Self-Assembling of Peptides is Tuned via an Extended Amphipathic Helix

淡江大學機構典藏 > 理學院 > 化學學系暨研究所 > 會議論文 > Item 987654321/116600

jsp.display-item.identifier=請使用永久網址來引用或連結此文件: https://tkuir.lib.tku.edu.tw/dspace/handle/987654321/116600

题名:	Self-Assembling of Peptides is Tuned via an Extended Amphipathic Helix
作者:	Lee, Chang-Shin
关键词:	diffusion;intermolecular interaction;nanostructure;self-assembly;pulsed field gradient NMR
日期:	2018-05-17
上传时间:	2019-05-11 12:11:34 (UTC+8)
摘要:	Four peptides, C1 (spanning the helical segment of human neuropeptide Y from residue 15 to residue 29), C2 (spanning the helical segment of 21 to 31), C3 (the C-terminal fragment of neuropeptide Y involving residues 20 to 36) and P34-C3 (replacement of the glutamine with proline in position 34 of C3) were synthesized to study interaction between species. The information about the intermolecular interactions was extracted from their self-assembly behaviors. The results from CD and NMR showed that the addition of 2, 2, 2-trifluoroethanol (TFE) induces a stable amphipathic helix in each peptides and an extended helix was formed at the N-terminal of C1 and the C-terminal of C3. Pulsed field gradient NMR data revealed that C3 may undergo an enhanced interaction with TFE and a more favorable self-assembly as temperature was increased. In contrast, other three peptides were found to form larger size of oligomers at lower temperature and continuously dissociate into the monomeric form with increased temperature. Our results demonstrate that the self-assembly behavior may be tuned by the entropy and the energetics contributed by an extended helical conformation at terminus.
显示于类别:	[化學學系暨研究所] 會議論文

文件中的档案:

档案	大小	格式	浏览次数
index.html	0Kb	HTML	199	检视/开启

在機構典藏中所有的数据项都受到原著作权保护.

TAIR相关文章

数据加载中.....