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Information Seminar Paper

Title

MD SIMULATION OF A21G ALZHEIMER AMYLOID-BETA (Aβ) FIBRIL TOWARD A MOLECULAR MECHANISM FOR ITS PATHOGENICITY

Pages

 Start Page | End Page

Abstract

 ROLE OF AB1-42 FIBRIL AS A PART OF APPI PROTEIN IN ALZHEIMER DISEASEHAS BEEN CONFIRMED IN MANY WORKS. HOWEVER, THERE ARE DISCREPANCIES ON THE MOLECULAR MECHANISM OF THIS PHENOMENON. ON THE OTHER HAND, THERE ARE SOME INTRODUCED NATURAL VARIENTS WITH CONFIRMED EFFECT ON PATHOGENICITY OF ALZHEIMER WITHOUT INVESTIGATION ON THEIR MOLECULAR MECHANISMS. ONE OF THESE WELL CONFIRMED VARIENTS IS A692G (IN APPI) OR A21G (IN AB1-42) WHICH CAN CAUSE A FAMILIAL ALZHEIMER. WE USED AN AMBER FORCE FIELD VIA GROMACS PACKAGE TO DO MD SIMULATION OF AB17-42 FIBRIL BY 2BEG PDB STRUCTURE. RMSD ANALYSIS AND CALCULATION OF DISTANCES BETWEEN DIFFERENT MONOMERS IN 2BEG STRUCTURE ILLUSTRATE MORE STABILITY OF A21G MUTATION IN COMPARISON WITH WILD TYPE. WE ALSO ANALYZED ONE BY ONE RESIDUE DISTANCES TO FIND STRENGTH OF HYDROPHOBIC INTERACTION FOR EACH RESIDUE. FIRSTLY, STABILITY OF 2BEG STRUCTURE AS A WILD TYPE IN 17-42 PART OF AB FIBRIL WHICH DIDN’T HAVE MUCH PROMISED NUCLEATION SITE OF FIBRIL FOR MORE THAN 17 NS IS AN IMPLY THAT REST OF THE STRUCTURE HAS OTHER NUCLEATION SITES AND A21G MUTATION COULD CAUSE MORE STABILITY FOR A FIBRIL STRUCTURE WHILE ALANINE HAS A BIGGER HYDROPHOBICITY THAN GLYCINE.

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