教師資料查詢 | 類別: 期刊論文 | 教師: 李長欣 CHANG-SHIN LEE (瀏覽個人網頁)

標題:Characterization the Effects of Structure and Energetics of Intermolecular Interactions on the Oligomerization of Peptides in Aqueous 2, 2, 2-Trifluoroethanol via Circular Dichroism and Nuclear Magnetic Resonance Spectroscopy
學年100
學期2
出版(發表)日期2012/04/01
作品名稱Characterization the Effects of Structure and Energetics of Intermolecular Interactions on the Oligomerization of Peptides in Aqueous 2, 2, 2-Trifluoroethanol via Circular Dichroism and Nuclear Magnetic Resonance Spectroscopy
作品名稱(其他語言)
著者Lee, Chang-Shin; Tung, Wei-Cheng; Luo, Wan-Chi
單位淡江大學化學學系
出版者New York: Springer New York LLC
著錄名稱、卷期、頁數The Protein Journal 31(3), pp.222-228
摘要Intermolecular interactions are of fundamental importance to fully comprehend a wide range of protein behaviors such as oligomerization, folding and recognition. Two peptides, NPY [18-36] and NPY [15-29], segmented from human neuropeptide Y (hNPY), were synthesized in this work to study the interaction between species. Information about intermolecular interactions was extracted from their oligomerizing behaviors. The results from CD and NMR showed that the addition of 2, 2, 2-trifluoroeth-anol (TFE) induces a stable helix in each peptides and an extended helix in NPY [18-36], formed between residues 30-36. Pulsed field gradient NMR data revealed that NPY [15-29] forms a larger oligomer at lower temperatures and continuously dissociates into the monomeric form with increasing temperature. NPY [18-36] was also found to undergo an enhanced interaction with TFE and a more favorable self-association at higher temperatures. We characterized the changes of oligomerized states with respect to temperature to infer the effects of entropy and interaction energy on the association-dissociation equilibrium. As shown by NPY [15-29], deletion of helical secondary structure or residues from the C-terminal segment may disrupt the solvation by TFE and results in entropy increase as the oligomer dissociates. Unlike that in NPY [15-29], the extended helix in NPY [18-36] improves the binding of TFE, and as a result, entropy is gained via the transfer of the TFE cluster from the interface between monomeric peptides into the bulk solvent. This observation suggests that the oligomerized state may be modulated by the entropy and energetics contributed by helical segments in the oligomerization process.
關鍵字Diffusion; Intermolecular interaction; Neuropeptide; Oligomerization; Pulsed field gradient NMR
語言英文
ISSN1875-8355;1572-3887
期刊性質國外
收錄於SCI
產學合作
通訊作者Lee, Chang-Shin
審稿制度
國別美國
公開徵稿
出版型式紙本;電子版
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