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Amyloid Beta-Peptide (12-28) (human) Sale

(Synonyms: 淀粉-Β-蛋白片段12-28,Val-His-His-Gln-Lys-Leu-Val-Phe-Phe-Ala-Glu-Asp-Val-Gly-Ser-Asn-Lys ) 目录号 : GP10049

Amyloid Beta-Peptide (12-28)(人)是 Amyloid Beta 蛋白 (1-42) (Aβ (1-42)) 的肽片段。

Amyloid Beta-Peptide (12-28) (human) Chemical Structure

Cas No.:107015-83-8

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Sample solution is provided at 25 µL, 10mM.

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实验参考方法

Cell experiment [1]:

Cell lines

PC12 cells

Preparation Method

Two days after plating cell were treated with different concentrations of aged β12-28 peptide. After 22 h, MTT (5 mg/ml) was added and incubation was continued for a further2 h. Cells were lysed and after 24 h at 37°C, colorimetric determination of MTT reduction was made at 550 nm.

Reaction Conditions

0.001, 0.1, 10, 40 µM for 22 hours

Applications

Freshly pre-pared solutions of β12 - 28 were non-toxic as expected, while aged solutions produce generally significant decreases in the MTT mitochondrial reduction by PC12 cells.

References:

[1]: Rabanal, F., Tusell, J. M., Sastre, L., et al. (2002) Structural, kinetic and cytotox-icity aspects of 12-28 β amyloid protein fragment: A reappraisal. J. Pept. Sci. 8,578-588.

产品描述

Amyloid Beta-Peptide (12-28) (human) is a peptide fragment of amyloid beta protein (1-42) (Aβ (1-42)) [1]. One of the neuropathological features of Alzheimer's disease (AD) is the presence of amyloid deposits in senile plaques and in blood vessel walls [2]. Amyloid Beta-Peptide (12-28) was used as an internal standard [1].

Amyloid Beta-Peptide (12-28) (human) could efficiently suppress the formation of the α7nAChR.Aβ (1-42) complex. Using human brain tissues and cells that overexpress either the α7 nicotinic acetylcholine receptor (α7nAChR) or amyloid precursor protein as the starting material, Aβ (1-42) and α7nAChR can be co-immunoprecipitated by the respective specific antibodies, suggesting that they are tightly associated [3].

References:
[1]. Wang R, Sweeney D, Gandy SE, Sisodia, SS (1996) The profile of soluble amyloid b protein in cultured cell media. Detection and quantificaiton of amyloid β protein and variants by immunoprecipitation-mass spectrometry. J Biol Chem 271:31894-31902.
[2]. Terry R. D., and Davies P.(1983) Aging of the Brain (Samuel, D., Algeri, S.,Gershon ,S., Grimm, V., and Toffano, G., eds) Vol. 22, pp. 47-59, Raven Press
[3]. Wang, H. Y. et al. β-Amyloid1-42 binds to α7 nicotinic acetylcholine receptor with high affinity. Implications for Alzheimer's disease pathology. J. Biol. Chem. 275, 5626-5632 (2000).

Amyloid Beta-Peptide (12-28)(人)是 Amyloid Beta 蛋白 (1-42) (Aβ (1-42)) [1] 的肽片段。阿尔茨海默病 (AD) 的神经病理学特征之一是老年斑和血管壁中存在淀粉样沉积物 [2]。 Amyloid Beta-Peptide (12-28) 用作内标[1]

Amyloid Beta-Peptide (12-28)(人)可有效抑制 α7nAChR.Aβ (1-42) 复合物的形成。使用过表达 α7 烟碱乙酰胆碱受体 (α7nAChR) 或淀粉样蛋白前体蛋白的人脑组织和细胞作为起始材料,Aβ (1-42) 和 α7nAChR 可以通过各自的特异性抗体进行免疫共沉淀,表明它们紧密结合关联的[3]

Chemical Properties

Cas No. 107015-83-8 SDF
别名 淀粉-Β-蛋白片段12-28,Val-His-His-Gln-Lys-Leu-Val-Phe-Phe-Ala-Glu-Asp-Val-Gly-Ser-Asn-Lys
分子式 C89H135N25O25 分子量 1955.2
溶解度 ≥ 195.5mg/mL in DMSO 储存条件 Desiccate at -20°C
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Research Update

Folding landscapes of the Alzheimer amyloid-beta(12-28) peptide

The energy landscape for folding of the 12-28 fragment of the Alzheimer amyloid beta (Abeta) peptide is characterized using replica-exchange molecular dynamics simulations with an all-atom peptide model and explicit solvent. At physiological temperatures, the peptide exists mostly as a collapsed random coil, populating a small fraction (less than 10%) of hairpins with a beta-turn at position V18F19, with another 10% of hairpin-like conformations possessing a bend rather than a turn in the central VFFA positions. A small fraction of the populated states, approximately 14%, adopt polyproline II (PPII) conformations. Folding of the structured hairpin states proceeds through the assembly of two locally stable segments, VFFAE and EDVGS. The interactions stabilizing these locally folded structural motifs are in conflict with those stabilizing the global fold of A12-28, a signature of underlying residual frustration in this peptide. At increased temperature, the population of both beta-strand and PPII conformations diminishes in favor of beta-turn and random-coil states. On the basis of the conformational preferences of Abeta 12-28 monomers, two models for the molecular structure of amyloid fibrils formed by this peptide are proposed.

