scholarly journals Protection against amyloid beta-peptide (1–42)-induced loss of phospholipid asymmetry in synaptosomal membranes by tricyclodecan-9-xanthogenate (D609) and ferulic acid ethyl ester: Implications for Alzheimer's disease

2005 ◽  
Vol 1741 (1-2) ◽  
pp. 140-148 ◽  
Author(s):  
Hafiz Mohmmad Abdul ◽  
D. Allan Butterfield
Keyword(s):  
Alzheimer’S Disease ◽  
Ferulic Acid ◽  
Ethyl Ester ◽  
Amyloid Beta ◽  
Acid Ethyl Ester ◽  
Amyloid Beta Peptide ◽  
Synaptosomal Membranes ◽  
Phospholipid Asymmetry ◽  
Beta Peptide ◽  
Ferulic Acid Ethyl Ester

In vivo protective effects of ferulic acid ethyl ester against amyloid-beta peptide 1–42-induced oxidative stress

2006 ◽  
Vol 84 (2) ◽  
pp. 418-426 ◽  
Author(s):  
Marzia Perluigi ◽  
Gururaj Joshi ◽  
Rukhsana Sultana ◽  
Vittorio Calabrese ◽  
Carlo De Marco ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Ferulic Acid ◽  
Ethyl Ester ◽  
Amyloid Beta ◽  
Acid Ethyl Ester ◽  
Amyloid Beta Peptide ◽  
Protective Effects ◽  
Beta Peptide ◽  
Ferulic Acid Ethyl Ester

Detecting bioactive amyloid beta peptide species in Alzheimer's disease

2004 ◽  
Vol 91 (3) ◽  
pp. 648-656 ◽  
Author(s):  
Yuanbin Liu ◽  
Richard Dargusch ◽  
Cindy Banh ◽  
Carol A. Miller ◽  
David Schubert
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Amyloid Beta ◽  
Amyloid Beta Peptide ◽  
Beta Peptide

Molecular dynamics studies of a β-sheet blocking peptide with the full-length amyloid beta peptide of Alzheimer’s disease

2016 ◽  
Vol 94 (10) ◽  
pp. 833-841 ◽  
Author(s):  
Zohreh Amini ◽  
Mohammad Hossein Fatemi ◽  
Arvi Rauk
Keyword(s):  
Alzheimer’S Disease ◽  
Molecular Dynamics ◽  
Amyloid Beta ◽  
Recognition Site ◽  
Full Length ◽  
The Self ◽  
Amyloid Beta Peptide ◽  
Self Recognition ◽  
Beta Peptide ◽  
Β Sheet

The region encompassing residues 13–23 of the amyloid beta peptide (Aβ(13–23)) of Alzheimer’s disease is the self-recognition site that initiates toxic oligomerization and fibrillization. A number of pseudopeptides have been designed to bind to Aβ(13–23) and been computationally shown to do so with high affinity. More interactions are available in full-length Aβ than are available in the shorter peptide. We describe herein a study by molecular dynamics (MD) of nine distinct complexes formed by one such pseudopeptide, SGA1, with full-length beta amyloid, Aβ(1–42). The relative stabilities of the Aβ–SGA1 complexes were estimated by a combination of MD and ab initio methods. The most stable complex, designated AB1, was found to be one in which SGA1 is bound to the self-recognition site of Aβ(1–42) in an antiparallel β-sheet fashion. Another complex, designated AB3, also involved SGA1 binding to the self-recognition region of Aβ(1–42), albeit with lower affinity. In both AB1 and AB3, SGA1 formed antiparallel β-sheets but to opposite edges of Aβ. A complex, AB4, with similar stability to AB3, was found with a parallel β-sheet in the self-recognition site. A fourth complex, AB7, also with similar stability, formed a parallel β-sheet in the hydrophobic central region of Aβ. In all cases, complexation of SGA1 induced extensive β-sheet structure in Aβ(1–42).

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