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Water-Soluble Tripeptide A� (9-11) Forms Amyloid-Like Fibrils and Exhibits Neurotoxicity

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Title Water-Soluble Tripeptide A� (9-11) Forms Amyloid-Like Fibrils and Exhibits Neurotoxicity
 
Creator Naskar, Jishu
Drew, Michael G B
Deb, Ishani
Das, Sumantra
Banerjee, Arindam
 
Subject Chemistry
 
Description The aggregation of normally soluble proteins into wellordered amyloid fibrils is associated with a number of
diseases including Alzheimer’s disease, Parkinson’s disease,
type II diabetes, prion-related diseases, and others.1 Among
these diseases, Alzheimer’s disease (AD) is the most
prevalent and progressive neurodegenerative disease associated with deposition of �-sheet-rich protein aggregates in specific regions of the human brain as amyloid fibrils,2 which consist mainly of amyloid peptides like A�(1-40) and A�(1- 42).3 A� peptides are generated from highly regulated and sequential cleavage of the amyloid precursor protein (APP) by proteases designated as �- and γ-secretases and are readily detected in human CSF4 as a range of isoforms between 38 and 43 amino acids in length. They normally exist as soluble random coils. However, in a diseased condition they misfold
and form self-assembled oligomers which further selfassociate to form amyloid fibrils.5 The molecular structure of full-length A� fibrils is still not completely clear because of the difficulty of growing good quality crystals that can diffract well enough to obtain crystal structures.
 
Date 2008
 
Type Article
PeerReviewed
 
Format application/pdf
 
Identifier http://www.eprints.iicb.res.in/189/1/ORGANIC_LETTERS%2C_10(_13)%2C_2625%2D2628%2C2008[52].pdf
Naskar, Jishu and Drew, Michael G B and Deb, Ishani and Das, Sumantra and Banerjee, Arindam (2008) Water-Soluble Tripeptide A� (9-11) Forms Amyloid-Like Fibrils and Exhibits Neurotoxicity. Organic Letters, 10 (13). pp. 2625-2528.
 
Relation http://dx.doi.org/10.1021/ol8007217
http://www.eprints.iicb.res.in/189/