The mutations at specific positions lead to instability at E22P and L34P stalled the aggregation of the peptide

Alzheimer's disease is a neurodegenerative disease that affects memory loss and is unable to continue to stimulate the brain, is the most common cause of dementia elderly (65+) delayed and less common in childhood Response (65 years ago) early onset, is divided into two phases. The disease prevalence extension of time, loss of memory deterioration, which hindered every aspect of everyday life. Personality and behavior changes affect social interaction and social environment of the trouble. Stirring, extraction, as well as memory loss and skills are appropriate result in death due to other infections, such as pneumonia, malnutrition, common symptoms of early-onset cases account for less than 5% in. Gene responsible for the disease is APP, which provides instructions for the preparation of the brain and spinal cord of a protein called amyloid precursor protein. Although the researchers envision that it can be combined with each other and pathogenesis mechanism attached to the surface of cells or help other several proteins remains a mystery. Several enzymatic cleavage of amyloid precursor protein into two smaller fragments or peptide amyloid precursor protein (APP) and β-amyloid peptides, which are released into the cell. β-amyloid peptide is likely involved in neuronal change and adapts over time (plasticity) capabilities.

In the APP gene mutation is responsible for the same accounting more than 50 kinds of different types of mutations, leading to early and late onset of the disease, some of which will be discussed later. The most common mutations are V717I leading to β-amyloid accumulation in the brain and form clumps called amyloid plaques and thus release of 40, 42 residues of Aβ peptide β-amyloid peptide. Six APP gene mutations has been found to cause hereditary cerebral amyloid angiopathy and characterized stroke and intellectual function (dementia), which began in the middle of the fall adult conditions. Dutch type, the most common of all types, is replaced by the amino acid glutamine and glutamic acid protein sequence (Glu22Gln or E22Q) caused by the position 22. Italian style and also cause changes in the Arctic-type glutamic acid at position 22. In Italy type, glutamic acid is replaced with lysine (Glu22Lys or E22K), and type in the Arctic, the amino acid glycine, glutamic acid substitution (Glu22Gly or E22G ). Flemish type substitution from alanine amino acid glycine section 21 (Ala21Gly or A21G) caused. It is switched to the amino acid asparagine at position 23 (or Asp23Asn D23N) in Iowa type amino acid aspartic acid. Piedmont type of hereditary cerebral amyloid angiopathy is replaced by the amino acid leucine at amino acid valine (Leu34Val or L34V) position 34 caused. These mutations lead to aggregation and β-amyloid peptide (1-42) in the brain prone to deposition, the formation of clusters and thus is known as plaque buildup in blood vessels leading to dementia.

In the recent study, the mutations were reported using NAMD and their deviation (RMSD) of molecular dynamics simulation, analysis and use of chimeras generate plots. The mutation leads to the formation of β fibers (α- helix into β fold) use stability PASTA2.0 mutant peptides were predicted using mutation analysis tools as PolyPhen 2.0 and I-3.0 mutants compared analysis wild-type β-amyloid peptide.

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