Amyloid Beta Peptide VHHQ, KLVFF, and IIGLMVGGVV Domains Involved in Fibrilization: AFM and Electrochemical Characterization

The time-dependent structural modifications and oxidation behavior of specifically chosen five short amyloid beta (Aβ) peptides, Aβ1-16, Aβ1-28, Aβ10-20, Aβ12-28, and Aβ17-42, fragments of the complete human Aβ1-40 peptide, were investigated by atomic force microscopy (AFM) and voltammetry. The objective was to determine the influence of different Aβ domains (VHHQ that contains electroactive histidine H residues, KLVFF that is the peptide hydrophobic aggregation core, and IIGLMVGGVV that is the C-terminus hydrophobic region), and of Aβ peptide hydrophobicity, in the fibrilization mechanism. The short Aβ peptides absence of aggregation or the time-dependent aggregation mechanisms, at room temperature, in free chloride media, within the time window from 0 to 48 h, were established by AFM via changes in their adsorption morphology, and by differential pulse voltammetry, via modifications of the amino acid residues oxidation peak currents. The first oxidation peak was of tyrosine Y residue and the second peak was of histidine H and methionine M residues oxidation. A correlation between the presence of an intact highly hydrophobic KLVFF aggregation core and the time-dependent changes on the Aβ peptides aggregation was found. The hydrophobic C-terminal domain IIGLMVGGVV, present in the Aβ1-40 peptide, also contributed to accelerate the formation of Aβ1-40 peptide aggregates and fibrils.

Binding of human apolipoprotein E to synthetic amyloid beta peptide: isoform-specific effects and implications for late-onset Alzheimer disease

Apolipoprotein E (apoE), a plasma apolipoprotein that plays a central role in lipoprotein metabolism, is localized in the senile plaques, congophilic angiopathy, and neurofibrillary tangles of Alzheimer disease. Late-onset familial and sporadic Alzheimer disease patients have an increased frequency of one of the three common apoE alleles, epsilon 4, suggesting apoE4 is associated with increased susceptibility to disease. To follow up on this suggestion, we compared the binding of synthetic amyloid beta (beta/A4) peptide to purified apoE4 and apoE3, the most common isoform. Both isoforms bound synthetic beta/A4 peptide, the primary constituent of the plaque and angiopathy, forming a complex that resisted dissociation by boiling in SDS. Oxygen-mediated complex formation was implicated because binding was increased in oxygenated buffer, reduced in nitrogen-purged buffer, and prevented by reduction with dithiothreitol or 2-mercaptoethanol. Binding of beta/A4 peptide was saturable at 10(-4) M peptide and required residues 12-28. Examination of apoE fragments revealed that residues 244-272 are critical for complex formation. Both oxidized apoE4 and apoE3 bound beta/A4 peptide; however, binding to apoE4 was observed in minutes, whereas binding to apoE3 required hours. In addition, apoE4 did not bind beta/A4 peptide at pH < 6.6, whereas apoE3 bound beta/A4 peptide from pH 7.6 to 4.6. Together these results indicate differences in the two isoforms in complexing with the beta/A4 peptide. Binding of beta/A4 peptide by oxidized apoE may determine the sequestration or targeting of either apoE or beta/A4 peptide, and isoform-specific differences in apoE binding or oxidation may be involved in the pathogenesis of the intra- and extracellular lesions of Alzheimer disease.

Specific domains of beta-amyloid from Alzheimer plaque elicit neuron killing in human microglia

Alzheimer's disease (AD) is found to have striking brain inflammation characterized by clusters of reactive microglia that surround senile plaques. A recent study has shown that microglia placed in contact with isolated plaque fragments release neurotoxins. To explore further this process of immunoactivation in AD, we fractionated plaque proteins and tested for the ability to stimulate microglia. Three plaque-derived fractions, each containing full-length native A beta 1-40 or A beta 1-42 peptides, elicited neurotoxin release from microglia. Screening of various synthetic peptides (A beta 1-16, A beta 1-28, A beta 12-28, A beta 25-35, A beta 17-43, A beta 1-40, and A beta 1-42) confirmed that microglia killed neurons only after exposure to nanomolar concentrations of human A beta 1-40 or human A beta 1-42, whereas the rodent A beta 1-40 (5Arg-->Gly, 10Tyr-->Phe 13His-->Arg) was not active. These findings suggested that specific portions of human A beta were necessary for microglia-plaque interactions. When coupled to microspheres, N-terminal portions of human A beta (A beta 1-16, A beta 1-28, A beta 12-28) provided anchoring sites for microglial adherence whereas C-terminal regions did not. Although itself not toxic, the 10-16 domain of human A beta was necessary for both microglial binding and activation. Peptide blockade of microglia-plaque interactions that occur in AD might prevent the immune-driven injury to neurons.

Charge-based binding of complement component C1q to the Alzheimer amyloid beta-peptide

Activation of the classical pathway in Alzheimer's disease derives from the binding of the first protein, subcomponent C1q, to the amyloid beta-peptide (A beta). Analysis of the binding of C1q to A beta by competitive enzyme-linked immunosorbent assay shows that A beta fragments 1-16 and 1-28 but not 12-28 and 17-42 are capable of inhibiting the A beta/C1q interaction, implicating the A beta 1-11 region as the C1q binding site. Binding is also shown to be inhibited by conditions of high ionic strength, suggesting that charged side chains in the A beta 1-11 region are critical to the A beta/c1q interaction. Ultrastructural evidence of binding is provided by platinum replica electron microscopy. Along with a previous demonstration of the 14-26 region of the C1q A chain as the A beta binding site, these findings suggest that attractions between a negative charge cluster in A beta 1-11 and a positive charge cluster in C1qA14-26 mediate the binding of A beta and C1q.