Amyloid beta: structure, biology and structure-based …
2017年7月17日 · In this paper, we review the structures, biological functions, and neurotoxicity role of Aβ. We also discuss the potential receptors that interact with Aβ and mediate Aβ intake, clearance, and...
Amyloid beta - Wikipedia
Early NMR-derived models of a 26-aminoacid polypeptide from amyloid beta (Aβ 10–35) show a collapsed coil structure devoid of significant secondary structure content. [56] However, the most recent (2012) NMR structure of (Aβ 1-40) has significant secondary and tertiary structure. [ 1 ]
Amyloid beta: structure, biology and structure-based …
In this paper, we review the structures, biological functions, and neurotoxicity role of Aβ. We also discuss the potential receptors that interact with Aβ and mediate Aβ intake, clearance, and metabolism. Additionally, we summarize the therapeutic developments and recent advances of different strategies for treating Alzheimer's disease.
Solution structure of the Alzheimer's disease amyloid beta
2002年9月6日 · The major components of neuritic plaques found in Alzheimer disease (AD) are peptides known as amyloid beta-peptides (Abeta), which derive from the proteolitic cleavage of the amyloid precursor proteins.
Different Aggregation Pathways and Structures for Aβ40 and Aβ42 ...
In this work, we study the detailed mechanism of different aggregation pathways for two types of Aβ and their related structures. Specifically, we visualized the aggregation process of Aβ40 and Aβ42 by using atomic force microscopy (AFM), which is able to image the small-scale proteins and protein assemblies such as oligomers and fibrils.
Cryo-EM structures of lipidic fibrils of amyloid-β (1-40)
2024年2月13日 · Here we present the cryo-electron microscopy (cryo-EM) structures of six lipidic Aβ40 fibrils that assemble from three filament folds, providing structural insights into fibril–lipid interactions.
RCSB PDB - 1BA4: THE SOLUTION STRUCTURE OF AMYLOID BETA-PEPTIDE (1-40 ...
1998年4月7日 · The three-dimensional solution structure of the 40 residue amyloid beta-peptide, Abeta(1-40), has been determined using NMR spectroscopy at pH 5.1, in aqueous sodium dodecyl sulfate (SDS) micelles. In this environment, which simulates to some extent a water-membrane medium, the peptide is unstructured between residues 1 and 14 which are mainly ...
Human beta-amyloid peptide (1-40) | C194H295N53O58S
Human beta-amyloid peptide (1-40) | C194H295N53O58S | CID 57339250 - structure, chemical names, physical and chemical properties, classification, patents, literature, biological activities, safety/hazards/toxicity information, supplier lists, and more.
A Partially Folded Structure of Amyloid-Beta(1-40) in an …
2011年7月7日 · While previous studies commonly show the Aβ 1-40 is largely unstructured in solution, we show that Aβ 1-40 can adopt a compact, partially folded structure. In this structure, the central hydrophobic region of the peptide forms a 3 10 helix from H13 to D23 and the N- and C-termini collapse against the helix due to the clustering of hydrophobic ...
RCSB PDB - 2LFM: A partially folded structure of amyloid-beta(1 40…
2011年7月6日 · Aggregation of the Aβ (1-40) peptide is linked to the development of extracellular plaques characteristic of Alzheimer's disease. While previous studies commonly show the Aβ (1-40) is largely unstructured in solution, we show that Aβ (1-40) can adopt a compact, partially folded structure.