The membrane-active amphibian peptide caerin 1.8 inhibits fibril formation of amyloid β1-42
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- 作者：Yanqin Liua ; Tianfang Wangb ; Antonio N. Calabresea ; John A. Carverc ; Scott F. Cumminsb ; John H. Bowiea ; john.bowie@adelaide.edu.au" class="auth_mail" title="E-mail the corresponding author
- 关键词：Aβ42 ; Amyloid β1-42 peptide ; AD ; Alzheimer&rsquo ; s disease ; APP ; Amyloid precursor protein ; HPLC ; High performance liquid chromatography ; IC50 ; Half maximal inhibitory concentration ; MALDI ; Mass analysed laser desorption ionization ; MD ; Molecular dynamics ; MS ; Mass spectrometry ; PBS ; Phosphate buffered saline ; ThT ; Thioflavin T ; TOF ; Time of flight
- 刊名：Peptides
- 出版年：2015
- 出版时间：November 2015
- 年：2015
- 卷：73
- 期：Complete
- 页码：1-6
- 全文大小：1266 K
文摘
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The amphibian peptide caerin 1.8 [1GLFKVLGSV10AKHLLPHVVP20VIAEKL(NH2)], and some truncated derivatives (e.g. caerin 1.8 (1–13) [1GLFKVLGSV10AKHL(NH2)] and caerin 1.8 (22–25) [KVLGSV10AKHLLPHVVP20VIAEKL(NH2)], inhibit fibril formation from amyloid β 1-42 peptide (Aβ42).
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MALDI MS shows formation of a protonated caerin 1.8/Aβ42 (1:1) complex.
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Molecular modeling provides the structure of a weakly-bound caerin 1.8/Aβ42 (1:1) complex in water, in which the 16KLVF20F region of the bound Aβ42 is partially blocked from addition of a further Aβ42 molecule.