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Ordered and Disordered Segments of Amyloid?? Drive Sequential Steps of the Toxic Pathway

Penulis : Barun Kumar Maity [-]
Kontributor / Dosen Pembimbing :
  • Anand Kant Das, Simli Dey, Ullhas Kaarthi Moorthi
Jenis Koleksi : Jurnal elektronik
Penerbit : Lain-lain
Fakultas :
Subjek :
Kata Kunci : Intracellular amyloid beta, Amyloid beta fragment, Amyloid beta interactions, Alzheimer’s disease (AD), amyloid-membrane interaction, amyloid enantiomer
Sumber : American Chemical Society
Staf Input/Edit : Irwan Sofiyan   Irwan Sofiyan
File : 1 file
Tanggal Input : 21 Mar 2019

2019_EJRNL_PP_Barun_Kumar_Maity_1.pdf
Terbatas Irwan Sofiyan
» ITB

While the roles of intrinsically disordered protein domains in driving interprotein interactions are increasingly well-appreciated, the mechanism of toxicity of disease-causing disordered proteins remains poorly understood. A prime example is Alzheimer’s disease (AD) associated amyloid beta (A?). A? oligomers are highly toxic partially structured peptide assemblies with a distinct ordered region (residues ?10?40) and a shorter disordered region (residues ?1?9). Here, we investigate the role of this disordered domain and its relation to the ordered domain in the manifestation of toxicity through a set of A? fragments and stereoisomers designed for this purpose...

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