Modified Amyloids

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CAT# Product Name M.W Molecular Formula Inquiry
A13012 Acetyl-beta-Amyloid (20-29), amide 1064.1 Inquiry
A13014 Beta-Amyloid (1-8)-Cys 1079.1 Inquiry
A13025 Cys-beta-Amyloid (25-35) 1163.4 Inquiry
A13037 Beta-Amyloid (1-9)-Gly-Gly-Cys 1250.3 Inquiry
A13040 Beta-Amyloid (1-10)-Cys 1299.4 Inquiry
A13053 Cys-beta-Amyloid (1-11) 1428.5 Inquiry
A13065 Beta-Amyloid P Component (27-38), amide 1494.8 Inquiry
A13071 Beta-Amyloid (1-12)-Cys--NH2 1526.6 Inquiry
A13072 Cys-beta-Amyloid (1-12) 1527.6 Inquiry
A13103 Beta-Amyloid (22-40)--NH2 1814.1 Inquiry
A13116 ch Beta-Amyloid (30-16) 1896.2 Inquiry
A13132 Beta-Amyloid (1-16)-Cys 2058.2 Inquiry
A13133 Beta-Amyloid (12-28)-Cys 2058.3 Inquiry
A13134 Cys-beta-Amyloid (12-28) 2058.3 Inquiry
A13136 Beta-Amyloid (13-29)-Gly-Cys 2073.3 Inquiry
A13144 Beta-Amyloid (1-17)-Cys 2171.3 Inquiry
A13150 Beta-Amyloid (1-40) Binding Peptide 2215.5 Inquiry
A13179 Beta-Amyloid (4-24)-Cys 2664.0 Inquiry
A13190 Beta-Amyloid (1-24)-Cys 2979.3 Inquiry
A13192 Anti-Parallel Topology beta-Amyloid Modified Peptide II 3014.4 Inquiry

Introduction

The pathology of Alzheimer’s disease is closely related to the processing of amyloid precursor protein (APP), resulting in the formation of a variety of amyloid-β (Aβ) peptides. They are found in insolent plaques as insoluble aggregates, a histopathological hallmark of the disease. These peptides are also present in the interstitial and cerebrospinal fluid in soluble, predominantly monomeric and dimeric forms. Due to the combination of several enzyme activities during APP processing, Aβ peptides are present in multiple isoforms with different N-terminus and C-terminus. These peptides include a portion of the proximal and transmembrane domains of APP. In addition to size differences, post-translational modifications of Aβ-including oxidation, phosphorylation, nitrification, racemization, isomerization, pyroglutamylation and glycosylation - produce excessive peptides with different physiological and pathological properties that can regulate disease progression.

Mechanism of action

Most AD cases were sporadic, while Aβ peptide production did not change. Thus, the propensity to form aggregates and toxic substances may be driven by factors other than those produced by certain Aβ peptides. Several post-translational modifications (PTM) have been discovered that generally increase the rate of aggregation of Aβ. Some of these modifications, such as oxidation and nitration, are apparently caused by the inflammatory environment of a component of AD. The most significant oxidative change site in Aβ is the 35-position (Met35) methionine. Increased oxidative stress has been described in the brains of patients with mild cognitive impairment and AD. PTMs can function as a molecular switch to evoke cellular responses, but one should consider that they may also be a result of protein aging that is random and without any physiological impact.

Application of Modified Amyloids

From too many Aβ species, some are produced very early in the APP process, some are modified immediately afterwards, or some are found or produced in some cells or extracellular compartments, and some are actually markers for the species’s slow to non-existent transformation. A polypeptide in an amyloid plaque. Certain Aβ regions contribute significantly to their properties, such as N-terminal truncations, and certain amino acids are hotspots for PTM. Some of these species may be excellent diagnostic markers or therapeutic targets in the future.

References

  1. Knowles, T. P., & Mezzenga, R. (2016). Amyloid fibrils as building blocks for natural and artificial functional materials. Advanced Materials, 28(31), 6546-6561.
  2. Soto, C., Estrada, L., & Castilla, J. (2006). Amyloids, prions and the inherent infectious nature of misfolded protein aggregates. Trends in biochemical sciences, 31(3), 150-155.
  3. Kummer, M. P., & Heneka, M. T. (2014). Truncated and modified amyloid-beta species. Alzheimer's research & therapy, 6(3), 28.
* Please kindly note that our products and services can only be used to support research purposes (Not for clinical use).
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