Amyloid β-Protein (1-16) trifluoroacetate salt

Modify Date: 2024-01-06 07:24:30

Amyloid β-Protein (1-16) trifluoroacetate salt Structure
Amyloid β-Protein (1-16) trifluoroacetate salt structure
Common Name Amyloid β-Protein (1-16) trifluoroacetate salt
CAS Number 131580-10-4 Molecular Weight 1955.04
Density 1.6±0.1 g/cm3 Boiling Point N/A
Molecular Formula C84H119N27O28 Melting Point N/A
MSDS N/A Flash Point N/A

 Use of Amyloid β-Protein (1-16) trifluoroacetate salt


β-Amyloid (1-16) is a β-Amyloid protein fragment involved in metal binding. Beta-amyloid is a peptide that forms amyloid plaques in the brains of Alzheimer's disease (AD) patients.

 Names

Name β-Amyloid 1-16
Synonym More Synonyms

  Biological Activity

Description β-Amyloid (1-16) is a β-Amyloid protein fragment involved in metal binding. Beta-amyloid is a peptide that forms amyloid plaques in the brains of Alzheimer's disease (AD) patients.
Related Catalog
Target

Amyloid-β[1]

In Vivo β-amyloid (1-16) fragment is considered as valid models to examine the contribution of the key histidine residues (His , His in mouse and His , His , His in human fragments) to the Ab–Cu2+ interaction. Oxidation targets for β-Amyloid (1-16) are the histidine residues coordinated to the metal ions. Copper is bound to Aβ in senile plaque of Alzheimer’s disease with β-Amyloid (1-16) taking part in the coordination of the Cu2+ ions. Cu2+ and Zn2+ are linked with the neurotoxicity of -Amyloid and free radical damage[1]. β-amyloid (1-16) is the minimal amino acidic sequence display a Cu coordination mode which involves three Histidines (His6, His13 and His14). β-amyloid (1-16) is supposed to be involved in metal binding[2]. Human β-amyloid interacts with zinc ions through its metal-binding domain 1-16. The C-tails of the two polypeptide chains of the rat Aβ(1-16) dimer are oriented in opposite directions to each other, which hinders the assembly of rat Aβ dimers into oligomeric aggregates. Thus, the differences in the structure of zinc-binding sites of human and rat β-Amyloid (1-16), their ability to form regular cross-monomer bonds, and the orientation of their hydrophobic C-tails could be responsible for the resistance of rats to Alzheimer's disease[3].
References

[1]. Kowalik-Jankowska T, et al. Coordination abilities of the 1-16 and 1-28 fragments of beta-amyloid peptide towards copper(II) ions: a combined potentiometric and spectroscopic study. J Inorg Biochem. 2003 Jul 1;95(4):270-82.

[2]. Minicozzi V, et al. Identifying the minimal copper- and zinc-binding site sequence in amyloid-beta peptides. J Biol Chem. 2008 Apr 18;283(16):10784-92.

[3]. Istrate AN, et al. NMR solution structure of rat aβ(1-16): toward understanding the mechanism of rats' resistance to Alzheimer's disease. Biophys J. 2012 Jan 4;102(1):136-43.

 Chemical & Physical Properties

Density 1.6±0.1 g/cm3
Molecular Formula C84H119N27O28
Molecular Weight 1955.04
Exact Mass 1953.871826
LogP -6.41
Index of Refraction 1.696
Storage condition -15°C
Water Solubility Soluble in water or aqueous buffer

 Synonyms

L-Lysine, L-α-aspartyl-L-alanyl-L-α-glutamyl-L-phenylalanyl-L-arginyl-L-histidyl-L-α-aspartyl-L-serylglycyl-L-tyrosyl-L-α-glutamyl-L-valyl-L-histidyl-L-histidyl-L-glutaminyl-
L-α-Aspartyl-L-alanyl-L-α-glutamyl-L-phenylalanyl-L-arginyl-L-histidyl-L-α-aspartyl-L-serylglycyl-L-tyrosyl-L-α-glutamyl-L-valyl-L-histidyl-L-histidyl-L-glutaminyl-L-lysine