1hz3 Citations

The Alzheimer's peptide a beta adopts a collapsed coil structure in water.

J Struct Biol 130 130-41 (2000)
Cited: 179 times
EuropePMC logo PMID: 10940221

Abstract

The self-assembly of the soluble peptide Abeta into Alzheimer's disease amyloid is believed to involve a conformational change. Hence the solution conformation of Abeta is of significant interest. In contrast to studies in other solvents, in water Abeta is collapsed into a compact series of loops, strands, and turns and has no alpha-helical or beta-sheet structure. Conformational stabilization is primarily attributed to van der Waals and electrostatic forces. A large conspicuous uninterrupted hydrophobic patch covers approximately 25% of the surface. The compact coil structure appears meta-stable, and because fibrillization leads to formation of intermolecular beta-sheet secondary structure, a global conformational rearrangement is highly likely. A molecular hypothesis for amyloidosis includes at least two primary driving forces, changes in solvation thermodynamics during formation of amyloid deposits and relief of internal conformational stress within the soluble precursor during formation of lower-energy amyloid fibrils.

Reviews - 1hz3 mentioned but not cited (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. Probing protein aggregation using discrete molecular dynamics. Sharma S, Ding F, Dokholyan NV. Front Biosci 13 4795-4808 (2008)
  3. Alzheimer's disease--a panorama glimpse. Zhao LN, Lu L, Chew LY, Mu Y. Int J Mol Sci 15 12631-12650 (2014)

Articles - 1hz3 mentioned but not cited (16)



Reviews citing this publication (16)

  1. Amyloid β Protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies. Nasica-Labouze J, Nguyen PH, Sterpone F, Berthoumieu O, Buchete NV, Coté S, De Simone A, Doig AJ, Faller P, Garcia A, Laio A, Li MS, Melchionna S, Mousseau N, Mu Y, Paravastu A, Pasquali S, Rosenman DJ, Strodel B, Tarus B, Viles JH, Zhang T, Zhang T, Wang C, Derreumaux P. Chem Rev 115 3518-3563 (2015)
  2. The chemistry of Alzheimer's disease. Rauk A. Chem Soc Rev 38 2698-2715 (2009)
  3. Amyloid-beta aggregation. Finder VH, Glockshuber R. Neurodegener Dis 4 13-27 (2007)
  4. From Alzheimer to Huntington: why is a structural understanding so difficult? Temussi PA, Masino L, Pastore A. EMBO J 22 355-361 (2003)
  5. FTIR spectroscopic imaging of protein aggregation in living cells. Miller LM, Bourassa MW, Smith RJ. Biochim Biophys Acta 1828 2339-2346 (2013)
  6. Structure and function of amyloid in Alzheimer's disease. Morgan C, Colombres M, Nuñez MT, Inestrosa NC. Prog Neurobiol 74 323-349 (2004)
  7. Protein aggregation processes: In search of the mechanism. Frieden C. Protein Sci 16 2334-2344 (2007)
  8. Aβ42 and Aβ40: similarities and differences. Qiu T, Liu Q, Chen YX, Zhao YF, Li YM. J Pept Sci 21 522-529 (2015)
  9. Structure-function relationships of pre-fibrillar protein assemblies in Alzheimer's disease and related disorders. Rahimi F, Shanmugam A, Bitan G. Curr Alzheimer Res 5 319-341 (2008)
  10. Transient dynamics of Aβ contribute to toxicity in Alzheimer's disease. Hubin E, van Nuland NA, Broersen K, Pauwels K. Cell Mol Life Sci 71 3507-3521 (2014)
  11. The role of molecular simulations in the development of inhibitors of amyloid β-peptide aggregation for the treatment of Alzheimer's disease. Lemkul JA, Bevan DR. ACS Chem Neurosci 3 845-856 (2012)
  12. Disrupting self-assembly and toxicity of amyloidogenic protein oligomers by "molecular tweezers" - from the test tube to animal models. Attar A, Bitan G. Curr Pharm Des 20 2469-2483 (2014)
  13. 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 E336 (2018)
  14. The underexplored question of β-amyloid monomers. Copani A. Eur J Pharmacol 817 71-75 (2017)
  15. Implications of protein structure instability: from physiological to pathological secondary structure. Sukhanova A, Poly S, Shemetov A, Bronstein I, Nabiev I. Biopolymers 97 577-588 (2012)
  16. Structural biology of cell surface receptors implicated in Alzheimer's disease. Hermans SJ, Nero TL, Morton CJ, Gooi JH, Crespi GAN, Hancock NC, Gao C, Ishii K, Markulić J, Parker MW. Biophys Rev 14 233-255 (2022)

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