Peptides Composed of Alternating L- and D-Amino Acids Inhibit Amyloidogenesis in Three Distinct Amyloid Systems Independent of Sequence
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- 作者：Jackson Kellock1 ; Gene Hopping1 ; Byron Caughey2 ; Valerie Daggett1 ; daggett@uw.edu" class="auth_mail" title="E-mail the corresponding author
- 关键词：Aβ42 ; amyloid Beta (1&ndash ; 42) ; IAPP ; islet amyloid polypeptide ; NOESY ; nuclear Overhauser effect spectroscopy ; TTR ; transthyretin ; ThT ; Thioflavin T ; CR ; Congo red ; CD ; circular dichroism spectroscopy ; FTIR ; Fourier Transform Infrared ; HFIP ; hexafluoro &ndash ; 1 ; 1 ; 1 ; 3 ; 3 ; 3 &ndash ; isopropanol ; RT ; room temperature
- 刊名：Journal of Molecular Biology
- 出版年：2016
- 出版时间：5 June 2016
- 年：2016
- 卷：428
- 期：11
- 页码：2317-2328
- 全文大小：904 K
文摘
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Molecular dynamics simulations imply that the α-sheet structure is associated with toxic amyloid oligomers.
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Alternating Cα chirality through strands confers α-sheet structure to peptides.
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Peptides with alternating Cα chirality inhibit Aβ42, IAPP, and TTR aggregation.
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Inhibitor potency correlates with the stability of α-sheet secondary structure.
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Results identify new class of inhibitors against amyloidosis.