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

IR@IICB: CSIR-Indian Institute of Chemical Biology, Kolkata

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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
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