1qxc › Citations

Solution structure of amyloid beta-peptide (25-35) in different media.

D'Ursi AM, Armenante MR, Guerrini R, Salvadori S, Sorrentino G, Picone D
J Med Chem 47 4231-8 (2004)
Related entries: 1qwp, 1qyt

Cited: 71 times
EuropePMC logo PMID: 15293994

Abstract

The design of molecules able to interact with the amyloid peptides either as inhibitors of fibril formation or as inhibitors of amyloid membrane pore formation represents one of the most relevant approaches in the development of anti-Alzheimer therapies. Abeta-(25-35), sequence GSNKGAIIGLM, is a highly toxic synthetic derivative of amyloid beta-peptides (Abeta-peptides), which forms fibrillary aggregates. Here, we report the NMR and CD investigation of Abeta-(25-35) in a membrane-mimicking environment and in isotropic mixtures of water and fluoro-alcohols to scan its conformational properties as a function of the medium. The analysis of the 3D structures in the mentioned conditions indicates a propensity of the peptide to behave as a typical transmembrane helix in the lipidic environment. In media characterized by different polarity, it loses the structural regularity at specific points of the sequence as a function of the environment. Furthermore, a comparison with the solution structure of full-length amyloid peptides suggests a role for the 25-27 kink region, which appears to be a general feature of all peptides under the solution conditions explored.

Reviews - 1qxc mentioned but not cited (1)

  1. Alzheimer's disease--a panorama glimpse. Zhao LN, Lu L, Chew LY, Mu Y. Int J Mol Sci 15 12631-12650 (2014)

Articles - 1qxc mentioned but not cited (6)

  1. The stability of monomeric intermediates controls amyloid formation: Abeta25-35 and its N27Q mutant. Ma B, Nussinov R. Biophys J 90 3365-3374 (2006)
  2. Amyloid β-peptide 25-35 self-assembly and its inhibition: a model undecapeptide system to gain atomistic and secondary structure details of the Alzheimer's disease process and treatment. Naldi M, Fiori J, Pistolozzi M, Drake AF, Bertucci C, Wu R, Mlynarczyk K, Filipek S, De Simone A, Andrisano V. ACS Chem Neurosci 3 952-962 (2012)
  3. Identifying Phlorofucofuroeckol-A as a Dual Inhibitor of Amyloid-β25-35 Self-Aggregation and Insulin Glycation: Elucidation of the Molecular Mechanism of Action. Seong SH, Paudel P, Jung HA, Choi JS. Mar Drugs 17 (2019)
  4. In silico and in vitro studies to elucidate the role of Cu2+ and galanthamine as the limiting step in the amyloid beta (1-42) fibrillation process. Hernández-Rodríguez M, Correa-Basurto J, Benitez-Cardoza CG, Resendiz-Albor AA, Rosales-Hernández MC. Protein Sci 22 1320-1335 (2013)
  5. ERp57 chaperon protein protects neuronal cells from Aβ-induced toxicity. Di Risola D, Ricci D, Marrocco I, Giamogante F, Grieco M, Francioso A, Vasco-Vidal A, Mancini P, Colotti G, Mosca L, Altieri F. J Neurochem 162 322-336 (2022)
  6. Structure-Activity Relationship of 5-mer Catalytides, GSGYR and RYGSG. Nakamura R, Akizawa T, Konishi M. Biomolecules 12 1766 (2022)


Reviews citing this publication (3)

  1. Amyloid beta: structure, biology and structure-based therapeutic development. Chen GF, Xu TH, Yan Y, Zhou YR, Jiang Y, Melcher K, Xu HE. Acta Pharmacol Sin 38 1205-1235 (2017)
  2. Nanoimaging for protein misfolding and related diseases. Lyubchenko YL, Sherman S, Shlyakhtenko LS, Uversky VN. J Cell Biochem 99 52-70 (2006)
  3. Insights into the Molecular Mechanisms of Alzheimer's and Parkinson's Diseases with Molecular Simulations: Understanding the Roles of Artificial and Pathological Missense Mutations in Intrinsically Disordered Proteins Related to Pathology. Coskuner-Weber O, Uversky VN. Int J Mol Sci 19 (2018)

