Alzheimer's disease: soluble oligomeric Abeta(1-40) peptide in membrane mimic environment from solution NMR and circular dichroism studies
- PMID: 15672549
- DOI: 10.1007/s11064-004-7035-1
Alzheimer's disease: soluble oligomeric Abeta(1-40) peptide in membrane mimic environment from solution NMR and circular dichroism studies
Abstract
Amyloid beta peptide (Abeta) is a small peptide present in normal cells and aggregated Abeta is the main constituent of the extracellular amyloid plaques found in Alzheimer's disease (AD) brain. Recent studies suggest that soluble Abeta oligomers are neurotoxic rather than amyloid fibrils found in amyloid plaques. This study using multidimensional NMR spectroscopy and circular dichroism (CD) provides the first direct evidence that alterations in membrane structure can trigger the conversion of soluble alpha-helical monomeric Abeta into oligomeric Abeta in a beta-sheet conformation.
Similar articles
-
Solution structure of the Alzheimer amyloid beta-peptide (1-42) in an apolar microenvironment. Similarity with a virus fusion domain.Eur J Biochem. 2002 Nov;269(22):5642-8. doi: 10.1046/j.1432-1033.2002.03271.x. Eur J Biochem. 2002. PMID: 12423364
-
Bacterial inclusion bodies of Alzheimer's disease β-amyloid peptides can be employed to study native-like aggregation intermediate states.Chembiochem. 2011 Feb 11;12(3):407-23. doi: 10.1002/cbic.201000602. Epub 2011 Jan 10. Chembiochem. 2011. PMID: 21290543
-
Two types of Alzheimer's beta-amyloid (1-40) peptide membrane interactions: aggregation preventing transmembrane anchoring versus accelerated surface fibril formation.J Mol Biol. 2004 Jan 23;335(4):1039-49. doi: 10.1016/j.jmb.2003.11.046. J Mol Biol. 2004. PMID: 14698298
-
Physicochemical characteristics of soluble oligomeric Abeta and their pathologic role in Alzheimer's disease.Neurol Res. 2005 Dec;27(8):869-81. doi: 10.1179/016164105X49436. Neurol Res. 2005. PMID: 16354549 Review.
-
Molecular simulation of the primary and secondary structures of the Abeta(1-42)-peptide of Alzheimer's disease.Med Res Rev. 1998 Nov;18(6):403-30. doi: 10.1002/(sici)1098-1128(199811)18:6<403::aid-med4>3.0.co;2-c. Med Res Rev. 1998. PMID: 9828040 Review.
Cited by
-
Measuring translational diffusion coefficients of peptides and proteins by PFG-NMR using band-selective RF pulses.Eur Biophys J. 2014 Jul;43(6-7):331-9. doi: 10.1007/s00249-014-0965-x. Epub 2014 May 14. Eur Biophys J. 2014. PMID: 24824112
-
Interactions of Amyloid-β with Membrane Proteins.Int J Mol Sci. 2021 Jun 4;22(11):6075. doi: 10.3390/ijms22116075. Int J Mol Sci. 2021. PMID: 34199915 Free PMC article. Review.
-
Self-assembling peptide and protein amyloids: from structure to tailored function in nanotechnology.Chem Soc Rev. 2017 Jul 31;46(15):4661-4708. doi: 10.1039/c6cs00542j. Chem Soc Rev. 2017. PMID: 28530745 Free PMC article. Review.
-
Mamma Mia, P-glycoprotein binds again.FEBS Lett. 2020 Dec;594(23):4076-4084. doi: 10.1002/1873-3468.13951. Epub 2020 Oct 20. FEBS Lett. 2020. PMID: 33022784 Free PMC article. Review.
-
β-Hairpin Alignment Alters Oligomer Formation in Aβ-Derived Peptides.Biochemistry. 2024 Jan 16;63(2):212-218. doi: 10.1021/acs.biochem.3c00526. Epub 2024 Jan 1. Biochemistry. 2024. PMID: 38163326 Free PMC article.
References
Publication types
MeSH terms
Substances
Grants and funding
LinkOut - more resources
Full Text Sources
Medical