Amyloid β-Protein (1-16) trifluoroacetate salt
Modify Date: 2024-01-06 07:24:30
Amyloid β-Protein (1-16) trifluoroacetate salt structure
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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 saltβ-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. |
| Name | β-Amyloid 1-16 |
|---|---|
| Synonym | More Synonyms |
| 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. |
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| 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 |
| 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 |
| 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 |