Articles citing this publication (61)

  1. The alpha-to-beta conformational transition of Alzheimer's Abeta-(1-42) peptide in aqueous media is reversible: a step by step conformational analysis suggests the location of beta conformation seeding. Tomaselli S, Esposito V, Vangone P, van Nuland NA, Bonvin AM, Guerrini R, Tancredi T, Temussi PA, Picone D. Chembiochem 7 257-267 (2006)
  2. Effects of solvent on the structure of the Alzheimer amyloid-beta(25-35) peptide. Wei G, Shea JE. Biophys J 91 1638-1647 (2006)
  3. Quercetin and rutin exhibit antiamyloidogenic and fibril-disaggregating effects in vitro and potent antioxidant activity in APPswe cells. Jiménez-Aliaga K, Bermejo-Bescós P, Benedí J, Martín-Aragón S. Life Sci 89 939-945 (2011)
  4. The 'O-acyl isopeptide method' for the synthesis of difficult sequence-containing peptides: application to the synthesis of Alzheimer's disease-related amyloid beta peptide (Abeta) 1-42. Sohma Y, Hayashi Y, Kimura M, Chiyomori Y, Taniguchi A, Sasaki M, Kimura T, Kiso Y. J Pept Sci 11 441-451 (2005)
  5. Role of β-hairpin formation in aggregation: the self-assembly of the amyloid-β(25-35) peptide. Larini L, Shea JE. Biophys J 103 576-586 (2012)
  6. Structural diversity of dimers of the Alzheimer amyloid-beta(25-35) peptide and polymorphism of the resulting fibrils. Wei G, Jewett AI, Shea JE. Phys Chem Chem Phys 12 3622-3629 (2010)
  7. Characterizing amyloid-beta protein misfolding from molecular dynamics simulations with explicit water. Lee C, Ham S. J Comput Chem 32 349-355 (2011)
  8. Protective effects of erythropoietin on tau phosphorylation induced by beta-amyloid. Sun ZK, Yang HQ, Pan J, Zhen H, Wang ZQ, Chen SD, Ding JQ. J Neurosci Res 86 3018-3027 (2008)
  9. Amyloid-beta-anti-amyloid-beta complex structure reveals an extended conformation in the immunodominant B-cell epitope. Miles LA, Wun KS, Crespi GA, Fodero-Tavoletti MT, Galatis D, Bagley CJ, Beyreuther K, Masters CL, Cappai R, McKinstry WJ, Barnham KJ, Parker MW. J Mol Biol 377 181-192 (2008)
  10. Structural similarities and differences between amyloidogenic and non-amyloidogenic islet amyloid polypeptide (IAPP) sequences and implications for the dual physiological and pathological activities of these peptides. Wu C, Shea JE. PLoS Comput Biol 9 e1003211 (2013)
  11. Beta-amyloid peptide toxicity in organotypic hippocampal slice culture involves Akt/PKB, GSK-3beta, and PTEN. Nassif M, Hoppe J, Santin K, Frozza R, Zamin LL, Simão F, Horn AP, Salbego C. Neurochem Int 50 229-235 (2007)
  12. The interaction between amyloid-β peptides and anionic lipid membranes containing cholesterol and melatonin. Dies H, Toppozini L, Rheinstädter MC. PLoS One 9 e99124 (2014)
  13. Rapid aggregation and assembly in aqueous solution of A beta (25-35) peptide. Millucci L, Raggiaschi R, Franceschini D, Terstappen G, Santucci A. J Biosci 34 293-303 (2009)
  14. Peptide-lipid interactions: experiments and applications. Galdiero S, Falanga A, Cantisani M, Vitiello M, Morelli G, Galdiero M. Int J Mol Sci 14 18758-18789 (2013)
  15. The effect of Abeta conformation on the metal affinity and aggregation mechanism studied by circular dichroism spectroscopy. Chen YR, Huang HB, Chyan CL, Shiao MS, Lin TH, Chen YC. J Biochem 139 733-740 (2006)
