131602-53-4 Usage
Description
AMYLOID BETA-PROTEIN (HUMAN, 25-35) TRIFLUOROACETATE, also known as Aβ25-35, is a fragment derived from the amyloid-β protein, which is a major component of senile plaques found in Alzheimer's disease (AD) in the brain. This fragment lacks the N-terminal domain and the metal binding site and is primarily generated by proteolytic cleavage of Aβ(1-40) peptides. Aβ25-35 has a β-sheet and β-turn structure, and it is associated with neurotoxicity, Alzheimer's disease induction, and apoptosis in various cell types.
Uses
Used in Pharmaceutical and Biomedical Research:
AMYLOID BETA-PROTEIN (HUMAN, 25-35) TRIFLUOROACETATE is used as a research tool for studying the mechanisms of Alzheimer's disease and related neurodegenerative conditions. It is particularly useful for investigating the effects of Aβ25-35 on cellular processes, such as apoptosis and neurotoxicity.
Used in Cortical Cultures:
In the field of neuroscience, AMYLOID BETA-PROTEIN (HUMAN, 25-35) TRIFLUOROACETATE is used as an inducer of neurotoxicity in cortical cultures. This application helps researchers understand the cellular and molecular mechanisms underlying the neurotoxic effects of Aβ25-35 and its role in Alzheimer's disease.
Used in Rat Models:
AMYLOID BETA-PROTEIN (HUMAN, 25-35) TRIFLUOROACETATE is used as an inducer of Alzheimer's disease in rat models. This application allows researchers to study the progression of the disease and test potential therapeutic interventions in a controlled animal model.
Used in Mesenchymal Stem Cells (MSCs):
In the field of stem cell research, AMYLOID BETA-PROTEIN (HUMAN, 25-35) TRIFLUOROACETATE is used as an inducer of apoptosis in mesenchymal stem cells (MSCs). This application helps researchers investigate the effects of Aβ25-35 on stem cell survival and its potential implications in the context of Alzheimer's disease and other neurodegenerative disorders.
Biological Activity
Amyloid β-peptide (25-35) (human) is a fragment of human amyloid β-peptide, functionally required for the neurotrophic and neurotoxic effects associated with Alzheimer's disease.
Biochem/physiol Actions
Amyloid β-Protein Fragment 25-35 (Aβ25-35) is involved in the pathogenesis of Alzheimer′s disease. Inhibitors of this transition may serve as a potential agent in managing Alzheimer′s disease. It is present in the subiculum and entorhinal cortex neurons of Alzheimer′s brain samples and inclusion-body myositis (IBM) muscle. It binds to receptors present in microglia and is capable of lipid membrane insertion. The functional domain sequence of Aβ comprising of sequence GSNKGAIIGLM elicits neurotrophic and neurotoxic effects. Aβ25-35 exhibits rapid aggregation and displays age dependant neurotoxicity.
Mechanism of action
Amyloid β (Aβ) peptide is a proven major contributing component of neuritic plaques of Alzheimer's disease (AD) . The formation of fibrillar deposits of Aβ peptide in brain is a key step in the pathogenesis of this disease, since the conversion of Aβ from soluble monomer to insoluble fibril is considered to cause the neuronal degeneration and clinical dementia in AD patients. Recent biophysical studies such as electron microscopy, solid-state NMR, Fourier transform infrared (FTIR), and electronic circular dichroism (ECD) spectra indicated that the Aβ fibrils exhibit a high β-sheet content. The conversion of normal Aβ peptides with water-soluble α-helical/random coil structures into the insoluble Aβ aggregates with an extensive β-sheet content is considered to be the predominant event in the onset of AD.
Check Digit Verification of cas no
The CAS Registry Mumber 131602-53-4 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 1,3,1,6,0 and 2 respectively; the second part has 2 digits, 5 and 3 respectively.
Calculate Digit Verification of CAS Registry Number 131602-53:
(8*1)+(7*3)+(6*1)+(5*6)+(4*0)+(3*2)+(2*5)+(1*3)=84
84 % 10 = 4
So 131602-53-4 is a valid CAS Registry Number.
InChI:InChI=1/C45H81N13O14S/c1-9-24(5)36(43(69)50-21-35(63)52-29(17-23(3)4)40(66)55-28(45(71)72)14-16-73-8)58-44(70)37(25(6)10-2)57-38(64)26(7)51-34(62)20-49-39(65)27(13-11-12-15-46)54-41(67)30(18-32(48)60)56-42(68)31(22-59)53-33(61)19-47/h23-31,36-37,59H,9-22,46-47H2,1-8H3,(H2,48,60)(H,49,65)(H,50,69)(H,51,62)(H,52,63)(H,53,61)(H,54,67)(H,55,66)(H,56,68)(H,57,64)(H,58,70)(H,71,72)/t24-,25-,26-,27-,28-,29-,30-,31-,36-,37-/m0/s1
131602-53-4Relevant articles and documents
Solution structure of amyloid β-peptide (25-35) in different media
D'Ursi, Anna M.,Armenante, Maria R.,Guerrini, Remo,Salvadori, Severo,Sorrentino, Giuseppe,Picone, Delia
, p. 4231 - 4238 (2004)
The design of molecules able to interact with the amyloid peptides either as inhibitors of fibril formation or as inhibitors of amyloid membrane pore formation represents one of the most relevant approaches in the development of anti-Alzheimer therapies. Aβ-(25-35), sequence GSNKGAIIGLM, is a highly toxic synthetic derivative of amyloid β-peptides (Aβ-peptides), which forms fibrillary aggregates. Here, we report the NMR and CD investigation of Aβ-(25-35) in a membrane-mimicking environment and in isotropic mixtures of water and fluoroalcohols to scan its conformational properties as a function of the medium. The analysis of the 3D structures in the mentioned conditions indicates a propensity of the peptide to behave as a typical transmembrane helix in the lipidic environment. In media characterized by different polarity, it loses the structural regularity at specific points of the sequence as a function of the environment. Furthermore, a comparison with the solution structure of full-length amyloid peptides suggests a role for the 25-27 kink region, which appears to be a general feature of all peptides under the solution conditions explored.
Synthesis of chemically-tethered amyloid-β segment trimer possessing amyloidogenic properties
Shinoda, Kiyomichi,Sohma, Youhei,Kanai, Motomu
supporting information, p. 2976 - 2979 (2015/06/22)
As amyloid-β (Aβ) undergoes dynamic aggregation, it is impossible to isolate ('hook') the transient Aβ oligomer in an assembly state-pure form (e.g., sole Aβ dimer, trimer, tetramer, etc.). Obtaining such a pure Aβ oligomer would allow us to establish an in vitro system to perform a more detailed investigation of the pathogenic properties of the oligomer. A chemically-tethered Aβ oligomer, constructed only by covalent bonds, could satisfy this demand. Here we designed a chemically-tethered trimer of a pathogenic Aβ fragment (Aβ25-35) (1) and successfully generated it in situ from its precursor (4), a water-soluble and non-aggregative O-acyl isopeptide of 1, in neutral aqueous media. Chemically-tethered 1 possessed stronger amyloidogenic properties, that is, potential for β-sheet structure, fibril formation, and cytotoxicity, than the corresponding monomer Aβ25-35 (6). Trimerization of Aβ25-35 sequence might affect both the aggregative properties and cytotoxicity, based on the present results. This work opens the door for chemical synthesis of oligomers bigger than trimers in an assembly state-pure form, allowing for identification of the most toxic Aβ oligomer.