| Identification | Back Directory | [Name]
Glycine, L-seryl-L-isoleucyl-L-arginyl-L-α-glutamyl-L-leucyl-L-α-glutamyl-L-alanyl-L-arginyl-L-isoleucyl-L-arginyl-L-α-glutamyl-L-leucyl-L-α-glutamyl-L-leucyl-L-arginyl-L-isoleucyl- | [CAS]
873582-78-6 | [Synonyms]
Glycine, L-seryl-L-isoleucyl-L-arginyl-L-α-glutamyl-L-leucyl-L-α-glutamyl-L-alanyl-L-arginyl-L-isoleucyl-L-arginyl-L-α-glutamyl-L-leucyl-L-α-glutamyl-L-leucyl-L-arginyl-L-isoleucyl- | [Molecular Formula]
C88H157N29O27 | [MOL File]
873582-78-6.mol | [Molecular Weight]
2053.37 |
| Chemical Properties | Back Directory | [density ]
1.44±0.1 g/cm3(Temp: 20 °C; Press: 760 Torr)(predicted) | [Sequence]
Ser-Ile-Arg-Glu-Leu-Glu-Ala-Arg-Ile-Arg-Glu-Leu-Glu-Leu-Arg-Ile-Gly |
| Hazard Information | Back Directory | [Uses]
CCβ is a simple 17-amino acid peptide designed in research. CCβ is able to mimic the conformational transition of proteins from α-helix to β-sheet, which is a key step in the aggregation of proteins associated with many diseases, such as Alzheimer's disease and prion disease. CCβ can be used to study diseases related to protein aggregation[1]. | [References]
[1] Ding F, et al. Direct observation of protein folding, aggregation, and a prion-like conformational conversion[J]. Journal of Biological Chemistry, 2005, 280(48): 40235-40240. DOI:10.1074/jbc.M506372200 |
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