关于 "Cytoskeleton & Motor Proteins" 的结果81+ 个结果

Cerebral amyloid angiopathy (CAA) is a common finding in Alzheimer's disease in which amyloid-Aβ vascular deposits are featured in >80% of the cases. Mutations in the positions 21-23 (e.g. Dutch mutation E22Q) are primarily associated with CAA, although they manifest with strikingly different clinical phenotypes: cerebral hemorrhage or dementia. The Piedmont L34V Aβ mutant, located outside this hot spot, shows a similar hemorrhagic phenotype, albeit less aggressive than the widely studied Dutch variant.

All-D Aβ (1-42) exhibits similar properites as the all-L Aβ. The peptide forms ion channels in lipid bilayers.

Experiments using sub-peptides of Aβ42 revealed that the epitope identified by the antibody A8, as described by Ying and coworkers, lies within the 1-6 region of Aβ. The antibody displays high affinity for soluble Aβ42 oligomers in the molecular weight range of 16.5-25 kDa, and detected target antigen in brain sections from senescence-accelerated SAMP 8 mice. Amidated or acetylated and amidated forms of the sequence were used for example for quantitative structure retention relationships (QSRR) experiments. The latter could allow prediction of reversed-phase high-performance liquid chromatography (HPLC) retention of peptides, as reported by Kaliszan and coworkers.

Amyloid β-Protein (25-35) amide是β淀粉样蛋白（amyloid-β，Aβ）酰胺化的一种产物，其中β淀粉样蛋白的生成能力已被强烈降低。

Biotinyl-Amyloid β-Protein (1-40) 是一种 N 端标记的生物素化淀粉样蛋白 ß-(1-40) 肽。

H13R, a mutation in the metal-binding region of Abeta reduces its copper-mediated toxicity. The native rodent sequence containing an arginine at this position is more tolerant to metals than the human amyloid peptide.

The English (H6R) mutation of β-amyloid peptides accelerates fibrillation without increasing protofibril formation. Ono et al. showed that the English and Tottori mutations alter Abeta assembly at its earliest stages, monomer folding and oligomerization, and produce oligomers that are more toxic to cultured neuronal cells than are wild type oligomers. The exchange of His? by Arg influences the structure of the Cu(II) complex formed by Aβ peptides.

The Iowa (D23N) mutant of Aβ 40 considerably more rapidly assembles in solution to form fibrils than the WT Aβ sequence. These fibrils also show a different structure, which could be responsible for their increased toxicity.

The Tottori (D7N) mutation of β-amyloid peptides accelerates fibrillation without increasing protofibril formation. Ono et al. showed that the English and Tottori mutations alter Abeta assembly at its earliest stages, monomer folding and oligomerization, and produce oligomers that are more toxic to cultured neuronal cells than are wild type oligomers.

The G37D mutant does not show the aggregation behavior of WT Abeta42 nor its neurotoxicity.

Cys-Aβ1-40 can be easily and selectively modified, labeled, coupled to carriers e.g. by maleimide chemistry without affecting the sequences involved in fibril formation. The free mercapto moiety of the peptide adheres to gold surfaces.

Aβ40 S26C has been used for generating the covalently linked Aβ40 homodimer. Dimerization can be easily reverted by reducing the soluble dimer with thiols as β-mercaptoethanol. Aβ40 S26C is perfectly suited for labeling with fluorescent tags

This all-D peptide contains two retro-inverso peptide klvff motifs of KLVFF (H-3682) corresponding to amino acids 16 to 20 of amyloid β-protein. The tandem dimer retro-inverso peptide showed about a 100-fold higher binding affinity (Kd = 1.3 . 10?² µM) for amyloid β-protein (1-40) fibrils than KLVFF (Kd = 1.1 ± 0.3 µM). It was also found to be more effective in preventing ordered fibril formation than the parent peptide KLVFF as judged by its increased ability to inhibit thioflavin T binding to β-sheet structures.

The Osaka mutation was the first deletion-type mutation to be identified in APP and Aβ. The Aβ E22delta mutant is more resistant to degradation by two major Aβ-degrading enzymes, neprilysin and insulin-degrading enzyme. Synthetic mutant Aβ showed unusual aggregation properties with enhanced oligomerization but no fibrillization. It also inhibited hippocampal long-term potentiation more efficiently than wild-type Aβ. A transgenic mouse model containing APP with the E693delta mutation has been developed. APP(OSK)-Tg mice exhibit intraneuronal Aβ E22delta oligomers and memory impairment as early as eight months of age.

Transgenic mice expressing the vasculotropic Dutch/Iowa (E693Q/D694N) mutant human Aβ precursor protein in brain (Tg-SwDI) accumulate abundant cerebral microvascular fibrillar amyloid deposits and exhibit robust neuroinflammation. In vitro, the doubly mutated Aβ peptides showed an increased propensity to fibrillation and pathogenicity compared to the Dutch and Iowa single mutants.

Oxidation of Met35 attenuates the formation of Aβ40 oligomers.

(Met(O)³?)-Amyloid β-protein (1-42) (H-5888), in contrast to Aβ 1-42 (H-1368), has been shown to be non-toxic to 9-11 day-old rat embryonic hippocampal neuronal cultures and not to produce any protein oxidation. It has also been demonstrated that fibril formation is not affected by Met(O)³?. For the Nle analog see H-7308.

Sulfoxide of Aβ 25-35.

Maiti et al. could show that, in contrast to the sulfoxide of Aβ (1-42), the sulfone was as toxic and aggregated as fast as wild-type Aβ (1-42).

5-FAM-Amyloid β；-Protein (1-40) 是 FAM 荧光标记的 β；-Amyloid (1-40) 肽（&Lambda；ex=492nm 和 &Lambda；em=518nm）。