184865-04-1

Basic information

• Product Name: AMYLOID BETA-PROTEIN (29-40)
• Synonyms: Amyloid β-Protein;AMyloid b-Protein (29-40)
• CAS NO: 184865-04-1
• Molecular Formula: C₄₉H₈₈N₁₂O₁₃S
• Molecular Weight: 1085.37
• Mol File: 184865-04-1.mol

Chemical Properties

• Appearance: /
• CAS DataBase Reference: AMYLOID BETA-PROTEIN (29-40)(CAS DataBase Reference)
• NIST Chemistry Reference: AMYLOID BETA-PROTEIN (29-40)(184865-04-1)
• EPA Substance Registry System: AMYLOID BETA-PROTEIN (29-40)(184865-04-1)

Safety Data

• Hazardous Substances Data: 184865-04-1(Hazardous Substances Data)

Upstream product

• 142825-10-3 R-sulforaphane 

Relevant articles and documents

Real-time evolution of Aβ40 metal-catalyzed oxidation reveals Asp1 as the main target and a dependence on metal binding site

Alzheimer's Disease (AD) is characterized by the deposition of amyloid plaques, mainly composed of aggregates of the Amyloid-β peptide (Aβ). There are evidences of oxidative damages on biomolecules and on Aβ in vivo, suggesting a link between oxidative stress and AD. The dyshomeostasis of redox-active metal ions observed in AD and in particular the ability of Cu ions to catalyze reactive oxygen species (ROS) production when bound to Aβ might contribute to the oxidative stress. In the present study, we have investigated by mass spectrometry (MS) the oxidative damages undergone by Aβ40 during the copper-catalyzed ROS production. N-terminal Asp1 was found to be the main target of ROS, along with His13 and His14, oxidized into oxo-histidine. As expected, the Met35 residue is also oxidized. The time evolution of Aβ40 oxidation indicates that the N-terminal part of the peptide, encompassing the main Cu binding sites, is the first target, the oxidation being stopped after several minutes. In contrast, the C-terminal one is regularly oxidized as a function of time although to a lesser extent.

Sulforaphane interaction with amyloid beta 1-40 peptide studied by electrospray ionization mass spectrometry

RATIONALE: Aggregation of amyloid beta 1-40 (Aβ) in the brain causes Alzheimer's disease (AD) and several small molecules are known to inhibit the aggregation process. Sulforaphane (SFN) is a natural isothiocyanate which is known to prevent various neurodegenerative processes. However, its interaction with Aβ is yet to be explored. Such studies could provide new mechanistic insights for its neuroprotective properties. METHODS: Liquid chromatography/electrospray ionization mass spectrometry (LC/ESI-MS) and in-source fragmentation experiments were performed on an Orbitrap mass spectrometer. The solution of Aβ and SFN was incubated and analyzed by mass spectrometry. Isotopic distribution patterns, accurate mass values and theoretical product ions were used to analyze the mass spectrometry data. The nature of binding of SFN and its binding sites with Aβ were evaluated by LC/MS and trypsin digestion experiments. RESULTS: ESI-MS analysis of the incubated solution of Aβ and SFN showed a 1:1 complex of [Aβ+SFN]. LC/MS analysis revealed that the solution contains three different [Aβ+SFN] complexes due to covalent binding of SFN to Aβ at three different sites. The in-source fragmentation experiments revealed that SFN is binding to free NH2 groups (N-terminal amino acid and lysines) in Aβ. Trypsin digestion experiments further confirmed the SFN binding sites in Aβ. CONCLUSIONS: The interaction of SFN, an anticancer agent, with Aβ was studied using ESI-MS. SFN is found to bind covalently and specifically with the free NH2 group of N-terminal aspartic acid and the ε-amino group of lysine at positions 16 and 28. Aggregation assay studies showed a lesser inclination of Aβ to aggregate when SFN is present. Hence the present study helps in understanding the mechanism of the action of SFN on the Aβ peptide. Copyright