Modulation of A尾(1鈥?0) Peptide Fibrillar Architectures by A尾-Based Peptide Amphiphiles

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• 作者：Chengqian He ; Yuchun Han ; Linyi Zhu ; Manli Deng ; Yilin Wang
• 刊名：Journal of Physical Chemistry B
• 出版年：2013
• 出版时间：September 12, 2013
• 年：2013
• 卷：117
• 期：36
• 页码：10475-10483
• 全文大小：479K
• 年卷期：v.117,no.36(September 12, 2013)
• ISSN：1520-5207

文摘

Modulation of the fibrillogenesis of amyloid peptide A尾(1鈥?0) with two A尾-based peptide amphiphiles has been studied. Both peptide amphiphiles contain two alkyl chains but in different positions. The two alkyl chains of 2C₁₂鈥揂尾(11鈥?7) are attached to the same terminus of A尾(11鈥?7), while those of C₁₂鈥揂尾(11鈥?7)鈥揅₁₂ are separately attached to opposite termini of A尾(11鈥?7). Thioflavin T fluorescence spectroscopy shows that all the peptide amphiphiles promote the formation of the cross-尾-sheet structure of A尾(1鈥?0) and the aggregation of A尾(1鈥?0), while 2C₁₂鈥揂尾(11鈥?7) does this more efficiently. The atom force microscopy images indicate that the modulations of these two peptide amphiphiles on the A尾(1鈥?0) aggregation experience two distinct pathways. 2C₁₂鈥揂尾(11鈥?7) leads to amorphous aggregates, whereas C₁₂鈥揂尾(11鈥?7)鈥揅₁₂ generates short rodlike fibrils. However, Fourier transform infrared spectroscopy suggests that the amorphous aggregates and rodlike fibrils display similar secondary structures. This work suggests that the aggregation ability and the aggregate structures of the peptide amphiphiles significantly affect their interactions with A尾(1鈥?0) and lead to different morphologies of the A尾(1鈥?0) aggregates.