  16. Effects of transmitters and amyloid-beta peptide on calcium signals in rat cortical astrocytes: Fura-2AM measurements and stochastic model simulations. Toivari E, Manninen T, Nahata AK, Jalonen TO, Linne ML. PLoS One 6 e17914 (2011)
  17. 'O-Acyl isopeptide method' for the efficient preparation of amyloid beta peptide 1-42 mutants. Sohma Y, Chiyomori Y, Kimura M, Fukao F, Taniguchi A, Hayashi Y, Kimura T, Kiso Y. Bioorg Med Chem 13 6167-6174 (2005)
  18. Controlled production of amyloid beta peptide from a photo-triggered, water-soluble precursor "click peptide". Taniguchi A, Skwarczynski M, Sohma Y, Okada T, Ikeda K, Prakash H, Mukai H, Hayashi Y, Kimura T, Hirota S, Matsuzaki K, Kiso Y. Chembiochem 9 3055-3065 (2008)
  19. Erythropoietin prevents PC12 cells from beta-amyloid-induced apoptosis via PI3K⁄Akt pathway. Zhi-Kun S, Hong-Qi Y, Zhi-Quan W, Jing P, Zhen H, Sheng-Di C. Transl Neurodegener 1 7 (2012)
  20. Structures of the glycine-rich diastereomeric peptides bombinin H2 and H4. Zangger K, Gössler R, Khatai L, Lohner K, Jilek A. Toxicon 52 246-254 (2008)
  21. Does tetracycline bind helix 2 of prion? An integrated spectroscopical and computational study of the interaction between the antibiotic and alpha helix 2 human prion protein fragments. Ronga L, Langella E, Palladino P, Marasco D, Tizzano B, Saviano M, Pedone C, Improta R, Ruvo M. Proteins 66 707-715 (2007)
  22. Exploring interaction of beta-amyloid segment (25-35) with membrane models through paramagnetic probes. Esposito C, Tedeschi A, Scrima M, D'errico G, Ottaviani MF, Rovero P, D'ursi AM. J Pept Sci 12 766-774 (2006)
  23. Structural and functional properties of peptides based on the N-terminus of HIV-1 gp41 and the C-terminus of the amyloid-beta protein. Gordon LM, Nisthal A, Lee AB, Eskandari S, Ruchala P, Jung CL, Waring AJ, Mobley PW. Biochim Biophys Acta 1778 2127-2137 (2008)
  24. Investigating the Neuroprotective Effects of Turmeric Extract: Structural Interactions of β-Amyloid Peptide with Single Curcuminoids. Randino R, Grimaldi M, Persico M, De Santis A, Cini E, Cabri W, Riva A, D'Errico G, Fattorusso C, D'Ursi AM, Rodriquez M. Sci Rep 6 38846 (2016)
  25. Structural determination of Abeta25-35 micelles by molecular dynamics simulations. Yu X, Wang Q, Zheng J. Biophys J 99 666-674 (2010)
  26. Aggregation of Aß(25-35) on DOPC and DOPC/DHA bilayers: an atomic force microscopy study. Sublimi Saponetti M, Grimaldi M, Scrima M, Albonetti C, Nori SL, Cucolo A, Bobba F, D'Ursi AM. PLoS One 9 e115780 (2014)
  27. Conformational stability of Abeta-(25-35) in the presence of thiazolidine derivatives. Campiglia P, Esposito C, Scrima M, Gomez-Monterrey I, Bertamino A, Grieco P, Novellino E, D'Ursi AM. Chem Biol Drug Des 69 111-118 (2007)
  28. Dynamics and orientation of a cationic antimicrobial peptide in two membrane-mimetic systems. Kosol S, Zangger K. J Struct Biol 170 172-179 (2010)
  29. Folding and membrane insertion of amyloid-beta (25-35) peptide and its mutants: implications for aggregation and neurotoxicity. Tsai HH, Lee JB, Tseng SS, Pan XA, Shih YC. Proteins 78 1909-1925 (2010)
