Abstract

Self-assembly of phenylalanine creates Phe fibers which is the characteristic fiber model found in amyloid fibrils linked with various neurodegenerative diseases. L-Isoleucyl-L-Phenylalanine (IlePhe) dipeptide is composed of isoleucine and phenylalanine amino acids, having fibrillary structure similar to nanotube forms of the core recognition motif of Alzheimer's β-amyloid polypeptide. The integrated coordination of neuronal responses via the PI3-K / Akt pathway has a significant functional impact on Alzheimer's disease. Exposure to Aβ in neuronal cultures leads to deterioration of PI3-K, Akt and mTOR signaling, which may cause cognitive loss during disease. Modulation of PI3-K, Akt and mTOR signal activity need aim to reduce or eliminate the accumulation of potential neurotoxins. The therapeutic approaches aimed to normalize neuronal responses on these pathways or activation of PI3-kinase have a protective effect against cognitive decline in animal models of Alzheimer disease. This study aims to determine the interaction of PI3-kinase with Ile-Phe dipeptide having amyloid fibril structure by three-dimensional simulation techniques such as molecular dynamics (with the GROMACS program) and molecular docking techniques (Schrodinger Software program).