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.
Piperazine and DBU: A safer alternative for rapid and efficient Fmoc deprotection in solid phase peptide synthesis
Ralhan, Krittika,KrishnaKumar, V. Guru,Gupta, Sharad
, p. 104417 - 104425 (2015/12/24)
In Solid Phase Peptide Synthesis (SPPS), contamination with deletion sequences which often co-elute with the target peptide continues to be a major challenge as these impurities can significantly affect the target peptide's properties. Here, we report an efficient Fmoc-deprotection solution containing piperazine and DBU which can cause complete removal of the Fmoc group in less than a minute. This combination rivals piperidine in speediness as revealed by kinetic studies. We demonstrate the efficiency of the piperazine/DBU solution by synthesizing the polyAla stretch with a significant reduction of deletion products occurring due to partial Fmoc deprotection. We verify the utility of the deprotection solution by successfully synthesizing four aggregation prone difficult peptide sequences. We further demonstrate that this combination can also be used to synthesize aspartimide and epimerization prone sequences when supplemented with 1% formic acid and is compatible with 2-chlorotrityl chloride resin. We conclude that piperazine/DBU can be used as a safer and effective alternative to piperidine in Fmoc-SPPS.