  30. Gallotannins and Tannic Acid: First Chemical Syntheses and In Vitro Inhibitory Activity on Alzheimer's Amyloid β-Peptide Aggregation. Sylla T, Pouységu L, Da Costa G, Deffieux D, Monti JP, Quideau S. Angew Chem Int Ed Engl 54 8217-8221 (2015)
  31. How accurate are your simulations? Effects of confined aqueous volume and AMBER FF99SB and CHARMM22/CMAP force field parameters on structural ensembles of intrinsically disordered proteins: Amyloid-β42 in water. Weber OC, Uversky VN. Intrinsically Disord Proteins 5 e1377813 (2017)
  32. pH effects on the conformational preferences of amyloid beta-peptide (1-40) in HFIP aqueous solution by NMR spectroscopy. Valerio M, Porcelli F, Zbilut JP, Giuliani A, Manetti C, Conti F. ChemMedChem 3 833-843 (2008)
  33. Membrane-Accelerated Amyloid-β Aggregation and Formation of Cross-β Sheets. Khondker A, Alsop RJ, Rheinstädter MC. Membranes (Basel) 7 (2017)
  34. Location and conformation of amyloid β(25-35) peptide and its sequence-shuffled peptides within membranes: implications for aggregation and toxicity in PC12 cells. Tsai HH, Lee JB, Shih YC, Wan L, Shieh FK, Chen CY. ChemMedChem 9 1002-1011 (2014)
  35. Conformational features of the Aβ42 peptide monomer and its interaction with the surrounding solvent. Khatua P, Jose JC, Sengupta N, Bandyopadhyay S. Phys Chem Chem Phys 18 30144-30159 (2016)
  36. Fibril aggregation inhibitory activity of the beta-sheet breaker peptides: a molecular docking approach. Chini MG, Scrima M, D'Ursi AM, Bifulco G. J Pept Sci 15 229-234 (2009)
  37. On enhancers and inhibitors of elastin-derived amyloidogenesis. Bochicchio B, Lorusso M, Pepe A, Tamburro AM. Nanomedicine (Lond) 4 31-46 (2009)
  38. Conformational solution studies of the SDS micelle-bound 11-28 fragment of two Alzheimer's beta-amyloid variants (E22K and A21G) using CD, NMR, and MD techniques. Rodziewicz-Motowidło S, Juszczyk P, Kołodziejczyk AS, Sikorska E, Skwierawska A, Oleszczuk M, Grzonka Z. Biopolymers 87 23-39 (2007)
  39. Insights into the Effect of Curcumin and (-)-Epigallocatechin-3-Gallate on the Aggregation of Aβ(1-40) Monomers by Means of Molecular Dynamics. Tavanti F, Pedone A, Menziani MC. Int J Mol Sci 21 (2020)
  40. A new series of 1,3-dihidro-imidazo[1,5-c]thiazole-5,7-dione derivatives: synthesis and interaction with Abeta(25-35) amyloid peptide. Campiglia P, Scrima M, Grimaldi M, Cioffi G, Bertamino A, Sala M, Aquino C, Gomez-Monterrey I, Grieco P, Novellino E, D'Ursi AM. Chem Biol Drug Des 74 224-233 (2009)
  41. Hydrophobic tail length plays a pivotal role in amyloid beta (25-35) fibril-surfactant interactions. Bag S, Chaudhury S, Pramanik D, DasGupta S, Dasgupta S. Proteins 84 1213-1223 (2016)
  42. Spectroscopic investigation of Ginkgo biloba terpene trilactones and their interaction with amyloid peptide Abeta(25-35). He J, Petrovic AG, Dzyuba SV, Berova N, Nakanishi K, Polavarapu PL. Spectrochim Acta A Mol Biomol Spectrosc 69 1213-1222 (2008)
  43. Amyloid-β regulates gap junction protein connexin 43 trafficking in cultured primary astrocytes. Maulik M, Vasan L, Bose A, Dutta Chowdhury S, Sengupta N, Das Sarma J. J Biol Chem 295 15097-15111 (2020)
