Pascual, Roberta Mazzucato, Annalisa Arcella, Marta Vilaseca, Modesto Orozco, Natàlia Carulla. SDS-PAGE analysis of Aβ oligomers is disserving research into Alzheimer´s disease: appealing for ESI-IM-MS. Scientific Reports 2015, 5 (1) https://doi.org/10.1038/srep14809
    52. Argyris Politis, Antoni J. Borysik. Assembling the pieces of macromolecular complexes: Hybrid structural biology approaches. PROTEOMICS 2015, 15 (16) , 2792-2803. https://doi.org/10.1002/pmic.201400507
    53. Payel Das, Brian Murray, Georges Belfort. Alzheimer’s Protective A2T Mutation Changes the Conformational Landscape of the Aβ1–42 Monomer Differently Than Does the A2V Mutation. Biophysical Journal 2015, 108 (3) , 738-747. https://doi.org/10.1016/j.bpj.2014.12.013
    54. Michael T. Bowers. Re-print of “Ion Mobility Spectrometry: A Personal View of its Development at UCSB”. International Journal of Mass Spectrometry 2015, 377 , 625-645. https://doi.org/10.1016/j.ijms.2014.08.017
    55. Ashley S. Phillips, Alexandre F. Gomes, Jason M. D. Kalapothakis, Jay E. Gillam, Jonas Gasparavicius, Fabio C. Gozzo, Tilo Kunath, Cait MacPhee, Perdita E. Barran. Conformational dynamics of α-synuclein: insights from mass spectrometry. The Analyst 2015, 140 (9) , 3070-3081. https://doi.org/10.1039/C4AN02306D
    56. Haiqiang Wu, Fang Zhang, Neil Williamson, Jie Jian, Liao Zhang, Zeqiu Liang, Jinyu Wang, Linkun An, Alan Tunnacliffe, Yizhi Zheng, . Effects of Secondary Metabolite Extract from Phomopsis occulta on β-Amyloid Aggregation. PLoS ONE 2014, 9 (10) , e109438. https://doi.org/10.1371/journal.pone.0109438
    57. Michael T. Bowers. Ion mobility spectrometry: A personal view of its development at UCSB. International Journal of Mass Spectrometry 2014, 370 , 75-95. https://doi.org/10.1016/j.ijms.2014.06.016
    58. Ewa Sitkiewicz, Marcin Kłoniecki, Jarosław Poznański, Wojciech Bal, Michał Dadlez. Factors Influencing Compact–Extended Structure Equilibrium in Oligomers of Aβ1–40 Peptide—An Ion Mobility Mass Spectrometry Study. Journal of Molecular Biology 2014, 426 (15) , 2871-2885. https://doi.org/10.1016/j.jmb.2014.05.015
    59. Ewa Sitkiewicz, Jacek Olędzki, Jarosław Poznański, Michał Dadlez, . Di-Tyrosine Cross-Link Decreases the Collisional Cross-Section of Aβ Peptide Dimers and Trimers in the Gas Phase: An Ion Mobility Study. PLoS ONE 2014, 9 (6) , e100200. https://doi.org/10.1371/journal.pone.0100200
    60. Francesco Lanucara, Stephen W. Holman, Christopher J. Gray, Claire E. Eyers. The power of ion mobility-mass spectrometry for structural characterization and the study of conformational dynamics. Nature Chemistry 2014, 6 (4) , 281-294. https://doi.org/10.1038/nchem.1889
    61. Leonid Breydo, Vladimir N. Uversky. Molecular Mechanisms of Protein Misfolding. 2014, 1-14. https://doi.org/10.1016/B978-0-12-394431-3.00001-8
    62. Hyunbum Jang, Fernando Teran Arce, Srinivasan Ramachandran, Bruce L. Kagan, Ratnesh Lal, Ruth Nussinov. Disordered amyloidogenic peptides may insert into the membrane and assemble into common cyclic structural motifs. Chem. Soc. Rev. 2014, 43 (19) , 6750-6764. https://doi.org/10.1039/C3CS60459D
    63. Xiaofang Shen, Xiaorong Deng, Yuehong Pang. Self-assembly of Cu(ii) with amyloid β19–20 peptide: relevant to Alzheimer's disease. RSC Advances 2014, 4 (42) , 21840. https://doi.org/10.1039/c4ra02758b
    64. Shuai Niu, Jessica N Rabuck, Brandon T Ruotolo. Ion mobility-mass spectrometry of intact protein–ligand complexes for pharmaceutical drug discovery and development. Current Opinion in Chemical Biology 2013, 17 (5) , 809-817. https://doi.org/10.1016/j.cbpa.2013.06.019
    65. Ying Zhang, Don L. Rempel, Jun Zhang, Anuj K. Sharma, Liviu M. Mirica, Michael L. Gross. Pulsed hydrogen–deuterium exchange mass spectrometry probes conformational changes in amyloid beta (Aβ) peptide aggregation. Proceedings of the National Academy of Sciences 2013, 110 (36) , 14604-14609. https://doi.org/10.1073/pnas.1309175110
    66. L.A. Woods, S.E. Radford, A.E. Ashcroft. Advances in ion mobility spectrometry–mass spectrometry reveal key insights into amyloid assembly. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 2013, 1834 (6) , 1257-1268. https://doi.org/10.1016/j.bbapap.2012.10.002
    67. A. Konijnenberg, A. Butterer, F. Sobott. Native ion mobility-mass spectrometry and related methods in structural biology. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 2013, 1834 (6) , 1239-1256. https://doi.org/10.1016/j.bbapap.2012.11.013
    68. Derya Meral, Brigita Urbanc. Discrete Molecular Dynamics Study of Oligomer Formation by N-Terminally Truncated Amyloid β-Protein. Journal of Molecular Biology 2013, 425 (12) , 2260-2275. https://doi.org/10.1016/j.jmb.2013.03.010
    69. Danielle M. Williams, Tara L. Pukala. Novel insights into protein misfolding diseases revealed by ion mobility‐mass spectrometry. Mass Spectrometry Reviews 2013, 32 (3) , 169-187. https://doi.org/10.1002/mas.21358
    70. Molly T. Soper, Alaina S. DeToma, Suk-Joon Hyung, Mi Hee Lim, Brandon T. Ruotolo. Amyloid-β–neuropeptide interactions assessed by ion mobility-mass spectrometry. Physical Chemistry Chemical Physics 2013, 15 (23) , 8952. https://doi.org/10.1039/c3cp50721a
    71. Tingyu Liu, Gal Bitan. Modulating Self‐Assembly of Amyloidogenic Proteins as a Therapeutic Approach for Neurodegenerative Diseases: Strategies and Mechanisms. ChemMedChem 2012, 7 (3) , 359-374. https://doi.org/10.1002/cmdc.201100585

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