Self-Assembling of Peptides is Tuned via an Extended Amphipathic Helix
學年 105
學期 2
發表日期 2017-05-17
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 Chang-Shin Lee
作品所屬單位
出版者
會議名稱 The 22nd Biophysics Conference
會議地點 Kaohsiung, Taiwan
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 diffusion;intermolecular interaction;nanostructure;self-assembly;pulsed field gradient NMR
語言 en_US
收錄於
會議性質 國內
校內研討會地點 無
研討會時間 20170517~20170520
通訊作者
國別 TWN
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機構典藏連結 ( http://tkuir.lib.tku.edu.tw:8080/dspace/handle/987654321/116600 )

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