  44. Effect of the air-water interface on the conformation of amyloid beta. Samantray S, Cheung DL. Biointerphases 15 061011 (2020)
  45. Glucosyl Platinum(II) Complexes Inhibit Aggregation of the C-Terminal Region of the Aβ Peptide. La Manna S, Leone M, Iacobucci I, Annuziata A, Di Natale C, Lagreca E, Malfitano AM, Ruffo F, Merlino A, Monti M, Marasco D. Inorg Chem 61 3540-3552 (2022)
  46. Interactions between gold nanoparticles and amyloid β25-35 peptide. Peng J, Weng J, Ren L, Sun LP. IET Nanobiotechnol 8 295-303 (2014)
  47. Opposing Effects of Cucurbit[7]uril and 1,2,3,4,6-Penta-O-galloyl-β-d-glucopyranose on Amyloid β25-35 Assembly. de Almeida NE, Do TD, Tro M, LaPointe NE, Feinstein SC, Shea JE, Bowers MT. ACS Chem Neurosci 7 218-226 (2016)
  48. Site-specific structure of Aβ(25-35) peptide: isotope-assisted vibrational circular dichroism study. Shanmugam G, Polavarapu PL. Biochim Biophys Acta 1834 308-316 (2013)
  49. A soluble amyloid fibril segment to study aggregate formation. Jaroch S. ChemMedChem 2 47-49 (2007)
  50. Increase in the β-Sheet Character of an Amyloidogenic Peptide upon Adsorption onto Gold and Silver Surfaces. Soltani N, Gholami MR. Chemphyschem 18 526-536 (2017)
  51. NMR structure of the water soluble Aβ17-34 peptide. Fonar G, Samson AO. Biosci Rep 34 e00155 (2014)
  52. Neuroprotective Effect of 2-Aminoethoxydiphenyl Borate (2-APB) in Amyloid β-Induced Memory Dysfunction: A Mechanistic Study. Thapak P, Khare P, Bishnoi M, Sharma SS. Cell Mol Neurobiol 42 1211-1223 (2022)
  53. Use-dependent inhibition of glycine-activated chloride current in rat neurons by β-amyloid peptide pretreated with hexafluoroisopropanol. Solntseva EI, Bukanova JV. Neuroreport 28 579-583 (2017)
  54. Affected albumin endocytosis as a new neurotoxicity mechanism of amyloid beta. Rasgado LAV, Urbieta AT, Jiménez JMM. AIMS Neurosci 7 344-359 (2020)
  55. Amyloid β-Peptide Causes the Permanent Activation of CaMKIIα through Its Oxidation. Picón-Pagès P, Fanlo-Ucar H, Herrera-Fernández V, Ausellé-Bosch S, Galera-López L, Gutiérrez DA, Ozaita A, Álvarez AR, Oliva B, Muñoz FJ. Int J Mol Sci 23 15169 (2022)
  56. Effects of Aβ-derived peptide fragments on fibrillogenesis of Aβ. Abedin F, Kandel N, Tatulian SA. Sci Rep 11 19262 (2021)
  57. Epitope Mapping by NMR of a Novel Anti-Aβ Antibody (STAB-MAb). Posado-Fernández A, Afonso CF, Dória G, Flores O, Cabrita EJ. Sci Rep 9 12241 (2019)
  58. Modelling of interactions between Aβ(25-35) peptide and phospholipid bilayers: effects of cholesterol and lipid saturation. Ermilova I, Lyubartsev AP. RSC Adv 10 3902-3915 (2020)
  59. Monitoring the Conformational Changes of the Aβ(25-35) Peptide in SDS Micelles: A Matter of Time. Santoro A, Buonocore M, Grimaldi M, Napolitano E, D'Ursi AM. Int J Mol Sci 24 971 (2023)
  60. Scorpion venom heat-resistant peptide alleviates mitochondrial dynamics imbalance induced by PM2.5 exposure by downregulating the PGC-1α/SIRT3 signaling pathway. Huang L, Xu J, Duan K, Bao T, Cheng Y, Zhang H, Zhang Y, Lin Y, Li F. Toxicol Res (Camb) 12 756-764 (2023)
  61. Structural Analysis of a Trimer of β2-Microgloblin Fragment by Molecular Dynamics Simulations. Nishikawa N, Sakae Y, Gouda T, Tsujimura Y, Okamoto Y. Biophys J 116 781-790 (2019)


Quick links