Self-Assembling of Peptides Is Tuned via an Extended Amphipathic Helix
學年 102
學期 2
出版（發表）日期 2014-07-01
作品名稱 Self-Assembling of Peptides Is Tuned via an Extended Amphipathic Helix
作品名稱（其他語言）
著者 Lee, Chang-Shin; Lin, Chia-Hao; Hsieh, Wan-Lun; Chiao, Szu-Min; Tung, Wei-Cheng
單位 淡江大學化學學系
出版者 Valencia: American Scientific Publishers
著錄名稱、卷期、頁數 Journal of Nanoscience and Nanotechnology 14(7), pp.5568-5573
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.
關鍵字
語言 en_US
ISSN 1533-4880 1533-4899
期刊性質 國外
收錄於 SCI
產學合作
通訊作者
審稿制度 是
國別 USA
公開徵稿
出版型式 電子版 紙本
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