Beta-Amyloid (1-39) Peptide
- Cat.Number : AS-24295
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A number of Aß protein variants, differing only at their carboxy terminus (1-39, 1-40, 1-42 and 1-43), are identified as the major components of the cerebral amyloid deposits in Alzheimer’s disease. The length of the C-terminus is a critical determinant of the rate of amyloid formation (“kinetic solubility”), with only a minor effect on the thermodynamic solubility. Amyloid formation by the kinetically soluble peptides (e.g. 1-39) can be nucleated, or “seeded” by peptides which include the critical C-terminal residues (1-42, 26-42, 26-43, 34-42).
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Citations
Microchip electrophoresis profiling of Aβ peptides in the cerebrospinal fluid of patients with Alzheimer’s disease.
Anal Chem . 2010 Sep 15 ; 82(18) 7611 | DOI : 10.1021/ac101337n
- M. Reza
Beta-amyloid peptide blocks the fast-inactivating K+ current in rat hippocampal neurons.
Biophys J 70, 296. . 1996 Jan 01 ; 70(1) 296 | DOI : 10.1016/S0006-3495(96)79570-X
- TA. Good
Recognition sequence design for peptidyl modulators of beta-amyloid aggregation and toxicity.
Biochem . 1999 Mar 23 ; 38(12) 3570 | DOI : 10.1021/bi982119e
- MM. Pallitto
A strategy for designing inhibitors of β-amyloid toxicity.
J Biol Chem . 1996 Nov 22 ; 271(47) 29525 | DOI : 10.1074/jbc.271.47.29525
- J. Ghanta
References
Conformational Changes of the Amyloid β-Peptide (1–40) Adsorbed on Solid Surfaces
Macromol Biosci . 2005 May 23 ; 5(5) 401 | DOI : https://doi.org/10.1002/mabi.200400189
- CE. Giacomelli
- W. Norde
The carboxy terminus of the .beta. amyloid protein is critical for the seeding of amyloid formation: Implications for the pathogenesis of Alzheimer's disease
Biochem. . 1993 May 01 ; 32(18) 4693 | DOI : https://doi.org/10.1021/bi00069a001
- JT. Jarrett
- et al